MX2012006126A - Oligopeptidos imp-3 y vacunas que incluyen los mismos. - Google Patents
Oligopeptidos imp-3 y vacunas que incluyen los mismos.Info
- Publication number
- MX2012006126A MX2012006126A MX2012006126A MX2012006126A MX2012006126A MX 2012006126 A MX2012006126 A MX 2012006126A MX 2012006126 A MX2012006126 A MX 2012006126A MX 2012006126 A MX2012006126 A MX 2012006126A MX 2012006126 A MX2012006126 A MX 2012006126A
- Authority
- MX
- Mexico
- Prior art keywords
- oligopeptide
- hla
- antigen
- imp
- peptides
- Prior art date
Links
- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 101
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 101
- 229960005486 vaccine Drugs 0.000 title claims description 19
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 claims abstract description 215
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 148
- 150000001413 amino acids Chemical class 0.000 claims abstract description 88
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 48
- 230000002980 postoperative effect Effects 0.000 claims abstract description 13
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 365
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 227
- 210000004027 cell Anatomy 0.000 claims description 162
- 238000000034 method Methods 0.000 claims description 133
- 201000011510 cancer Diseases 0.000 claims description 109
- 108091007433 antigens Proteins 0.000 claims description 91
- 102000036639 antigens Human genes 0.000 claims description 90
- 239000000427 antigen Substances 0.000 claims description 89
- 210000000612 antigen-presenting cell Anatomy 0.000 claims description 87
- 108010074032 HLA-A2 Antigen Proteins 0.000 claims description 75
- 102000025850 HLA-A2 Antigen Human genes 0.000 claims description 74
- 102000040430 polynucleotide Human genes 0.000 claims description 62
- 108091033319 polynucleotide Proteins 0.000 claims description 62
- 239000002157 polynucleotide Substances 0.000 claims description 62
- 239000008177 pharmaceutical agent Substances 0.000 claims description 38
- 239000004480 active ingredient Substances 0.000 claims description 33
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 31
- 239000003795 chemical substances by application Substances 0.000 claims description 31
- 230000001939 inductive effect Effects 0.000 claims description 31
- 238000011282 treatment Methods 0.000 claims description 30
- 108091008874 T cell receptors Proteins 0.000 claims description 29
- 238000004519 manufacturing process Methods 0.000 claims description 28
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 claims description 27
- 230000002265 prevention Effects 0.000 claims description 27
- 210000001808 exosome Anatomy 0.000 claims description 22
- 229920001184 polypeptide Polymers 0.000 claims description 22
- 239000012634 fragment Substances 0.000 claims description 20
- 238000011321 prophylaxis Methods 0.000 claims description 17
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 15
- 230000028993 immune response Effects 0.000 claims description 15
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 13
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 11
- 229930182817 methionine Natural products 0.000 claims description 11
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 8
- 239000004474 valine Substances 0.000 claims description 8
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 6
- 239000003937 drug carrier Substances 0.000 claims description 6
- 239000003981 vehicle Substances 0.000 claims description 6
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims description 5
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 31
- 239000003814 drug Substances 0.000 abstract description 10
- 229940079593 drug Drugs 0.000 abstract description 8
- 229940022399 cancer vaccine Drugs 0.000 abstract description 5
- 238000009566 cancer vaccine Methods 0.000 abstract description 5
- 238000002619 cancer immunotherapy Methods 0.000 abstract 1
- 101710126182 Insulin-like growth factor 2 mRNA-binding protein 3 Proteins 0.000 description 131
- 102100037920 Insulin-like growth factor 2 mRNA-binding protein 3 Human genes 0.000 description 118
- 235000001014 amino acid Nutrition 0.000 description 53
- 229940024606 amino acid Drugs 0.000 description 52
- 108090000623 proteins and genes Proteins 0.000 description 44
- 230000014509 gene expression Effects 0.000 description 40
- 102100037850 Interferon gamma Human genes 0.000 description 30
- 108010074328 Interferon-gamma Proteins 0.000 description 30
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 27
- 201000005202 lung cancer Diseases 0.000 description 27
- 208000020816 lung neoplasm Diseases 0.000 description 27
- 239000000523 sample Substances 0.000 description 27
- 230000001472 cytotoxic effect Effects 0.000 description 25
- 239000000203 mixture Substances 0.000 description 25
- 235000018102 proteins Nutrition 0.000 description 25
- 102000004169 proteins and genes Human genes 0.000 description 25
- 150000007523 nucleic acids Chemical class 0.000 description 24
- 150000003839 salts Chemical class 0.000 description 24
- 230000000638 stimulation Effects 0.000 description 23
- 239000013598 vector Substances 0.000 description 22
- 102000039446 nucleic acids Human genes 0.000 description 20
- 108020004707 nucleic acids Proteins 0.000 description 20
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 20
- 239000003153 chemical reaction reagent Substances 0.000 description 18
- 210000001519 tissue Anatomy 0.000 description 18
- 230000004048 modification Effects 0.000 description 17
- 238000012986 modification Methods 0.000 description 17
- 238000003556 assay Methods 0.000 description 16
- 239000000463 material Substances 0.000 description 16
- 125000003729 nucleotide group Chemical group 0.000 description 16
- 210000004443 dendritic cell Anatomy 0.000 description 15
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 15
- 230000004044 response Effects 0.000 description 15
- 239000000126 substance Substances 0.000 description 15
- 201000010099 disease Diseases 0.000 description 14
- 239000002773 nucleotide Substances 0.000 description 14
- 230000000694 effects Effects 0.000 description 13
- 238000000338 in vitro Methods 0.000 description 13
- 230000006698 induction Effects 0.000 description 13
- 208000000461 Esophageal Neoplasms Diseases 0.000 description 12
- 238000003114 enzyme-linked immunosorbent spot assay Methods 0.000 description 12
- 230000006870 function Effects 0.000 description 12
- 230000003389 potentiating effect Effects 0.000 description 12
- 201000004101 esophageal cancer Diseases 0.000 description 11
- 238000001727 in vivo Methods 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 11
- 238000012360 testing method Methods 0.000 description 11
- 102100035133 Lysosome-associated membrane glycoprotein 1 Human genes 0.000 description 10
- 206010030155 Oesophageal carcinoma Diseases 0.000 description 10
- 230000003013 cytotoxicity Effects 0.000 description 9
- 231100000135 cytotoxicity Toxicity 0.000 description 9
- 238000001514 detection method Methods 0.000 description 9
- 230000005764 inhibitory process Effects 0.000 description 9
- 238000006467 substitution reaction Methods 0.000 description 9
- 238000013519 translation Methods 0.000 description 9
- 238000011510 Elispot assay Methods 0.000 description 8
- 101001023379 Homo sapiens Lysosome-associated membrane glycoprotein 1 Proteins 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 210000004369 blood Anatomy 0.000 description 8
- 239000008280 blood Substances 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 8
- 108020004705 Codon Proteins 0.000 description 7
- 125000000539 amino acid group Chemical group 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 239000004615 ingredient Substances 0.000 description 7
- 108091005601 modified peptides Proteins 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 230000001105 regulatory effect Effects 0.000 description 7
- 210000004881 tumor cell Anatomy 0.000 description 7
- 241001465754 Metazoa Species 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 239000002585 base Substances 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 6
- 238000011161 development Methods 0.000 description 6
- 238000009169 immunotherapy Methods 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 235000013902 inosinic acid Nutrition 0.000 description 6
- 238000010647 peptide synthesis reaction Methods 0.000 description 6
- 125000006850 spacer group Chemical group 0.000 description 6
- 241000124008 Mammalia Species 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 239000011651 chromium Substances 0.000 description 5
- 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 5
- 230000002163 immunogen Effects 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- 239000012472 biological sample Substances 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 229910052739 hydrogen Inorganic materials 0.000 description 4
- 238000011835 investigation Methods 0.000 description 4
- 229910052751 metal Inorganic materials 0.000 description 4
- 239000002184 metal Substances 0.000 description 4
- 150000007522 mineralic acids Chemical class 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 239000013641 positive control Substances 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 230000004936 stimulating effect Effects 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 108010013476 HLA-A24 Antigen Proteins 0.000 description 3
- 101000599782 Homo sapiens Insulin-like growth factor 2 mRNA-binding protein 3 Proteins 0.000 description 3
- 101000702394 Homo sapiens Signal peptide peptidase-like 2A Proteins 0.000 description 3
- 101000960621 Homo sapiens U3 small nucleolar ribonucleoprotein protein IMP3 Proteins 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 3
- 241000699660 Mus musculus Species 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 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 3
- 235000004279 alanine Nutrition 0.000 description 3
- 229910052783 alkali metal Inorganic materials 0.000 description 3
- 150000001340 alkali metals Chemical class 0.000 description 3
- 230000005809 anti-tumor immunity Effects 0.000 description 3
- 230000005975 antitumor immune response Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 210000002919 epithelial cell Anatomy 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000002147 killing effect Effects 0.000 description 3
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 210000002433 mononuclear leukocyte Anatomy 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 150000007524 organic acids Chemical class 0.000 description 3
- 150000007530 organic bases Chemical class 0.000 description 3
- 210000005259 peripheral blood Anatomy 0.000 description 3
- 239000011886 peripheral blood Substances 0.000 description 3
- 239000002831 pharmacologic agent Substances 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 230000001177 retroviral effect Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 210000000952 spleen Anatomy 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 230000009261 transgenic effect Effects 0.000 description 3
- 238000011830 transgenic mouse model Methods 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 108700028369 Alleles Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000702421 Dependoparvovirus Species 0.000 description 2
- 241000283073 Equus caballus Species 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
- 102000011786 HLA-A Antigens Human genes 0.000 description 2
- 108010075704 HLA-A Antigens Proteins 0.000 description 2
- 102000006354 HLA-DR Antigens Human genes 0.000 description 2
- 108010058597 HLA-DR Antigens Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 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 2
- 206010027476 Metastases Diseases 0.000 description 2
- AFVFQIVMOAPDHO-UHFFFAOYSA-N Methanesulfonic acid Chemical compound CS(O)(=O)=O AFVFQIVMOAPDHO-UHFFFAOYSA-N 0.000 description 2
- 108700020796 Oncogene Proteins 0.000 description 2
- 241000009328 Perro Species 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- FKNQFGJONOIPTF-UHFFFAOYSA-N Sodium cation Chemical compound [Na+] FKNQFGJONOIPTF-UHFFFAOYSA-N 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 241000700618 Vaccinia virus Species 0.000 description 2
- 206010046865 Vaccinia virus infection Diseases 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000003501 co-culture Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 238000012790 confirmation Methods 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 239000010432 diamond Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 210000003038 endothelium Anatomy 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 229910052731 fluorine Inorganic materials 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 238000001415 gene therapy Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000001024 immunotherapeutic effect Effects 0.000 description 2
- 238000010253 intravenous injection Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- 238000002493 microarray Methods 0.000 description 2
- 230000005486 microgravity Effects 0.000 description 2
- 210000001616 monocyte Anatomy 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- NRNCYVBFPDDJNE-UHFFFAOYSA-N pemoline Chemical compound O1C(N)=NC(=O)C1C1=CC=CC=C1 NRNCYVBFPDDJNE-UHFFFAOYSA-N 0.000 description 2
- 230000002093 peripheral effect Effects 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 239000008196 pharmacological composition Substances 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 229910052700 potassium Inorganic materials 0.000 description 2
- 238000004321 preservation Methods 0.000 description 2
- 230000037452 priming Effects 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 229910001415 sodium ion Inorganic materials 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 238000007910 systemic administration Methods 0.000 description 2
- 230000008685 targeting Effects 0.000 description 2
- 230000009258 tissue cross reactivity Effects 0.000 description 2
- JOXIMZWYDAKGHI-UHFFFAOYSA-N toluene-4-sulfonic acid Chemical compound CC1=CC=C(S(O)(=O)=O)C=C1 JOXIMZWYDAKGHI-UHFFFAOYSA-N 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 229910052721 tungsten Inorganic materials 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- 208000007089 vaccinia Diseases 0.000 description 2
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 229910052727 yttrium Inorganic materials 0.000 description 2
- KPYXMALABCDPGN-HYOZMBHHSA-N (4s)-5-[[(2s)-6-amino-1-[[(2s,3s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2r)-1-[[2-[[2-[[(1s)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]a Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN)CC1=CC=C(O)C=C1 KPYXMALABCDPGN-HYOZMBHHSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- LEBVLXFERQHONN-UHFFFAOYSA-N 1-butyl-N-(2,6-dimethylphenyl)piperidine-2-carboxamide Chemical compound CCCCN1CCCCC1C(=O)NC1=C(C)C=CC=C1C LEBVLXFERQHONN-UHFFFAOYSA-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
- BMYNFMYTOJXKLE-UHFFFAOYSA-N 3-azaniumyl-2-hydroxypropanoate Chemical compound NCC(O)C(O)=O BMYNFMYTOJXKLE-UHFFFAOYSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Chemical compound OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000193738 Bacillus anthracis Species 0.000 description 1
- 101100314454 Caenorhabditis elegans tra-1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 208000017897 Carcinoma of esophagus Diseases 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 208000000666 Fowlpox Diseases 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
- 239000004471 Glycine Substances 0.000 description 1
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 1
- 101001043807 Homo sapiens Interleukin-7 Proteins 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-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
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-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
- 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
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 108010009254 Lysosomal-Associated Membrane Protein 1 Proteins 0.000 description 1
- 101710116782 Lysosome-associated membrane glycoprotein 1 Proteins 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
- 108010046117 N-palmitoyl-5,6-dipalmitoyl-S-glycerylcysteinyl-seryl-serine Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108091061960 Naked DNA Proteins 0.000 description 1
- GRYLNZFGIOXLOG-UHFFFAOYSA-N Nitric acid Chemical compound O[N+]([O-])=O GRYLNZFGIOXLOG-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 241001504519 Papio ursinus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 206010036790 Productive cough Diseases 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 238000012228 RNA interference-mediated gene silencing Methods 0.000 description 1
- 238000010240 RT-PCR analysis Methods 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000002278 Ribosomal Proteins Human genes 0.000 description 1
- 108010000605 Ribosomal Proteins Proteins 0.000 description 1
- YDBYJHTYSHBBAU-YFKPBYRVSA-N S-methyl-L-methioninate Chemical compound C[S+](C)CC[C@H](N)C([O-])=O YDBYJHTYSHBBAU-YFKPBYRVSA-N 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241000293871 Salmonella enterica subsp. enterica serovar Typhi Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 102100036011 T-cell surface glycoprotein CD4 Human genes 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
- 229910052770 Uranium Inorganic materials 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000001815 biotherapy Methods 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 229960003150 bupivacaine Drugs 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
- 230000005880 cancer cell killing Effects 0.000 description 1
- 230000005907 cancer growth Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- UHBYWPGGCSDKFX-UHFFFAOYSA-N carboxyglutamic acid Chemical compound OC(=O)C(N)CC(C(O)=O)C(O)=O UHBYWPGGCSDKFX-UHFFFAOYSA-N 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- -1 cationic lipid Chemical class 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000000973 chemotherapeutic effect Effects 0.000 description 1
- 229910052804 chromium Inorganic materials 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 238000012136 culture method Methods 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
- 230000001461 cytolytic effect Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000000368 destabilizing effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 229910003460 diamond Inorganic materials 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 229940088679 drug related substance Drugs 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- CCIVGXIOQKPBKL-UHFFFAOYSA-M ethanesulfonate Chemical compound CCS([O-])(=O)=O CCIVGXIOQKPBKL-UHFFFAOYSA-M 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000011888 foil Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- UKAUYVFTDYCKQA-UHFFFAOYSA-N homoserine Chemical compound OC(=O)C(N)CCO UKAUYVFTDYCKQA-UHFFFAOYSA-N 0.000 description 1
- 102000052622 human IL7 Human genes 0.000 description 1
- 150000002431 hydrogen Chemical group 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002998 immunogenetic effect Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 150000007529 inorganic bases Chemical class 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 210000001821 langerhans cell Anatomy 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 125000003473 lipid group Chemical group 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 229940098779 methanesulfonic acid Drugs 0.000 description 1
- 229960005173 methiosulfonium chloride Drugs 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 229920005615 natural polymer Polymers 0.000 description 1
- 230000017066 negative regulation of growth Effects 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- IPCSVZSSVZVIGE-UHFFFAOYSA-N palmitic acid group Chemical group C(CCCCCCCCCCCCCCC)(=O)O IPCSVZSSVZVIGE-UHFFFAOYSA-N 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 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
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000009117 preventive therapy Methods 0.000 description 1
- 238000011324 primary prophylaxis Methods 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 238000002331 protein detection Methods 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 239000013074 reference sample Substances 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 238000011309 routine diagnosis Methods 0.000 description 1
- 229960004889 salicylic acid Drugs 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000003802 sputum Anatomy 0.000 description 1
- 208000024794 sputum Diseases 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 150000003462 sulfoxides Chemical class 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 238000012546 transfer 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
- XVQKZSLOGHBCET-INVHGPFASA-N tripalmitoyl-S-glyceryl-cysteinyl-seryl-serine Chemical compound CCCCCCCCCCCCCCCC(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O)CSCC(OC(=O)CCCCCCCCCCCCCCC)COC(=O)CCCCCCCCCCCCCCC XVQKZSLOGHBCET-INVHGPFASA-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
- 210000002700 urine Anatomy 0.000 description 1
- 229910052720 vanadium Inorganic materials 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- 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
- A61K35/14—Blood; Artificial blood
- A61K35/17—Lymphocytes; B-cells; T-cells; Natural killer cells; Interferon-activated or cytokine-activated lymphocytes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/11—T-cells, e.g. tumour infiltrating lymphocytes [TIL] or regulatory T [Treg] cells; Lymphokine-activated killer [LAK] cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/19—Dendritic cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/20—Cellular immunotherapy characterised by the effect or the function of the cells
- A61K40/24—Antigen-presenting cells [APC]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/40—Cellular immunotherapy characterised by antigens that are targeted or presented by cells of the immune system
- A61K40/41—Vertebrate antigens
- A61K40/42—Cancer antigens
- A61K40/4202—Receptors, cell surface antigens or cell surface determinants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
- C12N5/0634—Cells from the blood or the immune system
-
- 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
- C12N5/0634—Cells from the blood or the immune system
- C12N5/0636—T lymphocytes
- C12N5/0638—Cytotoxic T lymphocytes [CTL] or lymphokine activated killer cells [LAK]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/515—Animal cells
- A61K2039/5154—Antigen presenting cells [APCs], e.g. dendritic cells or macrophages
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/515—Animal cells
- A61K2039/5156—Animal cells expressing foreign proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2239/00—Indexing codes associated with cellular immunotherapy of group A61K40/00
- A61K2239/38—Indexing codes associated with cellular immunotherapy of group A61K40/00 characterised by the dose, timing or administration schedule
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2239/00—Indexing codes associated with cellular immunotherapy of group A61K40/00
- A61K2239/46—Indexing codes associated with cellular immunotherapy of group A61K40/00 characterised by the cancer treated
- A61K2239/55—Lung
-
- 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
- C12N2501/00—Active agents used in cell culture processes, e.g. differentation
- C12N2501/998—Proteins not provided for elsewhere
-
- 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
- C12N2510/00—Genetically modified cells
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Zoology (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Cell Biology (AREA)
- Wood Science & Technology (AREA)
- Pharmacology & Pharmacy (AREA)
- Hematology (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Developmental Biology & Embryology (AREA)
- Biophysics (AREA)
- Virology (AREA)
- Mycology (AREA)
- Oncology (AREA)
- Molecular Biology (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US26565709P | 2009-12-01 | 2009-12-01 | |
| US37143410P | 2010-08-06 | 2010-08-06 | |
| PCT/JP2010/006966 WO2011067920A1 (en) | 2009-12-01 | 2010-11-30 | Imp-3 oligopeptides and vaccines including the same |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2012006126A true MX2012006126A (es) | 2012-06-19 |
Family
ID=44114782
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2012006126A MX2012006126A (es) | 2009-12-01 | 2010-11-30 | Oligopeptidos imp-3 y vacunas que incluyen los mismos. |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US20120308590A1 (OSRAM) |
| EP (1) | EP2507256A4 (OSRAM) |
| JP (1) | JP2013511958A (OSRAM) |
| KR (1) | KR20120099106A (OSRAM) |
| CN (1) | CN102741271B (OSRAM) |
| AU (1) | AU2010327878B2 (OSRAM) |
| BR (1) | BR112012013139A2 (OSRAM) |
| CA (1) | CA2782271A1 (OSRAM) |
| IL (1) | IL219976A0 (OSRAM) |
| MX (1) | MX2012006126A (OSRAM) |
| RU (1) | RU2550695C2 (OSRAM) |
| SG (2) | SG181107A1 (OSRAM) |
| TW (1) | TW201124530A (OSRAM) |
| WO (1) | WO2011067920A1 (OSRAM) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20140138900A (ko) | 2012-03-09 | 2014-12-04 | 온코세라피 사이언스 가부시키가이샤 | 펩티드를 포함한 의약 조성물 |
| TWI627182B (zh) * | 2013-05-24 | 2018-06-21 | 腫瘤療法 科學股份有限公司 | 對於ｔｈ１細胞之ｉｍｐ－３抗原決定位胜肽及含此之疫苗 |
| CN111925431B (zh) * | 2014-08-04 | 2025-04-15 | 肿瘤疗法科学股份有限公司 | Koc1衍生的肽和包含它们的疫苗 |
| GB201603568D0 (en) * | 2016-03-01 | 2016-04-13 | Immatics Biotechnologies Gmbh | Efficient treatment options including peptides and combination of peptide and cell based medicaments for use in immunotherapy against urinary bladder cancer |
| RS63727B1 (sr) | 2016-03-16 | 2022-12-30 | Immatics Biotechnologies Gmbh | Transficirane t ćelije i t-ćelijski receptori za upotrebu u imunoterapiji protiv malignih tumora |
| GB201604494D0 (en) * | 2016-03-16 | 2016-04-27 | Immatics Biotechnologies Gmbh | Transfected T-Cells and T-Cell receptors for use in immunotherapy against cancers |
| GB201604490D0 (en) * | 2016-03-16 | 2016-04-27 | Immatics Biotechnologies Gmbh | Peptides combination of peptides for use in immunotherapy against cancers |
| HUE058717T2 (hu) | 2017-01-25 | 2022-09-28 | Ose Immunotherapeutics | Eljárás egy stabil emulzió elõállítására peptid szállításához |
| EP3727434A1 (en) * | 2017-12-23 | 2020-10-28 | Rubius Therapeutics, Inc. | Artificial antigen presenting cells and methods of use |
| CN114853847B (zh) | 2022-06-29 | 2022-09-27 | 中国农业大学 | 辣椒籽分离的寡肽ftle及其在预防或治疗癌症中的应用 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7579160B2 (en) * | 1998-03-18 | 2009-08-25 | Corixa Corporation | Methods for the detection of cervical cancer |
| EP1317275A1 (de) * | 2000-09-06 | 2003-06-11 | Müller, Friederike | Arzneimittel mit einer für das rna-bindende koc-protein kodierenden dna-sequenz, einem koc-protein oder einer dna-sequenz des koc-promotors |
| ES2459492T3 (es) * | 2005-02-25 | 2014-05-09 | Oncotherapy Science, Inc. | Vacunas de péptidos para cánceres de pulmón que expresan polipéptidos TTK, URLC10 o KOC1 |
| US10611818B2 (en) * | 2007-09-27 | 2020-04-07 | Agilent Technologies, Inc. | MHC multimers in tuberculosis diagnostics, vaccine and therapeutics |
| PL2172211T3 (pl) * | 2008-10-01 | 2015-05-29 | Immatics Biotechnologies Gmbh | Kompozycja związanych z guzem peptydów i związana z tym szczepionka przeciwrakowa do leczenia glejaka (GBM) i innych rodzajów raka |
-
2010
- 2010-11-26 TW TW099140933A patent/TW201124530A/zh unknown
- 2010-11-30 EP EP10834374.0A patent/EP2507256A4/en not_active Withdrawn
- 2010-11-30 KR KR1020127017018A patent/KR20120099106A/ko not_active Withdrawn
- 2010-11-30 US US13/513,120 patent/US20120308590A1/en not_active Abandoned
- 2010-11-30 MX MX2012006126A patent/MX2012006126A/es active IP Right Grant
- 2010-11-30 CA CA2782271A patent/CA2782271A1/en not_active Abandoned
- 2010-11-30 CN CN201080062874.XA patent/CN102741271B/zh not_active Expired - Fee Related
- 2010-11-30 AU AU2010327878A patent/AU2010327878B2/en not_active Ceased
- 2010-11-30 SG SG2012039277A patent/SG181107A1/en unknown
- 2010-11-30 JP JP2012524961A patent/JP2013511958A/ja active Pending
- 2010-11-30 RU RU2012127358/04A patent/RU2550695C2/ru not_active IP Right Cessation
- 2010-11-30 WO PCT/JP2010/006966 patent/WO2011067920A1/en not_active Ceased
- 2010-11-30 SG SG10201407944TA patent/SG10201407944TA/en unknown
- 2010-11-30 BR BR112012013139A patent/BR112012013139A2/pt not_active IP Right Cessation
-
2012
- 2012-05-24 IL IL219976A patent/IL219976A0/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| RU2012127358A (ru) | 2014-01-10 |
| RU2550695C2 (ru) | 2015-05-10 |
| SG181107A1 (en) | 2012-07-30 |
| JP2013511958A (ja) | 2013-04-11 |
| US20120308590A1 (en) | 2012-12-06 |
| EP2507256A1 (en) | 2012-10-10 |
| SG10201407944TA (en) | 2015-01-29 |
| WO2011067920A1 (en) | 2011-06-09 |
| CN102741271B (zh) | 2014-11-05 |
| KR20120099106A (ko) | 2012-09-06 |
| AU2010327878B2 (en) | 2014-11-20 |
| AU2010327878A1 (en) | 2012-06-21 |
| IL219976A0 (en) | 2012-07-31 |
| BR112012013139A2 (pt) | 2016-10-11 |
| CN102741271A (zh) | 2012-10-17 |
| CA2782271A1 (en) | 2011-06-09 |
| EP2507256A4 (en) | 2013-10-16 |
| TW201124530A (en) | 2011-07-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP2408912B1 (en) | Foxm1 peptides and vaccines containing the same | |
| RU2550695C2 (ru) | Олигопептиды imp-3 и содержащие их вакцины | |
| US8735361B2 (en) | C1ORF59 peptides and vaccines including the same | |
| US9745343B2 (en) | Method of inducing an immune response by administering WDRPUH epitope peptides | |
| WO2010070877A1 (en) | Elovl7 epitope peptides and vaccines containing the same | |
| AU2010216980B2 (en) | FOXM1 peptides and vaccines containing the same | |
| HK1240953A1 (en) | Wdrpuh epitope peptides and vaccines containing the same | |
| HK1165460A (en) | Foxm1 peptides and vaccines containing the same | |
| HK1165460B (en) | Foxm1 peptides and vaccines containing the same |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Grant or registration |