NO318764B1 - Humant <beta><N>2</N>-integrin-alfa-subenhet - Google Patents
Humant <beta><N>2</N>-integrin-alfa-subenhet Download PDFInfo
- Publication number
- NO318764B1 NO318764B1 NO19974852A NO974852A NO318764B1 NO 318764 B1 NO318764 B1 NO 318764B1 NO 19974852 A NO19974852 A NO 19974852A NO 974852 A NO974852 A NO 974852A NO 318764 B1 NO318764 B1 NO 318764B1
- Authority
- NO
- Norway
- Prior art keywords
- cells
- human
- protein
- mouse
- expression
- Prior art date
Links
- 102000006495 integrins Human genes 0.000 title description 49
- 108010044426 integrins Proteins 0.000 title description 49
- 210000004408 hybridoma Anatomy 0.000 claims description 30
- MWUXSHHQAYIFBG-UHFFFAOYSA-N Nitric oxide Chemical compound O=[N] MWUXSHHQAYIFBG-UHFFFAOYSA-N 0.000 description 328
- 210000004027 cell Anatomy 0.000 description 249
- 102100025390 Integrin beta-2 Human genes 0.000 description 159
- 101000935040 Homo sapiens Integrin beta-2 Proteins 0.000 description 154
- 108090000623 proteins and genes Proteins 0.000 description 136
- 102000004169 proteins and genes Human genes 0.000 description 112
- 241000700159 Rattus Species 0.000 description 105
- 235000018102 proteins Nutrition 0.000 description 104
- 241000699666 Mus <mouse, genus> Species 0.000 description 102
- 230000014509 gene expression Effects 0.000 description 94
- 230000027455 binding Effects 0.000 description 91
- 210000002540 macrophage Anatomy 0.000 description 69
- 108020004414 DNA Proteins 0.000 description 68
- 239000013615 primer Substances 0.000 description 65
- 239000000872 buffer Substances 0.000 description 63
- 239000000523 sample Substances 0.000 description 61
- 239000002299 complementary DNA Substances 0.000 description 60
- 239000006228 supernatant Substances 0.000 description 59
- 241000283973 Oryctolagus cuniculus Species 0.000 description 56
- 210000001519 tissue Anatomy 0.000 description 53
- 210000000952 spleen Anatomy 0.000 description 52
- 238000003752 polymerase chain reaction Methods 0.000 description 47
- 239000012528 membrane Substances 0.000 description 46
- 239000012634 fragment Substances 0.000 description 45
- 210000004379 membrane Anatomy 0.000 description 43
- 238000010186 staining Methods 0.000 description 42
- 210000000265 leukocyte Anatomy 0.000 description 41
- 239000000243 solution Substances 0.000 description 40
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 39
- 101000599862 Homo sapiens Intercellular adhesion molecule 3 Proteins 0.000 description 38
- 102100037871 Intercellular adhesion molecule 3 Human genes 0.000 description 38
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 37
- 230000004927 fusion Effects 0.000 description 37
- 239000000047 product Substances 0.000 description 37
- 201000010099 disease Diseases 0.000 description 36
- 210000002966 serum Anatomy 0.000 description 36
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 35
- 108090000765 processed proteins & peptides Proteins 0.000 description 35
- 125000003275 alpha amino acid group Chemical group 0.000 description 34
- 239000003446 ligand Substances 0.000 description 34
- 239000006166 lysate Substances 0.000 description 33
- 102000004196 processed proteins & peptides Human genes 0.000 description 32
- 238000011534 incubation Methods 0.000 description 31
- 238000000034 method Methods 0.000 description 31
- 241000699670 Mus sp. Species 0.000 description 30
- 230000000875 corresponding effect Effects 0.000 description 29
- 238000009396 hybridization Methods 0.000 description 29
- 239000013612 plasmid Substances 0.000 description 29
- 229920001184 polypeptide Polymers 0.000 description 29
- 238000004458 analytical method Methods 0.000 description 27
- 241000282465 Canis Species 0.000 description 26
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 26
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 25
- 108020001507 fusion proteins Proteins 0.000 description 24
- 102000037865 fusion proteins Human genes 0.000 description 24
- 238000002347 injection Methods 0.000 description 24
- 239000007924 injection Substances 0.000 description 24
- 239000002773 nucleotide Substances 0.000 description 24
- 229940098773 bovine serum albumin Drugs 0.000 description 23
- 238000006243 chemical reaction Methods 0.000 description 23
- 230000003053 immunization Effects 0.000 description 23
- 238000002649 immunization Methods 0.000 description 23
- 238000002955 isolation Methods 0.000 description 23
- 125000003729 nucleotide group Chemical group 0.000 description 23
- 239000002953 phosphate buffered saline Substances 0.000 description 23
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 23
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 22
- 239000000427 antigen Substances 0.000 description 22
- 108091007433 antigens Proteins 0.000 description 22
- 102000036639 antigens Human genes 0.000 description 22
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 22
- 238000002965 ELISA Methods 0.000 description 21
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 21
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 21
- 238000005119 centrifugation Methods 0.000 description 21
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 21
- 101001046686 Homo sapiens Integrin alpha-M Proteins 0.000 description 20
- 102100022338 Integrin alpha-M Human genes 0.000 description 20
- 238000007792 addition Methods 0.000 description 20
- 239000003795 chemical substances by application Substances 0.000 description 20
- 150000001875 compounds Chemical class 0.000 description 20
- 238000009826 distribution Methods 0.000 description 20
- 210000004072 lung Anatomy 0.000 description 20
- PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 20
- 239000011780 sodium chloride Substances 0.000 description 20
- 238000011282 treatment Methods 0.000 description 20
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 19
- 238000010790 dilution Methods 0.000 description 19
- 239000012895 dilution Substances 0.000 description 19
- 239000003112 inhibitor Substances 0.000 description 19
- 230000009257 reactivity Effects 0.000 description 19
- 238000012216 screening Methods 0.000 description 19
- 238000012163 sequencing technique Methods 0.000 description 19
- 241000282472 Canis lupus familiaris Species 0.000 description 18
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 18
- 230000000903 blocking effect Effects 0.000 description 18
- 239000000833 heterodimer Substances 0.000 description 18
- 230000003902 lesion Effects 0.000 description 18
- 239000000463 material Substances 0.000 description 18
- 201000008752 progressive muscular atrophy Diseases 0.000 description 18
- 206010003210 Arteriosclerosis Diseases 0.000 description 17
- 108091028043 Nucleic acid sequence Proteins 0.000 description 17
- 208000011775 arteriosclerosis disease Diseases 0.000 description 17
- 238000011161 development Methods 0.000 description 17
- 230000018109 developmental process Effects 0.000 description 17
- 239000013613 expression plasmid Substances 0.000 description 17
- 238000001114 immunoprecipitation Methods 0.000 description 17
- 230000004054 inflammatory process Effects 0.000 description 17
- 239000013598 vector Substances 0.000 description 17
- 206010061218 Inflammation Diseases 0.000 description 16
- 238000004519 manufacturing process Methods 0.000 description 16
- 239000011347 resin Substances 0.000 description 16
- 229920005989 resin Polymers 0.000 description 16
- 241000283707 Capra Species 0.000 description 15
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 15
- 230000004913 activation Effects 0.000 description 15
- 238000000684 flow cytometry Methods 0.000 description 15
- 230000006870 function Effects 0.000 description 15
- 210000005259 peripheral blood Anatomy 0.000 description 15
- 239000011886 peripheral blood Substances 0.000 description 15
- 229920002684 Sepharose Polymers 0.000 description 14
- 108010000134 Vascular Cell Adhesion Molecule-1 Proteins 0.000 description 14
- 102100023543 Vascular cell adhesion protein 1 Human genes 0.000 description 14
- 235000001014 amino acid Nutrition 0.000 description 14
- 238000003556 assay Methods 0.000 description 14
- 230000006378 damage Effects 0.000 description 14
- 230000003993 interaction Effects 0.000 description 14
- 238000002372 labelling Methods 0.000 description 14
- 210000001616 monocyte Anatomy 0.000 description 14
- 238000012546 transfer Methods 0.000 description 14
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 13
- 102100022297 Integrin alpha-X Human genes 0.000 description 13
- 108091034117 Oligonucleotide Proteins 0.000 description 13
- 210000001744 T-lymphocyte Anatomy 0.000 description 13
- 150000001413 amino acids Chemical class 0.000 description 13
- 210000004369 blood Anatomy 0.000 description 13
- 239000008280 blood Substances 0.000 description 13
- 238000010367 cloning Methods 0.000 description 13
- 230000000694 effects Effects 0.000 description 13
- 239000000499 gel Substances 0.000 description 13
- 239000003550 marker Substances 0.000 description 13
- 239000008188 pellet Substances 0.000 description 13
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 12
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 12
- 210000003714 granulocyte Anatomy 0.000 description 12
- 210000004698 lymphocyte Anatomy 0.000 description 12
- 239000000203 mixture Substances 0.000 description 12
- 201000006417 multiple sclerosis Diseases 0.000 description 12
- 210000000440 neutrophil Anatomy 0.000 description 12
- 239000012591 Dulbecco’s Phosphate Buffered Saline Substances 0.000 description 11
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 11
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 11
- 239000002671 adjuvant Substances 0.000 description 11
- 239000011324 bead Substances 0.000 description 11
- 239000002158 endotoxin Substances 0.000 description 11
- 210000002216 heart Anatomy 0.000 description 11
- 229920006008 lipopolysaccharide Polymers 0.000 description 11
- 239000002609 medium Substances 0.000 description 11
- 229960004452 methionine Drugs 0.000 description 11
- 241000894007 species Species 0.000 description 11
- 210000004988 splenocyte Anatomy 0.000 description 11
- 108010059108 CD18 Antigens Proteins 0.000 description 10
- 108010078015 Complement C3b Proteins 0.000 description 10
- 101100019412 Homo sapiens ITGB2 gene Proteins 0.000 description 10
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 10
- 239000007983 Tris buffer Substances 0.000 description 10
- 238000013461 design Methods 0.000 description 10
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 10
- 229930182817 methionine Natural products 0.000 description 10
- 150000007523 nucleic acids Chemical class 0.000 description 10
- 230000007115 recruitment Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- 108091026890 Coding region Proteins 0.000 description 9
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 9
- 238000010171 animal model Methods 0.000 description 9
- 230000015572 biosynthetic process Effects 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 9
- 239000013604 expression vector Substances 0.000 description 9
- 230000002163 immunogen Effects 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 230000001225 therapeutic effect Effects 0.000 description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 8
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 8
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 8
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 8
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 8
- 206010003246 arthritis Diseases 0.000 description 8
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 8
- 238000010276 construction Methods 0.000 description 8
- 230000001086 cytosolic effect Effects 0.000 description 8
- 239000003599 detergent Substances 0.000 description 8
- 230000029087 digestion Effects 0.000 description 8
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 8
- 210000003979 eosinophil Anatomy 0.000 description 8
- 230000001965 increasing effect Effects 0.000 description 8
- 238000003780 insertion Methods 0.000 description 8
- 230000037431 insertion Effects 0.000 description 8
- 239000011777 magnesium Substances 0.000 description 8
- 102000040430 polynucleotide Human genes 0.000 description 8
- 108091033319 polynucleotide Proteins 0.000 description 8
- 239000002157 polynucleotide Substances 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 230000002441 reversible effect Effects 0.000 description 8
- 238000001890 transfection Methods 0.000 description 8
- 238000005406 washing Methods 0.000 description 8
- 108020004705 Codon Proteins 0.000 description 7
- 230000004568 DNA-binding Effects 0.000 description 7
- 241000282412 Homo Species 0.000 description 7
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 7
- 108060003951 Immunoglobulin Proteins 0.000 description 7
- 108010076504 Protein Sorting Signals Proteins 0.000 description 7
- 239000013504 Triton X-100 Substances 0.000 description 7
- 229920004890 Triton X-100 Polymers 0.000 description 7
- 210000001132 alveolar macrophage Anatomy 0.000 description 7
- 230000003321 amplification Effects 0.000 description 7
- 210000003719 b-lymphocyte Anatomy 0.000 description 7
- 229960003669 carbenicillin Drugs 0.000 description 7
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 7
- 239000006285 cell suspension Substances 0.000 description 7
- 239000012228 culture supernatant Substances 0.000 description 7
- 238000012217 deletion Methods 0.000 description 7
- 230000037430 deletion Effects 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 229910052739 hydrogen Inorganic materials 0.000 description 7
- 102000018358 immunoglobulin Human genes 0.000 description 7
- 210000004185 liver Anatomy 0.000 description 7
- 239000012139 lysis buffer Substances 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 238000003199 nucleic acid amplification method Methods 0.000 description 7
- 238000000159 protein binding assay Methods 0.000 description 7
- 230000002829 reductive effect Effects 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- QAPSNMNOIOSXSQ-YNEHKIRRSA-N 1-[(2r,4s,5r)-4-[tert-butyl(dimethyl)silyl]oxy-5-(hydroxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O[Si](C)(C)C(C)(C)C)C1 QAPSNMNOIOSXSQ-YNEHKIRRSA-N 0.000 description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 6
- 201000001320 Atherosclerosis Diseases 0.000 description 6
- 102000014914 Carrier Proteins Human genes 0.000 description 6
- 208000011231 Crohn disease Diseases 0.000 description 6
- 108010010803 Gelatin Proteins 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 239000000020 Nitrocellulose Substances 0.000 description 6
- 238000012408 PCR amplification Methods 0.000 description 6
- 102220469872 Protein argonaute-3_E37A_mutation Human genes 0.000 description 6
- 108700008625 Reporter Genes Proteins 0.000 description 6
- 108091023040 Transcription factor Proteins 0.000 description 6
- 102000040945 Transcription factor Human genes 0.000 description 6
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 6
- 238000013019 agitation Methods 0.000 description 6
- 239000012148 binding buffer Substances 0.000 description 6
- 108091008324 binding proteins Proteins 0.000 description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 6
- OXZOLXJZTSUDOM-UHFFFAOYSA-N fluoro 2,2,2-trifluoroacetate Chemical compound FOC(=O)C(F)(F)F OXZOLXJZTSUDOM-UHFFFAOYSA-N 0.000 description 6
- 239000008273 gelatin Substances 0.000 description 6
- 229920000159 gelatin Polymers 0.000 description 6
- 235000019322 gelatine Nutrition 0.000 description 6
- 235000011852 gelatine desserts Nutrition 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 230000002757 inflammatory effect Effects 0.000 description 6
- 230000028709 inflammatory response Effects 0.000 description 6
- 230000000977 initiatory effect Effects 0.000 description 6
- 238000011835 investigation Methods 0.000 description 6
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 6
- 229920001220 nitrocellulos Polymers 0.000 description 6
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 6
- 239000013641 positive control Substances 0.000 description 6
- 239000002002 slurry Substances 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 230000000638 stimulation Effects 0.000 description 6
- 210000001258 synovial membrane Anatomy 0.000 description 6
- 230000000451 tissue damage Effects 0.000 description 6
- 231100000827 tissue damage Toxicity 0.000 description 6
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 5
- 206010001889 Alveolitis Diseases 0.000 description 5
- 239000003155 DNA primer Substances 0.000 description 5
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 5
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 5
- 108090001005 Interleukin-6 Proteins 0.000 description 5
- 208000004852 Lung Injury Diseases 0.000 description 5
- 108010064548 Lymphocyte Function-Associated Antigen-1 Proteins 0.000 description 5
- 239000002033 PVDF binder Substances 0.000 description 5
- 206010069363 Traumatic lung injury Diseases 0.000 description 5
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 5
- 102100040247 Tumor necrosis factor Human genes 0.000 description 5
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 5
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 5
- 238000001261 affinity purification Methods 0.000 description 5
- 210000004204 blood vessel Anatomy 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 230000001684 chronic effect Effects 0.000 description 5
- 230000009089 cytolysis Effects 0.000 description 5
- 206010012601 diabetes mellitus Diseases 0.000 description 5
- 210000003743 erythrocyte Anatomy 0.000 description 5
- 201000001155 extrinsic allergic alveolitis Diseases 0.000 description 5
- 210000000497 foam cell Anatomy 0.000 description 5
- 230000006801 homologous recombination Effects 0.000 description 5
- 238000002744 homologous recombination Methods 0.000 description 5
- 208000022098 hypersensitivity pneumonitis Diseases 0.000 description 5
- 230000001900 immune effect Effects 0.000 description 5
- 230000028993 immune response Effects 0.000 description 5
- 210000004153 islets of langerhan Anatomy 0.000 description 5
- 231100000515 lung injury Toxicity 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 239000013642 negative control Substances 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 239000002245 particle Substances 0.000 description 5
- 230000035699 permeability Effects 0.000 description 5
- 102000013415 peroxidase activity proteins Human genes 0.000 description 5
- 108040007629 peroxidase activity proteins Proteins 0.000 description 5
- 229920002401 polyacrylamide Polymers 0.000 description 5
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- 238000002054 transplantation Methods 0.000 description 5
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 4
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 4
- 241000699800 Cricetinae Species 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 239000007995 HEPES buffer Substances 0.000 description 4
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 4
- 101710154606 Hemagglutinin Proteins 0.000 description 4
- 101000917858 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-A Proteins 0.000 description 4
- 101000917839 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-B Proteins 0.000 description 4
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 4
- 102000003960 Ligases Human genes 0.000 description 4
- 108090000364 Ligases Proteins 0.000 description 4
- 102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 4
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 4
- 239000004677 Nylon Substances 0.000 description 4
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 4
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 4
- 241000276498 Pollachius virens Species 0.000 description 4
- 229920001213 Polysorbate 20 Polymers 0.000 description 4
- 101710176177 Protein A56 Proteins 0.000 description 4
- 229920005654 Sephadex Polymers 0.000 description 4
- 239000012507 Sephadex™ Substances 0.000 description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 4
- 238000009825 accumulation Methods 0.000 description 4
- 230000002378 acidificating effect Effects 0.000 description 4
- 230000001154 acute effect Effects 0.000 description 4
- 239000011543 agarose gel Substances 0.000 description 4
- 238000000137 annealing Methods 0.000 description 4
- 230000003143 atherosclerotic effect Effects 0.000 description 4
- 210000003651 basophil Anatomy 0.000 description 4
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 4
- 230000021164 cell adhesion Effects 0.000 description 4
- 239000013592 cell lysate Substances 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 235000012000 cholesterol Nutrition 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 239000012133 immunoprecipitate Substances 0.000 description 4
- 238000007901 in situ hybridization Methods 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 239000002198 insoluble material Substances 0.000 description 4
- 210000003734 kidney Anatomy 0.000 description 4
- 229910052749 magnesium Inorganic materials 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
- 210000000822 natural killer cell Anatomy 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- 229920001778 nylon Polymers 0.000 description 4
- 230000036961 partial effect Effects 0.000 description 4
- 230000001575 pathological effect Effects 0.000 description 4
- 230000002093 peripheral effect Effects 0.000 description 4
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 4
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 4
- -1 polypropylene Polymers 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 239000011541 reaction mixture Substances 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 210000003491 skin Anatomy 0.000 description 4
- 229910052708 sodium Inorganic materials 0.000 description 4
- 239000011734 sodium Substances 0.000 description 4
- DAEPDZWVDSPTHF-UHFFFAOYSA-M sodium pyruvate Chemical compound [Na+].CC(=O)C([O-])=O DAEPDZWVDSPTHF-UHFFFAOYSA-M 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 229940104230 thymidine Drugs 0.000 description 4
- 210000001541 thymus gland Anatomy 0.000 description 4
- 230000003827 upregulation Effects 0.000 description 4
- 239000011534 wash buffer Substances 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 3
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 3
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 3
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 3
- 229920002307 Dextran Polymers 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 206010018691 Granuloma Diseases 0.000 description 3
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 3
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 3
- 102100037872 Intercellular adhesion molecule 2 Human genes 0.000 description 3
- 101710148794 Intercellular adhesion molecule 2 Proteins 0.000 description 3
- 102100037850 Interferon gamma Human genes 0.000 description 3
- 108010074328 Interferon-gamma Proteins 0.000 description 3
- 108010002616 Interleukin-5 Proteins 0.000 description 3
- 239000012741 Laemmli sample buffer Substances 0.000 description 3
- 201000001779 Leukocyte adhesion deficiency Diseases 0.000 description 3
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 3
- 102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 3
- 108010021466 Mutant Proteins Proteins 0.000 description 3
- 102000008300 Mutant Proteins Human genes 0.000 description 3
- 102000005717 Myeloma Proteins Human genes 0.000 description 3
- 108010045503 Myeloma Proteins Proteins 0.000 description 3
- 101100028920 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cfp gene Proteins 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 229930040373 Paraformaldehyde Natural products 0.000 description 3
- 101150003085 Pdcl gene Proteins 0.000 description 3
- 206010057249 Phagocytosis Diseases 0.000 description 3
- 108091000080 Phosphotransferase Proteins 0.000 description 3
- 206010035664 Pneumonia Diseases 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 108010022394 Threonine synthase Proteins 0.000 description 3
- 108020004440 Thymidine kinase Proteins 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 229960005305 adenosine Drugs 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 230000002917 arthritic effect Effects 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 208000037976 chronic inflammation Diseases 0.000 description 3
- 230000006020 chronic inflammation Effects 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 239000002131 composite material Substances 0.000 description 3
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 3
- 229960002086 dextran Drugs 0.000 description 3
- 235000005911 diet Nutrition 0.000 description 3
- 230000037213 diet Effects 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 102000004419 dihydrofolate reductase Human genes 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 238000001378 electrochemiluminescence detection Methods 0.000 description 3
- 210000000981 epithelium Anatomy 0.000 description 3
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 3
- 229960005542 ethidium bromide Drugs 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 210000003630 histaminocyte Anatomy 0.000 description 3
- 238000007654 immersion Methods 0.000 description 3
- 230000008595 infiltration Effects 0.000 description 3
- 238000001764 infiltration Methods 0.000 description 3
- 210000004969 inflammatory cell Anatomy 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 208000014674 injury Diseases 0.000 description 3
- 102000017777 integrin alpha chain Human genes 0.000 description 3
- 239000007928 intraperitoneal injection Substances 0.000 description 3
- 108010052968 leupeptin Proteins 0.000 description 3
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 3
- 230000002025 microglial effect Effects 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 229920002866 paraformaldehyde Polymers 0.000 description 3
- 230000037361 pathway Effects 0.000 description 3
- 108010091212 pepstatin Proteins 0.000 description 3
- 229950000964 pepstatin Drugs 0.000 description 3
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 3
- 230000008782 phagocytosis Effects 0.000 description 3
- 102000020233 phosphotransferase Human genes 0.000 description 3
- 229920002704 polyhistidine Polymers 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 238000011552 rat model Methods 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 210000001533 respiratory mucosa Anatomy 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 210000004989 spleen cell Anatomy 0.000 description 3
- 230000003393 splenic effect Effects 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 239000011550 stock solution Substances 0.000 description 3
- 231100000331 toxic Toxicity 0.000 description 3
- 230000002588 toxic effect Effects 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 3
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 2
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 2
- DVLFYONBTKHTER-UHFFFAOYSA-N 3-(N-morpholino)propanesulfonic acid Chemical compound OS(=O)(=O)CCCN1CCOCC1 DVLFYONBTKHTER-UHFFFAOYSA-N 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 2
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 2
- 241000585703 Adelphia <angiosperm> Species 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 2
- 208000002109 Argyria Diseases 0.000 description 2
- 208000032116 Autoimmune Experimental Encephalomyelitis Diseases 0.000 description 2
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 2
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 2
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 2
- 102000001327 Chemokine CCL5 Human genes 0.000 description 2
- 108010055166 Chemokine CCL5 Proteins 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 241000699679 Cricetulus migratorius Species 0.000 description 2
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 101150099632 Dd gene Proteins 0.000 description 2
- 206010014824 Endotoxic shock Diseases 0.000 description 2
- 229920001917 Ficoll Polymers 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 101000581981 Homo sapiens Neural cell adhesion molecule 1 Proteins 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 102000003839 Human Proteins Human genes 0.000 description 2
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 108010058683 Immobilized Proteins Proteins 0.000 description 2
- 108060004056 Integrin alpha Chain Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 206010023203 Joint destruction Diseases 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- 229930182816 L-glutamine Natural products 0.000 description 2
- 108010007622 LDL Lipoproteins Proteins 0.000 description 2
- 102000007330 LDL Lipoproteins Human genes 0.000 description 2
- 102000043131 MHC class II family Human genes 0.000 description 2
- 108091054438 MHC class II family Proteins 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 241000252067 Megalops atlanticus Species 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 101100341513 Mus musculus Itgam gene Proteins 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 102100027347 Neural cell adhesion molecule 1 Human genes 0.000 description 2
- 206010030113 Oedema Diseases 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 229920002535 Polyethylene Glycol 1500 Polymers 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- 239000012722 SDS sample buffer Substances 0.000 description 2
- 206010040070 Septic Shock Diseases 0.000 description 2
- 108050007496 Shikimate kinase 2 Proteins 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 101710136739 Teichoic acid poly(glycerol phosphate) polymerase Proteins 0.000 description 2
- 102000006601 Thymidine Kinase Human genes 0.000 description 2
- 108700029229 Transcriptional Regulatory Elements Proteins 0.000 description 2
- 230000003187 abdominal effect Effects 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 208000038016 acute inflammation Diseases 0.000 description 2
- 230000006022 acute inflammation Effects 0.000 description 2
- 206010069351 acute lung injury Diseases 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 229960003896 aminopterin Drugs 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 229960004405 aprotinin Drugs 0.000 description 2
- 230000004872 arterial blood pressure Effects 0.000 description 2
- 208000006673 asthma Diseases 0.000 description 2
- 238000007846 asymmetric PCR Methods 0.000 description 2
- 230000000923 atherogenic effect Effects 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 238000010364 biochemical engineering Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 239000002981 blocking agent Substances 0.000 description 2
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 2
- 210000000621 bronchi Anatomy 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 229910002091 carbon monoxide Inorganic materials 0.000 description 2
- 230000000747 cardiac effect Effects 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000020411 cell activation Effects 0.000 description 2
- 229960003677 chloroquine Drugs 0.000 description 2
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 2
- 230000024203 complement activation Effects 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 229960004397 cyclophosphamide Drugs 0.000 description 2
- 210000005220 cytoplasmic tail Anatomy 0.000 description 2
- 230000034994 death Effects 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- FFYPMLJYZAEMQB-UHFFFAOYSA-N diethyl pyrocarbonate Chemical compound CCOC(=O)OC(=O)OCC FFYPMLJYZAEMQB-UHFFFAOYSA-N 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 201000002491 encephalomyelitis Diseases 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 235000019688 fish Nutrition 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 235000019253 formic acid Nutrition 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 210000004907 gland Anatomy 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 239000000185 hemagglutinin Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 230000003100 immobilizing effect Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000000099 in vitro assay Methods 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 210000000936 intestine Anatomy 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 239000002085 irritant Substances 0.000 description 2
- 231100000021 irritant Toxicity 0.000 description 2
- 210000001503 joint Anatomy 0.000 description 2
- 230000002147 killing effect Effects 0.000 description 2
- 238000011694 lewis rat Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 210000002751 lymph Anatomy 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 239000011325 microbead Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 125000001446 muramyl group Chemical group N[C@@H](C=O)[C@@H](O[C@@H](C(=O)*)C)[C@H](O)[C@H](O)CO 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 108091027963 non-coding RNA Proteins 0.000 description 2
- 102000042567 non-coding RNA Human genes 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 108010071584 oxidized low density lipoprotein Proteins 0.000 description 2
- 230000008506 pathogenesis Effects 0.000 description 2
- 230000007170 pathology Effects 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 239000000825 pharmaceutical preparation Substances 0.000 description 2
- 239000002644 phorbol ester Substances 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000009465 prokaryotic expression Effects 0.000 description 2
- 230000000644 propagated effect Effects 0.000 description 2
- 238000011555 rabbit model Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 238000010079 rubber tapping Methods 0.000 description 2
- 238000007423 screening assay Methods 0.000 description 2
- 210000002460 smooth muscle Anatomy 0.000 description 2
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 2
- 229940054269 sodium pyruvate Drugs 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 238000003153 stable transfection Methods 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 210000005222 synovial tissue Anatomy 0.000 description 2
- 210000002437 synoviocyte Anatomy 0.000 description 2
- 201000004595 synovitis Diseases 0.000 description 2
- VUYXVWGKCKTUMF-UHFFFAOYSA-N tetratriacontaethylene glycol monomethyl ether Chemical compound COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO VUYXVWGKCKTUMF-UHFFFAOYSA-N 0.000 description 2
- 230000008719 thickening Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000010474 transient expression Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000001960 triggered effect Effects 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 238000012800 visualization Methods 0.000 description 2
- 210000004885 white matter Anatomy 0.000 description 2
- YMXHPSHLTSZXKH-RVBZMBCESA-N (2,5-dioxopyrrolidin-1-yl) 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoate Chemical compound C([C@H]1[C@H]2NC(=O)N[C@H]2CS1)CCCC(=O)ON1C(=O)CCC1=O YMXHPSHLTSZXKH-RVBZMBCESA-N 0.000 description 1
- LYUGPLUDRALHKJ-UHFFFAOYSA-N 1-(cyclohexylamino)propane-1-sulfonic acid Chemical compound CCC(S(O)(=O)=O)NC1CCCCC1 LYUGPLUDRALHKJ-UHFFFAOYSA-N 0.000 description 1
- NHJVRSWLHSJWIN-UHFFFAOYSA-N 2,4,6-trinitrobenzenesulfonic acid Chemical compound OS(=O)(=O)C1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O NHJVRSWLHSJWIN-UHFFFAOYSA-N 0.000 description 1
- AXAVXPMQTGXXJZ-UHFFFAOYSA-N 2-aminoacetic acid;2-amino-2-(hydroxymethyl)propane-1,3-diol Chemical compound NCC(O)=O.OCC(N)(CO)CO AXAVXPMQTGXXJZ-UHFFFAOYSA-N 0.000 description 1
- LHYQAEFVHIZFLR-UHFFFAOYSA-L 4-(4-diazonio-3-methoxyphenyl)-2-methoxybenzenediazonium;dichloride Chemical compound [Cl-].[Cl-].C1=C([N+]#N)C(OC)=CC(C=2C=C(OC)C([N+]#N)=CC=2)=C1 LHYQAEFVHIZFLR-UHFFFAOYSA-L 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 description 1
- DLQPMEMYCIGJIM-UHFFFAOYSA-N Adjuvant peptide Natural products CC(NC(=O)CCOC1C(O)C(CO)OC(O)C1NC(=O)C)C(=O)NC(CCC(=O)O)C(=O)N DLQPMEMYCIGJIM-UHFFFAOYSA-N 0.000 description 1
- 208000031873 Animal Disease Models Diseases 0.000 description 1
- 206010003497 Asphyxia Diseases 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101100289995 Caenorhabditis elegans mac-1 gene Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- 206010007558 Cardiac failure chronic Diseases 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 208000003322 Coinfection Diseases 0.000 description 1
- 206010009900 Colitis ulcerative Diseases 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 208000014997 Crohn colitis Diseases 0.000 description 1
- 229930105110 Cyclosporin A Natural products 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 102000004860 Dipeptidases Human genes 0.000 description 1
- 108090001081 Dipeptidases Proteins 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- 206010014561 Emphysema Diseases 0.000 description 1
- 241000709661 Enterovirus Species 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- 108010001515 Galectin 4 Proteins 0.000 description 1
- 102100039556 Galectin-4 Human genes 0.000 description 1
- 206010018364 Glomerulonephritis Diseases 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 102100036242 HLA class II histocompatibility antigen, DQ alpha 2 chain Human genes 0.000 description 1
- 108010017480 Hemosiderin Proteins 0.000 description 1
- 241001622557 Hesperia Species 0.000 description 1
- 101000930801 Homo sapiens HLA class II histocompatibility antigen, DQ alpha 2 chain Proteins 0.000 description 1
- 102000039966 ICAM family Human genes 0.000 description 1
- 108091069108 ICAM family Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102100025323 Integrin alpha-1 Human genes 0.000 description 1
- 108010041341 Integrin alpha1 Proteins 0.000 description 1
- 108010055795 Integrin alpha1beta1 Proteins 0.000 description 1
- 108010017642 Integrin alpha2beta1 Proteins 0.000 description 1
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 1
- 108010064600 Intercellular Adhesion Molecule-3 Proteins 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102000043129 MHC class I family Human genes 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 239000012901 Milli-Q water Substances 0.000 description 1
- 108090000143 Mouse Proteins Proteins 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- 241001045988 Neogene Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- IOVCWXUNBOPUCH-UHFFFAOYSA-M Nitrite anion Chemical compound [O-]N=O IOVCWXUNBOPUCH-UHFFFAOYSA-M 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 241000609499 Palicourea Species 0.000 description 1
- 108091081548 Palindromic sequence Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 108010001267 Protein Subunits Proteins 0.000 description 1
- 102000002067 Protein Subunits Human genes 0.000 description 1
- 201000004681 Psoriasis Diseases 0.000 description 1
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241001222774 Salmonella enterica subsp. enterica serovar Minnesota Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 230000006043 T cell recruitment Effects 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 206010060872 Transplant failure Diseases 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 201000006704 Ulcerative Colitis Diseases 0.000 description 1
- 206010072810 Vascular wall hypertrophy Diseases 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 230000009102 absorption Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 208000009956 adenocarcinoma Diseases 0.000 description 1
- 201000000028 adult respiratory distress syndrome Diseases 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000011316 allogeneic transplantation Methods 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 208000007502 anemia Diseases 0.000 description 1
- 238000011558 animal model by disease Methods 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 230000006472 autoimmune response Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000002902 bimodal effect Effects 0.000 description 1
- 230000002051 biphasic effect Effects 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 230000000981 bystander Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000010805 cDNA synthesis kit Methods 0.000 description 1
- DEGAKNSWVGKMLS-UHFFFAOYSA-N calcein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC(CN(CC(O)=O)CC(O)=O)=C(O)C=C1OC1=C2C=C(CN(CC(O)=O)CC(=O)O)C(O)=C1 DEGAKNSWVGKMLS-UHFFFAOYSA-N 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 235000011089 carbon dioxide Nutrition 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000023402 cell communication Effects 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 208000037887 cell injury Diseases 0.000 description 1
- 239000002771 cell marker Substances 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 230000030570 cellular localization Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000035605 chemotaxis Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000012539 chromatography resin Substances 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 208000035850 clinical syndrome Diseases 0.000 description 1
- 238000000749 co-immunoprecipitation Methods 0.000 description 1
- 206010009887 colitis Diseases 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 230000000112 colonic effect Effects 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 210000004351 coronary vessel Anatomy 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000018044 dehydration Effects 0.000 description 1
- 238000006297 dehydration reaction Methods 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 230000023077 detection of light stimulus Effects 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- OZRNSSUDZOLUSN-LBPRGKRZSA-N dihydrofolic acid Chemical compound N=1C=2C(=O)NC(N)=NC=2NCC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OZRNSSUDZOLUSN-LBPRGKRZSA-N 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 210000004921 distal colon Anatomy 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002257 embryonic structure Anatomy 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 108010030074 endodeoxyribonuclease MluI Proteins 0.000 description 1
- 210000003038 endothelium Anatomy 0.000 description 1
- 210000003989 endothelium vascular Anatomy 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 208000012997 experimental autoimmune encephalomyelitis Diseases 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 230000003176 fibrotic effect Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 210000000285 follicular dendritic cell Anatomy 0.000 description 1
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 201000007192 granulomatous hepatitis Diseases 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 210000003547 hepatic macrophage Anatomy 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 206010020718 hyperplasia Diseases 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000002991 immunohistochemical analysis Methods 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000011532 immunohistochemical staining Methods 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000003960 inflammatory cascade Effects 0.000 description 1
- 238000011850 initial investigation Methods 0.000 description 1
- 102000017776 integrin beta chain Human genes 0.000 description 1
- 108060004057 integrin beta chain Proteins 0.000 description 1
- 230000008611 intercellular interaction Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 230000010189 intracellular transport Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 208000018937 joint inflammation Diseases 0.000 description 1
- 230000000366 juvenile effect Effects 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 230000023404 leukocyte cell-cell adhesion Effects 0.000 description 1
- 238000000670 ligand binding assay Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 231100000516 lung damage Toxicity 0.000 description 1
- 210000001365 lymphatic vessel Anatomy 0.000 description 1
- 210000003563 lymphoid tissue Anatomy 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- MIKKOBKEXMRYFQ-WZTVWXICSA-N meglumine amidotrizoate Chemical compound C[NH2+]C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO.CC(=O)NC1=C(I)C(NC(C)=O)=C(I)C(C([O-])=O)=C1I MIKKOBKEXMRYFQ-WZTVWXICSA-N 0.000 description 1
- 210000003071 memory t lymphocyte Anatomy 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 210000002864 mononuclear phagocyte Anatomy 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 230000009854 mucosal lesion Effects 0.000 description 1
- BSOQXXWZTUDTEL-QAQREVAFSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-QAQREVAFSA-N 0.000 description 1
- 101150091879 neo gene Proteins 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- VIKNJXKGJWUCNN-XGXHKTLJSA-N norethisterone Chemical compound O=C1CC[C@@H]2[C@H]3CC[C@](C)([C@](CC4)(O)C#C)[C@@H]4[C@@H]3CCC2=C1 VIKNJXKGJWUCNN-XGXHKTLJSA-N 0.000 description 1
- 230000001473 noxious effect Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 229960002378 oftasceine Drugs 0.000 description 1
- 210000004248 oligodendroglia Anatomy 0.000 description 1
- 230000003349 osteoarthritic effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 230000000242 pagocytic effect Effects 0.000 description 1
- 210000002741 palatine tonsil Anatomy 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- NTGBUUXKGAZMSE-UHFFFAOYSA-N phenyl n-[4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]carbamate Chemical compound C1=CC(OC)=CC=C1N1CCN(C=2C=CC(NC(=O)OC=3C=CC=CC=3)=CC=2)CC1 NTGBUUXKGAZMSE-UHFFFAOYSA-N 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 230000007505 plaque formation Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 210000003281 pleural cavity Anatomy 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000023603 positive regulation of transcription initiation, DNA-dependent Effects 0.000 description 1
- 230000000270 postfertilization Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 238000011045 prefiltration Methods 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 230000007425 progressive decline Effects 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- INCIMLINXXICKS-UHFFFAOYSA-M pyronin Y Chemical compound [Cl-].C1=CC(=[N+](C)C)C=C2OC3=CC(N(C)C)=CC=C3C=C21 INCIMLINXXICKS-UHFFFAOYSA-M 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 239000000700 radioactive tracer Substances 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000011808 rodent model Methods 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 238000002821 scintillation proximity assay Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000007493 shaping process Methods 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 230000009131 signaling function Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- FRGKKTITADJNOE-UHFFFAOYSA-N sulfanyloxyethane Chemical compound CCOS FRGKKTITADJNOE-UHFFFAOYSA-N 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000017960 syncytium formation Effects 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 210000000115 thoracic cavity Anatomy 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 210000003437 trachea Anatomy 0.000 description 1
- 238000012301 transgenic model Methods 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000008728 vascular permeability Effects 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 235000008979 vitamin B4 Nutrition 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70546—Integrin superfamily
- C07K14/70553—Integrin beta2-subunit-containing molecules, e.g. CD11, CD18
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
- C07K16/2845—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily against integrin beta2-subunit-containing molecules, e.g. CD11, CD18
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6813—Hybridisation assays
- C12Q1/6816—Hybridisation assays characterised by the detection means
- C12Q1/6818—Hybridisation assays characterised by the detection means involving interaction of two or more labels, e.g. resonant energy transfer
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/04—Endocrine or metabolic disorders
- G01N2800/042—Disorders of carbohydrate metabolism, e.g. diabetes, glucose metabolism
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Cell Biology (AREA)
- Toxicology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US08/605,672 US5817515A (en) | 1993-12-23 | 1996-02-22 | Human B2 integrin alpha subunit antibodies |
PCT/US1997/002713 WO1997031099A1 (en) | 1996-02-22 | 1997-02-24 | Human beta 2 integrin alpha subunit |
Publications (3)
Publication Number | Publication Date |
---|---|
NO974852D0 NO974852D0 (no) | 1997-10-21 |
NO974852L NO974852L (no) | 1997-12-19 |
NO318764B1 true NO318764B1 (no) | 2005-05-02 |
Family
ID=24424704
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19974852A NO318764B1 (no) | 1996-02-22 | 1997-10-21 | Humant <beta><N>2</N>-integrin-alfa-subenhet |
Country Status (18)
Country | Link |
---|---|
US (1) | US5817515A (hu) |
EP (1) | EP0835301B1 (hu) |
JP (1) | JP2001526524A (hu) |
CN (1) | CN1103812C (hu) |
AT (1) | ATE293685T1 (hu) |
AU (1) | AU723110B2 (hu) |
BR (1) | BR9702101A (hu) |
CA (1) | CA2218755C (hu) |
CZ (1) | CZ287921B6 (hu) |
DE (1) | DE69733051D1 (hu) |
FI (1) | FI974018A (hu) |
HU (1) | HU223977B1 (hu) |
IL (1) | IL122011A (hu) |
NO (1) | NO318764B1 (hu) |
PL (1) | PL187013B1 (hu) |
RU (1) | RU2183671C2 (hu) |
SK (1) | SK283135B6 (hu) |
WO (1) | WO1997031099A1 (hu) |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5837478A (en) * | 1993-12-23 | 1998-11-17 | Icos Corporation | Method of identifying modulators of binding between and VCAM-1 |
US6620915B2 (en) * | 1993-12-23 | 2003-09-16 | Icos Corporation | Monoclonal antibodies specific for integrin α-d subunit |
US20030055231A1 (en) * | 1998-10-28 | 2003-03-20 | Jian Ni | 12 human secreted proteins |
JP2003527439A (ja) | 2000-03-17 | 2003-09-16 | ミレニアム・ファーマシューティカルズ・インコーポレイテッド | 抗cd18抗体と抗ccr2抗体の混合物を用いる狭窄および再狭窄を抑制する方法 |
WO2023235971A1 (en) * | 2022-06-08 | 2023-12-14 | The Regents Of The University Of California | Antibodies and immunotherapies that target the active conformation of integrin beta 2 |
Family Cites Families (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4271139A (en) * | 1978-03-27 | 1981-06-02 | Hiram Hart | Scintillation proximity assay |
US4568649A (en) * | 1983-02-22 | 1986-02-04 | Immunex Corporation | Immediate ligand detection assay |
WO1992006697A1 (en) * | 1990-10-23 | 1992-04-30 | Repligen Corporation | Anti-inflammatory composition |
CA2120500A1 (en) * | 1991-10-01 | 1993-04-15 | Mitsuaki Isobe | Preventing allograft rejection with antibodies to adhesion molecules |
DE69229275T2 (de) * | 1991-10-04 | 1999-12-30 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, Rockville | Herstellung eines arzneimittels zur behandlung von augenentzündung durch blockierung von zelladhäsionsmolekulen |
US5470953A (en) * | 1993-12-23 | 1995-11-28 | Icos Corporation | Human β2 integrin α subunit |
WO1995027736A1 (en) * | 1994-04-12 | 1995-10-19 | Boehringer Ingelheim Pharmaceuticals, Inc. | Use of agents which block intercellular adhesion molecule/receptor interaction in the treatment of respiratory viral infection |
-
1996
- 1996-02-22 US US08/605,672 patent/US5817515A/en not_active Expired - Fee Related
-
1997
- 1997-02-24 RU RU97119175/13A patent/RU2183671C2/ru not_active IP Right Cessation
- 1997-02-24 JP JP53033797A patent/JP2001526524A/ja active Pending
- 1997-02-24 PL PL97323195A patent/PL187013B1/pl not_active IP Right Cessation
- 1997-02-24 CA CA002218755A patent/CA2218755C/en not_active Expired - Fee Related
- 1997-02-24 AU AU21333/97A patent/AU723110B2/en not_active Ceased
- 1997-02-24 SK SK1409-97A patent/SK283135B6/sk unknown
- 1997-02-24 AT AT97906713T patent/ATE293685T1/de not_active IP Right Cessation
- 1997-02-24 DE DE69733051T patent/DE69733051D1/de not_active Expired - Lifetime
- 1997-02-24 CN CN97190406A patent/CN1103812C/zh not_active Expired - Fee Related
- 1997-02-24 BR BR9702101A patent/BR9702101A/pt not_active IP Right Cessation
- 1997-02-24 CZ CZ19973286A patent/CZ287921B6/cs not_active IP Right Cessation
- 1997-02-24 WO PCT/US1997/002713 patent/WO1997031099A1/en active IP Right Grant
- 1997-02-24 IL IL12201197A patent/IL122011A/en not_active IP Right Cessation
- 1997-02-24 EP EP97906713A patent/EP0835301B1/en not_active Expired - Lifetime
- 1997-02-24 HU HU9901579A patent/HU223977B1/hu not_active IP Right Cessation
- 1997-10-21 FI FI974018A patent/FI974018A/fi unknown
- 1997-10-21 NO NO19974852A patent/NO318764B1/no unknown
Also Published As
Publication number | Publication date |
---|---|
SK283135B6 (sk) | 2003-03-04 |
CA2218755A1 (en) | 1997-08-28 |
EP0835301A1 (en) | 1998-04-15 |
BR9702101A (pt) | 1999-07-20 |
IL122011A0 (en) | 1998-03-10 |
FI974018A (fi) | 1997-12-03 |
HUP9901579A3 (en) | 2001-10-29 |
AU2133397A (en) | 1997-09-10 |
PL187013B1 (pl) | 2004-04-30 |
US5817515A (en) | 1998-10-06 |
HU223977B1 (hu) | 2005-03-29 |
SK140997A3 (en) | 1998-09-09 |
NO974852L (no) | 1997-12-19 |
CN1189851A (zh) | 1998-08-05 |
CA2218755C (en) | 1999-08-31 |
HUP9901579A2 (hu) | 1999-08-30 |
CZ328697A3 (cs) | 1998-07-15 |
DE69733051D1 (de) | 2005-05-25 |
RU2183671C2 (ru) | 2002-06-20 |
NO974852D0 (no) | 1997-10-21 |
CZ287921B6 (cs) | 2001-03-14 |
WO1997031099A1 (en) | 1997-08-28 |
PL323195A1 (en) | 1998-03-16 |
IL122011A (en) | 2001-05-20 |
CN1103812C (zh) | 2003-03-26 |
FI974018A0 (fi) | 1997-10-21 |
ATE293685T1 (de) | 2005-05-15 |
JP2001526524A (ja) | 2001-12-18 |
AU723110B2 (en) | 2000-08-17 |
EP0835301B1 (en) | 2005-04-20 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
AU2001296839B2 (en) | Use of anti-human integrin alpha D antibodies to treat spinal cord injury | |
JP3261383B2 (ja) | 新規ヒトβ2インテグリンアルファサブユニット | |
US5837478A (en) | Method of identifying modulators of binding between and VCAM-1 | |
US20060280739A1 (en) | Novel human beta-2 integrin alpha subunit | |
AU2001296839A1 (en) | Use of anti-human integrin alpha D antibodies to treat spinal cord injury | |
AU775300B2 (en) | Method for inhibiting macrophage infiltration using monoclonal anti-alpha-d-antibodies | |
NO318764B1 (no) | Humant <beta><N>2</N>-integrin-alfa-subenhet | |
US5728533A (en) | Human β2 integrin αsubunit | |
US5831029A (en) | Human β2 integrin α subunit | |
EP2182008A2 (en) | Monoclonal anti alpha-D (ITGAD) antibodies for use in the treatment of inflammation | |
Gallatin et al. | Human beta2 integrin alpha subunit |