ES2763433T3 - Aplicación de laminina a cultivos de células endoteliales de la córnea - Google Patents
Aplicación de laminina a cultivos de células endoteliales de la córnea Download PDFInfo
- Publication number
- ES2763433T3 ES2763433T3 ES14831100T ES14831100T ES2763433T3 ES 2763433 T3 ES2763433 T3 ES 2763433T3 ES 14831100 T ES14831100 T ES 14831100T ES 14831100 T ES14831100 T ES 14831100T ES 2763433 T3 ES2763433 T3 ES 2763433T3
- Authority
- ES
- Spain
- Prior art keywords
- laminin
- chain
- seq
- corneal endothelial
- cell
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 210000000399 corneal endothelial cell Anatomy 0.000 title claims abstract description 135
- 238000004113 cell culture Methods 0.000 title description 15
- 108010085895 Laminin Proteins 0.000 claims abstract description 293
- 239000012634 fragment Substances 0.000 claims abstract description 118
- 238000000034 method Methods 0.000 claims abstract description 82
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 55
- 108010038862 laminin 10 Proteins 0.000 claims abstract description 49
- 230000001737 promoting effect Effects 0.000 claims abstract description 14
- 238000000338 in vitro Methods 0.000 claims abstract description 3
- 210000004087 cornea Anatomy 0.000 claims description 50
- 210000002889 endothelial cell Anatomy 0.000 claims description 38
- 230000012010 growth Effects 0.000 claims description 29
- 230000001413 cellular effect Effects 0.000 claims description 5
- 230000010261 cell growth Effects 0.000 abstract description 11
- 102000007547 Laminin Human genes 0.000 description 286
- 210000004027 cell Anatomy 0.000 description 120
- 108090000623 proteins and genes Proteins 0.000 description 109
- 102000006495 integrins Human genes 0.000 description 102
- 108010044426 integrins Proteins 0.000 description 102
- 108090000765 processed proteins & peptides Proteins 0.000 description 84
- 102000004169 proteins and genes Human genes 0.000 description 81
- 235000018102 proteins Nutrition 0.000 description 79
- 229920001184 polypeptide Polymers 0.000 description 75
- 102000004196 processed proteins & peptides Human genes 0.000 description 75
- 239000000203 mixture Substances 0.000 description 61
- 102000040430 polynucleotide Human genes 0.000 description 59
- 108091033319 polynucleotide Proteins 0.000 description 59
- 239000002157 polynucleotide Substances 0.000 description 59
- 150000007523 nucleic acids Chemical class 0.000 description 56
- 125000003275 alpha amino acid group Chemical group 0.000 description 50
- 102000039446 nucleic acids Human genes 0.000 description 48
- 108020004707 nucleic acids Proteins 0.000 description 48
- 239000011248 coating agent Substances 0.000 description 35
- 235000001014 amino acid Nutrition 0.000 description 33
- 229940024606 amino acid Drugs 0.000 description 33
- 150000001413 amino acids Chemical class 0.000 description 33
- 238000000576 coating method Methods 0.000 description 33
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 32
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 32
- 239000002609 medium Substances 0.000 description 32
- 230000004071 biological effect Effects 0.000 description 31
- 210000000871 endothelium corneal Anatomy 0.000 description 31
- 230000021164 cell adhesion Effects 0.000 description 28
- 230000000694 effects Effects 0.000 description 28
- 238000012258 culturing Methods 0.000 description 27
- 108091034117 Oligonucleotide Proteins 0.000 description 26
- 238000009472 formulation Methods 0.000 description 26
- 239000010410 layer Substances 0.000 description 26
- 210000002744 extracellular matrix Anatomy 0.000 description 25
- 230000006870 function Effects 0.000 description 25
- 239000000306 component Substances 0.000 description 23
- 239000000463 material Substances 0.000 description 23
- 230000003511 endothelial effect Effects 0.000 description 19
- 230000002441 reversible effect Effects 0.000 description 19
- 239000000243 solution Substances 0.000 description 19
- 239000003814 drug Substances 0.000 description 16
- 108010028309 kalinin Proteins 0.000 description 16
- 108010035532 Collagen Proteins 0.000 description 14
- 102000008186 Collagen Human genes 0.000 description 14
- 239000001888 Peptone Substances 0.000 description 14
- 108010080698 Peptones Proteins 0.000 description 14
- 235000019319 peptone Nutrition 0.000 description 14
- 238000002054 transplantation Methods 0.000 description 14
- WOVKYSAHUYNSMH-RRKCRQDMSA-N 5-bromodeoxyuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-RRKCRQDMSA-N 0.000 description 13
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 13
- 229920001436 collagen Polymers 0.000 description 13
- 239000001963 growth medium Substances 0.000 description 13
- 239000000126 substance Substances 0.000 description 13
- WOVKYSAHUYNSMH-UHFFFAOYSA-N BROMODEOXYURIDINE Natural products C1C(O)C(CO)OC1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-UHFFFAOYSA-N 0.000 description 12
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 12
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 12
- 210000002555 descemet membrane Anatomy 0.000 description 12
- 238000006467 substitution reaction Methods 0.000 description 12
- -1 thromboespondin Proteins 0.000 description 12
- 108020004414 DNA Proteins 0.000 description 11
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 11
- 210000002469 basement membrane Anatomy 0.000 description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 11
- 210000001519 tissue Anatomy 0.000 description 11
- JLEPZAUPTZFVIM-RHIZIOMBSA-N (3s,5s,9r,10s,13r,17r)-3-hydroxy-10,13-dimethyl-17-[(2r)-6-methylheptan-2-yl]-1,2,3,4,5,6,9,11,12,15,16,17-dodecahydrocyclopenta[a]phenanthrene-14-carbaldehyde Chemical compound C1[C@@H](O)CC[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@H](C)CCCC(C)C)CCC33C=O)C)C3=CC[C@H]21 JLEPZAUPTZFVIM-RHIZIOMBSA-N 0.000 description 10
- 238000004519 manufacturing process Methods 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- 102000003390 tumor necrosis factor Human genes 0.000 description 10
- 102000004506 Blood Proteins Human genes 0.000 description 9
- 108010017384 Blood Proteins Proteins 0.000 description 9
- 108010010803 Gelatin Proteins 0.000 description 9
- 101001023271 Homo sapiens Laminin subunit gamma-2 Proteins 0.000 description 9
- 102100027454 Laminin subunit beta-2 Human genes 0.000 description 9
- 241000288906 Primates Species 0.000 description 9
- 238000007792 addition Methods 0.000 description 9
- 239000008273 gelatin Substances 0.000 description 9
- 229920000159 gelatin Polymers 0.000 description 9
- 235000019322 gelatine Nutrition 0.000 description 9
- 235000011852 gelatine desserts Nutrition 0.000 description 9
- 108020004999 messenger RNA Proteins 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- 239000002773 nucleotide Substances 0.000 description 9
- 210000002966 serum Anatomy 0.000 description 9
- 108700028369 Alleles Proteins 0.000 description 8
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 8
- 241000282412 Homo Species 0.000 description 8
- 101001008558 Homo sapiens Laminin subunit beta-2 Proteins 0.000 description 8
- 102100035159 Laminin subunit gamma-2 Human genes 0.000 description 8
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 8
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 8
- 230000004075 alteration Effects 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 239000012091 fetal bovine serum Substances 0.000 description 8
- 210000002950 fibroblast Anatomy 0.000 description 8
- 238000001727 in vivo Methods 0.000 description 8
- 239000003446 ligand Substances 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 102100022746 Laminin subunit alpha-1 Human genes 0.000 description 7
- 102100022744 Laminin subunit alpha-3 Human genes 0.000 description 7
- 230000002349 favourable effect Effects 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 238000010899 nucleation Methods 0.000 description 7
- 239000012071 phase Substances 0.000 description 7
- 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
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 6
- 241000283690 Bos taurus Species 0.000 description 6
- 101000972489 Homo sapiens Laminin subunit alpha-1 Proteins 0.000 description 6
- 101000946306 Homo sapiens Laminin subunit gamma-1 Proteins 0.000 description 6
- 108060003951 Immunoglobulin Proteins 0.000 description 6
- 241001529936 Murinae Species 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 241000283973 Oryctolagus cuniculus Species 0.000 description 6
- 208000035475 disorder Diseases 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 238000009396 hybridization Methods 0.000 description 6
- 102000018358 immunoglobulin Human genes 0.000 description 6
- 108010008094 laminin alpha 3 Proteins 0.000 description 6
- 238000012423 maintenance Methods 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 239000011734 sodium Substances 0.000 description 6
- 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 6
- 241000282693 Cercopithecidae Species 0.000 description 5
- 206010010996 Corneal degeneration Diseases 0.000 description 5
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 5
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 5
- 101000972491 Homo sapiens Laminin subunit alpha-2 Proteins 0.000 description 5
- 101000972488 Homo sapiens Laminin subunit alpha-4 Proteins 0.000 description 5
- 101001023261 Homo sapiens Laminin subunit gamma-3 Proteins 0.000 description 5
- 102100022745 Laminin subunit alpha-2 Human genes 0.000 description 5
- 102100027450 Laminin subunit alpha-5 Human genes 0.000 description 5
- 102100024629 Laminin subunit beta-3 Human genes 0.000 description 5
- 102000016387 Pancreatic elastase Human genes 0.000 description 5
- 108010067372 Pancreatic elastase Proteins 0.000 description 5
- 229940098773 bovine serum albumin Drugs 0.000 description 5
- 201000004781 bullous keratopathy Diseases 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 5
- 201000010099 disease Diseases 0.000 description 5
- 229940126864 fibroblast growth factor Drugs 0.000 description 5
- 238000000684 flow cytometry Methods 0.000 description 5
- 108010090909 laminin gamma 1 Proteins 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 239000007790 solid phase Substances 0.000 description 5
- 239000013598 vector Substances 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 4
- 102000029816 Collagenase Human genes 0.000 description 4
- 108060005980 Collagenase Proteins 0.000 description 4
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 4
- 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 4
- 238000002965 ELISA Methods 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 108010067306 Fibronectins Proteins 0.000 description 4
- 102000016359 Fibronectins Human genes 0.000 description 4
- 229930182566 Gentamicin Natural products 0.000 description 4
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 4
- 101001008527 Homo sapiens Laminin subunit alpha-5 Proteins 0.000 description 4
- 102100022743 Laminin subunit alpha-4 Human genes 0.000 description 4
- 102100034710 Laminin subunit gamma-1 Human genes 0.000 description 4
- 102100035158 Laminin subunit gamma-3 Human genes 0.000 description 4
- 239000012124 Opti-MEM Substances 0.000 description 4
- 102000016611 Proteoglycans Human genes 0.000 description 4
- 108010067787 Proteoglycans Proteins 0.000 description 4
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000003044 adaptive effect Effects 0.000 description 4
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 4
- 238000013459 approach Methods 0.000 description 4
- 230000008827 biological function Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 229960002424 collagenase Drugs 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 230000004069 differentiation Effects 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 229960002518 gentamicin Drugs 0.000 description 4
- 229960004857 mitomycin Drugs 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 102000029752 retinol binding Human genes 0.000 description 4
- 108091000053 retinol binding Proteins 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 229940035893 uracil Drugs 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 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 3
- FWBHETKCLVMNFS-UHFFFAOYSA-N 4',6-Diamino-2-phenylindol Chemical compound C1=CC(C(=N)N)=CC=C1C1=CC2=CC=C(C(N)=N)C=C2N1 FWBHETKCLVMNFS-UHFFFAOYSA-N 0.000 description 3
- SQDAZGGFXASXDW-UHFFFAOYSA-N 5-bromo-2-(trifluoromethoxy)pyridine Chemical compound FC(F)(F)OC1=CC=C(Br)C=N1 SQDAZGGFXASXDW-UHFFFAOYSA-N 0.000 description 3
- 229920001287 Chondroitin sulfate Polymers 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 241000547293 Lambis Species 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108010038807 Oligopeptides Proteins 0.000 description 3
- 102000015636 Oligopeptides Human genes 0.000 description 3
- 229930182555 Penicillin Natural products 0.000 description 3
- 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 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 108010071690 Prealbumin Proteins 0.000 description 3
- 102000007584 Prealbumin Human genes 0.000 description 3
- 108010071390 Serum Albumin Proteins 0.000 description 3
- 102000007562 Serum Albumin Human genes 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 230000000692 anti-sense effect Effects 0.000 description 3
- 229960005070 ascorbic acid Drugs 0.000 description 3
- 235000010323 ascorbic acid Nutrition 0.000 description 3
- 239000011668 ascorbic acid Substances 0.000 description 3
- 210000000988 bone and bone Anatomy 0.000 description 3
- 230000004663 cell proliferation Effects 0.000 description 3
- 239000006285 cell suspension Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 229940059329 chondroitin sulfate Drugs 0.000 description 3
- 229940104302 cytosine Drugs 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 210000003038 endothelium Anatomy 0.000 description 3
- 210000002919 epithelial cell Anatomy 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- NGOGFTYYXHNFQH-UHFFFAOYSA-N fasudil Chemical compound C=1C=CC2=CN=CC=C2C=1S(=O)(=O)N1CCCNCC1 NGOGFTYYXHNFQH-UHFFFAOYSA-N 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 238000002515 oligonucleotide synthesis Methods 0.000 description 3
- 229940049954 penicillin Drugs 0.000 description 3
- 150000004713 phosphodiesters Chemical class 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 210000000130 stem cell Anatomy 0.000 description 3
- 229960005322 streptomycin Drugs 0.000 description 3
- 238000001356 surgical procedure Methods 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 3
- 102000011690 Adiponectin Human genes 0.000 description 2
- 108010076365 Adiponectin Proteins 0.000 description 2
- 239000012099 Alexa Fluor family Substances 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 241000282472 Canis lupus familiaris Species 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000012422 Collagen Type I Human genes 0.000 description 2
- 108010022452 Collagen Type I Proteins 0.000 description 2
- 206010011033 Corneal oedema Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 229920002683 Glycosaminoglycan Polymers 0.000 description 2
- 102000014702 Haptoglobin Human genes 0.000 description 2
- 108050005077 Haptoglobin Proteins 0.000 description 2
- 101001008568 Homo sapiens Laminin subunit beta-1 Proteins 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- 102100027448 Laminin subunit beta-1 Human genes 0.000 description 2
- 241001352366 Leucoma Species 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 102000014128 RANK Ligand Human genes 0.000 description 2
- 108010025832 RANK Ligand Proteins 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 238000000692 Student's t-test Methods 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 102000004338 Transferrin Human genes 0.000 description 2
- 108090000901 Transferrin Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 210000001691 amnion Anatomy 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 239000001045 blue dye Substances 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 210000003855 cell nucleus Anatomy 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 230000021615 conjugation Effects 0.000 description 2
- 201000004778 corneal edema Diseases 0.000 description 2
- 210000004748 cultured cell Anatomy 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 210000004177 elastic tissue Anatomy 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 230000001605 fetal effect Effects 0.000 description 2
- 210000003754 fetus Anatomy 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 239000000834 fixative Substances 0.000 description 2
- 238000010230 functional analysis Methods 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 108010046591 human laminin-511 Proteins 0.000 description 2
- 102000007573 human laminin-511 Human genes 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 238000012744 immunostaining Methods 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 108010057670 laminin 1 Proteins 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000012533 medium component Substances 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000001172 regenerating effect Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000003757 reverse transcription PCR Methods 0.000 description 2
- 239000003590 rho kinase inhibitor Substances 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- 210000001082 somatic cell Anatomy 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 230000008093 supporting effect Effects 0.000 description 2
- 239000012581 transferrin Substances 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 239000002753 trypsin inhibitor Substances 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 1
- LLAPDLPYIYKTGQ-UHFFFAOYSA-N 1-aminoethyl Chemical group C[CH]N LLAPDLPYIYKTGQ-UHFFFAOYSA-N 0.000 description 1
- VGONTNSXDCQUGY-RRKCRQDMSA-N 2'-deoxyinosine Chemical group C1[C@H](O)[C@@H](CO)O[C@H]1N1C(N=CNC2=O)=C2N=C1 VGONTNSXDCQUGY-RRKCRQDMSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- 102100022464 5'-nucleotidase Human genes 0.000 description 1
- 108091006112 ATPases Proteins 0.000 description 1
- 102000057290 Adenosine Triphosphatases Human genes 0.000 description 1
- 102100036601 Aggrecan core protein Human genes 0.000 description 1
- 108010067219 Aggrecans Proteins 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010029697 CD40 Ligand Proteins 0.000 description 1
- 102100032937 CD40 ligand Human genes 0.000 description 1
- 208000004434 Calcinosis Diseases 0.000 description 1
- 102000004266 Collagen Type IV Human genes 0.000 description 1
- 108010042086 Collagen Type IV Proteins 0.000 description 1
- 206010062621 Corneal endotheliitis Diseases 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000004237 Decorin Human genes 0.000 description 1
- 108090000738 Decorin Proteins 0.000 description 1
- 235000017274 Diospyros sandwicensis Nutrition 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 102000017177 Fibromodulin Human genes 0.000 description 1
- 108010013996 Fibromodulin Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102100040870 Glycine amidinotransferase, mitochondrial Human genes 0.000 description 1
- 229920002971 Heparan sulfate Polymers 0.000 description 1
- 208000003923 Hereditary Corneal Dystrophies Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000678236 Homo sapiens 5'-nucleotidase Proteins 0.000 description 1
- 101000893303 Homo sapiens Glycine amidinotransferase, mitochondrial Proteins 0.000 description 1
- 101100398641 Homo sapiens LAMA5 gene Proteins 0.000 description 1
- 101001051313 Homo sapiens Laminin subunit beta-3 Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 241000282838 Lama Species 0.000 description 1
- 102000002297 Laminin Receptors Human genes 0.000 description 1
- 108010000851 Laminin Receptors Proteins 0.000 description 1
- 101710200522 Laminin subunit alpha-1 Proteins 0.000 description 1
- 241000251236 Lamna Species 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 229940110339 Long-acting muscarinic antagonist Drugs 0.000 description 1
- 102100032114 Lumican Human genes 0.000 description 1
- 108010076371 Lumican Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 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
- 108010072582 Matrilin Proteins Proteins 0.000 description 1
- 102000055008 Matrilin Proteins Human genes 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108010019160 Pancreatin Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108010043958 Peptoids Proteins 0.000 description 1
- 240000004713 Pisum sativum Species 0.000 description 1
- 235000010582 Pisum sativum Nutrition 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 102100033237 Pro-epidermal growth factor Human genes 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 238000011530 RNeasy Mini Kit Methods 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108700005075 Regulator Genes Proteins 0.000 description 1
- 101100127659 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) LAM5 gene Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 102100040247 Tumor necrosis factor Human genes 0.000 description 1
- 102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 description 1
- 108050002568 Tumor necrosis factor ligand superfamily member 6 Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 102100035140 Vitronectin Human genes 0.000 description 1
- 108010031318 Vitronectin Proteins 0.000 description 1
- 241000282485 Vulpes vulpes Species 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- 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 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 102000013529 alpha-Fetoproteins Human genes 0.000 description 1
- 108010026331 alpha-Fetoproteins Proteins 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000002805 bone matrix Anatomy 0.000 description 1
- 210000004045 bowman membrane Anatomy 0.000 description 1
- 229950004398 broxuridine Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- VTYYLEPIZMXCLO-UHFFFAOYSA-L calcium carbonate Substances [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 239000002771 cell marker Substances 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 239000002458 cell surface marker Substances 0.000 description 1
- 238000012054 celltiter-glo Methods 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 239000008199 coating composition Substances 0.000 description 1
- 230000001143 conditioned effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 210000001608 connective tissue cell Anatomy 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 208000021921 corneal disease Diseases 0.000 description 1
- 206010011005 corneal dystrophy Diseases 0.000 description 1
- 201000004180 corneal endothelial dystrophy Diseases 0.000 description 1
- 210000003683 corneal stroma Anatomy 0.000 description 1
- 235000012343 cottonseed oil Nutrition 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical class 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
- 230000006378 damage Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 201000011268 dilated cardiomyopathy 1JJ Diseases 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 108010007093 dispase Proteins 0.000 description 1
- 238000007905 drug manufacturing Methods 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 230000005611 electricity Effects 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 210000003560 epithelium corneal Anatomy 0.000 description 1
- 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 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 201000004949 exfoliation syndrome Diseases 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000010195 expression analysis Methods 0.000 description 1
- 210000001723 extracellular space Anatomy 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 229960002435 fasudil Drugs 0.000 description 1
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001046 green dye Substances 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000007825 histological assay Methods 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 102000044420 human LAMA4 Human genes 0.000 description 1
- 102000049977 human LAMC2 Human genes 0.000 description 1
- 102000054352 human LAMC3 Human genes 0.000 description 1
- 108700002956 human laminin 11 Proteins 0.000 description 1
- 102000044407 human laminin 11 Human genes 0.000 description 1
- 210000003035 hyaline cartilage Anatomy 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229960003160 hyaluronic acid Drugs 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 210000004263 induced pluripotent stem cell Anatomy 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 210000001630 jejunum Anatomy 0.000 description 1
- 235000021174 kaiseki Nutrition 0.000 description 1
- 108010057725 laminin 6 Proteins 0.000 description 1
- 108010057719 laminin 7 Proteins 0.000 description 1
- 108010057717 laminin 8 Proteins 0.000 description 1
- 108010057697 laminin 9 Proteins 0.000 description 1
- 108010008097 laminin alpha 2 Proteins 0.000 description 1
- 108010088360 laminin alpha5 Proteins 0.000 description 1
- 108010009114 laminin beta2 Proteins 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000029226 lipidation Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000012567 medical material Substances 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 210000001724 microfibril Anatomy 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 230000003562 morphometric effect Effects 0.000 description 1
- 238000013425 morphometry Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 229930014626 natural product Natural products 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 230000014511 neuron projection development Effects 0.000 description 1
- 230000006576 neuronal survival Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000012758 nuclear staining Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 210000000963 osteoblast Anatomy 0.000 description 1
- 210000001819 pancreatic juice Anatomy 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 150000008300 phosphoramidites Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920003213 poly(N-isopropyl acrylamide) Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 239000004417 polycarbonate Substances 0.000 description 1
- 229920000515 polycarbonate Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 239000003761 preservation solution Substances 0.000 description 1
- 238000007639 printing Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 238000005086 pumping Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 239000001044 red dye Substances 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 230000037390 scarring Effects 0.000 description 1
- 210000004116 schwann cell Anatomy 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 210000003491 skin Anatomy 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
- 239000007787 solid Substances 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 210000002435 tendon Anatomy 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 231100000747 viability assay Toxicity 0.000 description 1
- 238000003026 viability measurement method Methods 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/06—Animal cells or tissues; Human cells or tissues
- C12N5/0602—Vertebrate cells
- C12N5/0618—Cells of the nervous system
- C12N5/0621—Eye cells, e.g. cornea, iris pigmented cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
- A61K35/30—Nerves; Brain; Eyes; Corneal cells; Cerebrospinal fluid; Neuronal stem cells; Neuronal precursor cells; Glial cells; Oligodendrocytes; Schwann cells; Astroglia; Astrocytes; Choroid plexus; Spinal cord tissue
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2533/00—Supports or coatings for cell culture, characterised by material
- C12N2533/50—Proteins
- C12N2533/52—Fibronectin; Laminin
Landscapes
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Cell Biology (AREA)
- General Health & Medical Sciences (AREA)
- Ophthalmology & Optometry (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Developmental Biology & Embryology (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Virology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2013244972 | 2013-11-27 | ||
| PCT/JP2014/081917 WO2015080297A1 (en) | 2013-11-27 | 2014-11-26 | Application of laminin to corneal endothelial cell culture |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2763433T3 true ES2763433T3 (es) | 2020-05-28 |
Family
ID=52432880
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES14831100T Active ES2763433T3 (es) | 2013-11-27 | 2014-11-26 | Aplicación de laminina a cultivos de células endoteliales de la córnea |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US11624053B2 (enExample) |
| EP (1) | EP3074508B1 (enExample) |
| JP (3) | JP6470286B2 (enExample) |
| CN (1) | CN105814195A (enExample) |
| BR (1) | BR112016011096A2 (enExample) |
| CA (1) | CA2931280A1 (enExample) |
| ES (1) | ES2763433T3 (enExample) |
| MX (1) | MX2016006915A (enExample) |
| RU (1) | RU2704984C1 (enExample) |
| WO (1) | WO2015080297A1 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2858173C (en) | 2011-12-06 | 2023-09-26 | Advanced Cell Technology, Inc. | Method of directed differentiation producing corneal endothelial cells, compositions thereof, and uses thereof |
| CN113559246A (zh) | 2014-10-31 | 2021-10-29 | 京都府公立大学法人 | 使用层粘连蛋白的新的角膜的治疗 |
| WO2016067629A1 (ja) | 2014-10-31 | 2016-05-06 | 京都府公立大学法人 | ラミニンによる網膜および神経の新規治療 |
| JP6849957B2 (ja) * | 2015-11-10 | 2021-03-31 | 国立大学法人京都大学 | ラミニンフラグメント含有培地を用いる細胞培養方法 |
| JP6605618B2 (ja) * | 2015-11-10 | 2019-11-20 | 日機装株式会社 | 細胞支持複合体および細胞支持複合体の製造方法 |
| MY192056A (en) * | 2017-01-31 | 2022-07-25 | Univ Osaka | Method for controlling differentiation of pluripotent stem cells |
| US20210372995A1 (en) * | 2017-10-22 | 2021-12-02 | The Johns Hopkins University | Biomimetic platforms to model vascular pathophysiology, diagnostics, and therapy |
| WO2019102593A1 (ja) * | 2017-11-24 | 2019-05-31 | 株式会社Ihi | 細胞培養装置 |
| CA3109705A1 (en) * | 2018-10-02 | 2020-04-09 | The Doshisha | Method and vessel for preserving corneal endothelial cells |
| JP6664755B1 (ja) * | 2018-10-02 | 2020-03-13 | 学校法人同志社 | 角膜内皮細胞を保存するための方法および容器 |
| US20220133659A1 (en) * | 2019-03-12 | 2022-05-05 | Nissan Chemical Corporation | Therapeutic agent for corneal diseases |
| JP2023025311A (ja) * | 2020-02-05 | 2023-02-22 | 味の素株式会社 | タンパク質の製造方法 |
| CN112522179A (zh) * | 2020-12-23 | 2021-03-19 | 江苏艾尔康生物医药科技有限公司 | 一种角膜内皮细胞的分离培养方法 |
Family Cites Families (62)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4678783B1 (en) | 1983-11-04 | 1995-04-04 | Asahi Chemical Ind | Substituted isoquinolinesulfonyl compounds |
| EP1195372A1 (en) | 1994-04-18 | 2002-04-10 | Mitsubishi Pharma Corporation | N-heterocyclic substituted benzamide derivatives with antihypertensive activity |
| JP3421217B2 (ja) | 1995-11-20 | 2003-06-30 | 麒麟麦酒株式会社 | Ｒｈｏ標的タンパク質Ｒｈｏキナーゼ |
| EP0954328A4 (en) | 1996-06-05 | 2002-07-17 | Gen Hospital Corp | Laminin-5 and the production of a basement membrane structure |
| FR2765781B1 (fr) | 1997-07-08 | 1999-09-24 | Gioia Bruno Di | Procede de fabrication d'un accessoire de mode, dispositif pour la mise en oeuvre du procede et accessoire de mode ainsi realise |
| US6042262A (en) | 1997-07-29 | 2000-03-28 | Stryker Technologies Corportion | Apparatus for storing, mixing, and dispensing two-component bone cement |
| US6693169B1 (en) | 1998-10-13 | 2004-02-17 | The General Hospital Corporation | Laminin 5, 13 and 14 and uses thereof |
| WO2000066731A2 (en) | 1999-04-30 | 2000-11-09 | Biostatum, Inc. | Recombinant laminin 5 |
| US6635616B2 (en) | 2000-05-01 | 2003-10-21 | The General Hospital Corporation | Laminin 15 |
| WO2002050111A2 (en) | 2000-12-21 | 2002-06-27 | Biostratum, Inc. | Isolated laminin 10 |
| MXPA03008658A (es) | 2001-03-23 | 2005-04-11 | Bayer Ag | Inhibidores de rho-cinasa. |
| UY27225A1 (es) | 2001-03-23 | 2002-10-31 | Bayer Corp | Inhibidores de la rho-quinasa |
| CN101310771B (zh) | 2001-04-11 | 2012-08-08 | 千寿制药株式会社 | 视觉功能障碍改善剂 |
| WO2002100833A1 (en) | 2001-06-12 | 2002-12-19 | Sumitomo Pharmaceuticals Company, Limited | Rho KINASE INHIBITORS |
| CA2472619A1 (en) | 2002-01-10 | 2003-07-24 | Bayer Corporation | Fused pyrimidine derivates as rho-kinase inhibitors |
| US6943172B2 (en) | 2002-01-23 | 2005-09-13 | Bayer Pharmaceuticals Corporation | Rho-kinase inhibitors |
| AU2003211971A1 (en) * | 2002-04-30 | 2003-11-17 | Amniotec Inc. | Corneal endothelium-like sheet and method of constructing the same |
| JP2004024852A (ja) | 2002-04-30 | 2004-01-29 | Amniotec:Kk | 角膜内皮様シート、及びその作製方法 |
| AU2003281623B8 (en) | 2002-07-22 | 2009-06-11 | Asahi Kasei Pharma Corporation | 5-substituted isoquinoline derivative |
| CA2400996A1 (en) | 2002-09-03 | 2004-03-03 | Lisa Mckerracher | 1,4-substituted cyclohexane derivatives |
| US7160894B2 (en) | 2003-06-06 | 2007-01-09 | Asahi Kasei Pharma Corporation | Tricyclic compound |
| JP2007516196A (ja) | 2003-07-02 | 2007-06-21 | ガラパゴス エヌブイ | Ｒｈｏキナーゼ阻害剤としてのピラジン及びピラリジン誘導体 |
| WO2005039564A1 (en) | 2003-10-02 | 2005-05-06 | Vertex Pharmaceuticals Incorporated | Phthalimide compounds useful as protein kinase inhibitors |
| EP1670466A4 (en) | 2003-10-06 | 2007-04-25 | Glaxo Group Ltd | PREPARATION OF 1,6,7-TRISUBSTITUTED AZABENIC ZIMIDAZOLES AS KINASE-INHIBITORS |
| ES2387780T3 (es) | 2003-10-06 | 2012-10-01 | Glaxosmithkline Llc | Preparación de azabencimidazoles 1,6-disustituidos como inhibidores de quinasas |
| EP1689393A4 (en) | 2003-10-06 | 2008-12-17 | Glaxo Group Ltd | PREPARATION OF 1,7-DISUBSTITUTED AZABENZIMIDAZOLES AS KINASE INHIBITORS |
| EP1675944B1 (en) | 2003-10-10 | 2010-11-24 | Ge Ming Lui | Human corneal endothelial cells and methods of obtaining and culturing cells for corneal cell transplantation |
| JP2007509643A (ja) | 2003-10-10 | 2007-04-19 | ゲ・ミン・ルイ | 角膜内皮および関連細胞のバイオポリマー上での増殖のための方法および組成物ならびに人工角膜移植片の作成 |
| CN100560142C (zh) * | 2003-10-10 | 2009-11-18 | 细胞生物工程公司 | 用于在生物聚合物上培养角膜内皮细胞和相关细胞以及产生人工角膜移植物的方法和组合物 |
| JP2007015928A (ja) | 2003-10-15 | 2007-01-25 | Ube Ind Ltd | 新規オレフィン誘導体 |
| JP2007008816A (ja) | 2003-10-15 | 2007-01-18 | Ube Ind Ltd | 新規イソキノリン誘導体 |
| WO2005035506A1 (ja) | 2003-10-15 | 2005-04-21 | Ube Industries, Ltd. | 新規インダゾール誘導体 |
| SG188122A1 (en) | 2004-01-23 | 2013-03-28 | Advanced Cell Tech Inc | Improved modalities for the treatment of degenerative diseases of the retina |
| ES2532778T3 (es) | 2004-02-12 | 2015-03-31 | Government Of The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Administración terapéutica del péptido antiangiogénico mezclado C16Y |
| EP1720874A4 (en) | 2004-02-24 | 2010-03-03 | Bioaxone Therapeutique Inc | 4-SUBSTITUTED PIPERIDINE DERIVATIVES |
| MXPA06011328A (es) | 2004-04-02 | 2006-12-15 | Vertex Pharma | Azaindoles utiles como inhibidotes de roca y otras proteinas cinasas. |
| JPWO2006057270A1 (ja) | 2004-11-26 | 2008-06-05 | 旭化成ファーマ株式会社 | 含窒素３環化合物 |
| EP1932841B1 (en) | 2005-08-30 | 2014-01-01 | Asahi Kasei Pharma Corporation | Sulfonamide compound |
| WO2007083685A1 (ja) | 2006-01-19 | 2007-07-26 | Senju Pharmaceutical Co., Ltd. | 生体内で細胞増殖可能な角膜内皮製剤 |
| US20090175835A1 (en) | 2006-02-07 | 2009-07-09 | Korea Institute Of Radiological & Medical Sciences | Composition for treating damage of central or peripheral nerve system |
| WO2007127172A2 (en) | 2006-04-27 | 2007-11-08 | The Trustees Of Columbia University In The City Of New York | Layered bio-adhesive compositions and uses thereof |
| US8951799B2 (en) | 2007-01-04 | 2015-02-10 | Biolamina Ab | Composition and method for enabling proliferation of pluripotent stem cells |
| KR20100080514A (ko) * | 2007-08-29 | 2010-07-08 | 센주 세이야꾸 가부시키가이샤 | 각막 내피 세포 접착 촉진제 |
| US20090306772A1 (en) | 2008-04-18 | 2009-12-10 | The Regents Of The University Of California | Ocular Scaffolds and Methods for Subretinal Repair of Bruch's Membrane |
| US8680182B2 (en) | 2009-06-04 | 2014-03-25 | Clemson University Research Foundation | Methods for promoting the revascularization and reenervation of CNS lesions |
| JP2011010653A (ja) | 2009-06-05 | 2011-01-20 | Kumamoto Univ | 細胞の分化誘導方法 |
| JP5590646B2 (ja) * | 2009-10-08 | 2014-09-17 | 国立大学法人大阪大学 | ヒト多能性幹細胞用培養基材およびその利用 |
| RU2418067C1 (ru) | 2009-12-03 | 2011-05-10 | Государственное образовательное учреждение высшего профессионального образования "Оренбургский государственный университет" | Способ культивирования клеток |
| WO2011080984A1 (en) | 2009-12-29 | 2011-07-07 | Senju Pharmaceutical Co., Ltd. | Therapeutic agent (y - 39983 ) for corneal endothelial dysfunction |
| US8415156B2 (en) | 2010-12-17 | 2013-04-09 | Biolamina Ab | Recombinant laminin-521 |
| WO2012173207A1 (ja) | 2011-06-14 | 2012-12-20 | 独立行政法人理化学研究所 | 網膜細胞への分化誘導方法 |
| WO2013012087A1 (ja) * | 2011-07-15 | 2013-01-24 | 国立大学法人大阪大学 | 角膜内皮細胞の調製方法 |
| WO2013047763A1 (ja) | 2011-09-29 | 2013-04-04 | オリエンタル酵母工業株式会社 | ラミニン５１１を含んだ系で哺乳類細胞を培養する方法 |
| CA2855941A1 (en) | 2011-11-14 | 2013-05-23 | Advanced Cell Technology, Inc. | Pharmaceutical preparations of human rpe cells and uses thereof |
| CN113817679A (zh) | 2011-11-25 | 2021-12-21 | 住友化学株式会社 | 制备视网膜组织和视网膜相关细胞的方法 |
| JP5985207B2 (ja) | 2011-11-25 | 2016-09-06 | 住友化学株式会社 | 網膜色素上皮細胞の製造方法 |
| CA2858173C (en) * | 2011-12-06 | 2023-09-26 | Advanced Cell Technology, Inc. | Method of directed differentiation producing corneal endothelial cells, compositions thereof, and uses thereof |
| WO2013148377A1 (en) | 2012-03-25 | 2013-10-03 | The Board Of Trustees Of The Leland Stanford Junior University | Methods for modulating hair growth using truncated laminin-511 |
| EP2925856B1 (en) | 2012-12-03 | 2018-03-07 | Biolamina AB | Methods of producing rpe cells |
| US11492593B2 (en) | 2013-10-09 | 2022-11-08 | Healios K.K. | Method for purification of retinal pigment epithelial cells |
| WO2016067629A1 (ja) | 2014-10-31 | 2016-05-06 | 京都府公立大学法人 | ラミニンによる網膜および神経の新規治療 |
| CN113559246A (zh) | 2014-10-31 | 2021-10-29 | 京都府公立大学法人 | 使用层粘连蛋白的新的角膜的治疗 |
-
2014
- 2014-11-26 RU RU2016125225A patent/RU2704984C1/ru not_active IP Right Cessation
- 2014-11-26 ES ES14831100T patent/ES2763433T3/es active Active
- 2014-11-26 JP JP2016535065A patent/JP6470286B2/ja active Active
- 2014-11-26 BR BR112016011096A patent/BR112016011096A2/pt not_active Application Discontinuation
- 2014-11-26 US US15/100,147 patent/US11624053B2/en active Active
- 2014-11-26 WO PCT/JP2014/081917 patent/WO2015080297A1/en not_active Ceased
- 2014-11-26 EP EP14831100.4A patent/EP3074508B1/en active Active
- 2014-11-26 CN CN201480065134.XA patent/CN105814195A/zh active Pending
- 2014-11-26 MX MX2016006915A patent/MX2016006915A/es unknown
- 2014-11-26 CA CA2931280A patent/CA2931280A1/en not_active Abandoned
-
2019
- 2019-01-17 JP JP2019006098A patent/JP2019054828A/ja not_active Withdrawn
-
2020
- 2020-06-05 JP JP2020098407A patent/JP2020188778A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| CA2931280A1 (en) | 2015-06-04 |
| MX2016006915A (es) | 2017-01-23 |
| JP2020188778A (ja) | 2020-11-26 |
| JP2016539641A (ja) | 2016-12-22 |
| EP3074508A1 (en) | 2016-10-05 |
| CN105814195A (zh) | 2016-07-27 |
| RU2016125225A (ru) | 2018-01-09 |
| WO2015080297A1 (en) | 2015-06-04 |
| JP6470286B2 (ja) | 2019-02-13 |
| BR112016011096A2 (pt) | 2017-09-19 |
| EP3074508B1 (en) | 2019-11-06 |
| JP2019054828A (ja) | 2019-04-11 |
| US20170002318A1 (en) | 2017-01-05 |
| RU2704984C1 (ru) | 2019-11-01 |
| US11624053B2 (en) | 2023-04-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2763433T3 (es) | Aplicación de laminina a cultivos de células endoteliales de la córnea | |
| Okumura et al. | ROCK inhibitor converts corneal endothelial cells into a phenotype capable of regenerating in vivo endothelial tissue | |
| RU2718062C2 (ru) | Новое лечение роговицы с применением ламинина | |
| ES2896504T3 (es) | Fármaco que contiene inhibidor de caspasa para el tratamiento o la prevención de trastornos causados por TGF-beta y aplicaciones del mismo | |
| CN103403148A (zh) | 通过细胞产生牙本质、牙骨质和牙釉质 | |
| JPWO2020045642A1 (ja) | 眼細胞を保存または培養するための組成物および方法 | |
| US11918630B2 (en) | Treatment of retina and nerve using laminin | |
| CN107249607A (zh) | 包括工程化内皮细胞的生物相容性植入物 | |
| Scafetta et al. | Suitability of human Tenon’s fibroblasts as feeder cells for culturing human limbal epithelial stem cells | |
| Igoucheva et al. | Protein therapeutics for Junctional Epidermolysis bullosa: incorporation of recombinant β3 chain into laminin 332 in β3-/-keratinocytes in vitro | |
| Wu et al. | Co-culture of RhoA-overexpressed microtia chondrocytes and adipose-derived stem cells in the construction of tissue-engineered ear-shaped cartilage | |
| JP6440107B2 (ja) | 細胞シートの製造方法、組成物、細胞培養補助剤、及び細胞培養方法 | |
| An et al. | Tissue engineered ultra-thin descemet stripping corneal endothelial layers using porcine cornea and stem cells | |
| Bird et al. | Effects of microinjected small GTPases on the actin cytoskeleton of human neutrophils | |
| US9682118B1 (en) | Inhibition of metastasis by cell penetrating peptides | |
| Chen et al. | Research on the construction of corneal endothelium transplantation with acellular amniotic membrane as a scaffold | |
| Nolan | The role of growth factors in the pathogenesis of pterygium |