UA72426C2 - Human mutant interleukin-6, dna molecule coding it, vector, host cell, and also a method for obtaining and use of mutant il-6 for treatment of diseases with which il-6 has a pathogenic influence - Google Patents
Human mutant interleukin-6, dna molecule coding it, vector, host cell, and also a method for obtaining and use of mutant il-6 for treatment of diseases with which il-6 has a pathogenic influence Download PDFInfo
- Publication number
- UA72426C2 UA72426C2 UA98115904A UA98115904A UA72426C2 UA 72426 C2 UA72426 C2 UA 72426C2 UA 98115904 A UA98115904 A UA 98115904A UA 98115904 A UA98115904 A UA 98115904A UA 72426 C2 UA72426 C2 UA 72426C2
- Authority
- UA
- Ukraine
- Prior art keywords
- mutant
- human
- sequence
- interleukin
- fragment
- Prior art date
Links
- 201000010099 disease Diseases 0.000 title claims abstract description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title claims abstract description 6
- 230000001717 pathogenic effect Effects 0.000 title claims abstract description 4
- 241000282414 Homo sapiens Species 0.000 title claims description 57
- 108020004414 DNA Proteins 0.000 title claims description 24
- 238000000034 method Methods 0.000 title claims description 15
- 239000013598 vector Substances 0.000 title claims description 15
- 102000053602 DNA Human genes 0.000 title claims description 6
- 108090001005 Interleukin-6 Proteins 0.000 title abstract description 29
- 102000004889 Interleukin-6 Human genes 0.000 title description 26
- 229940100601 interleukin-6 Drugs 0.000 title description 26
- 108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 4
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract 2
- 230000035772 mutation Effects 0.000 claims description 21
- 230000000694 effects Effects 0.000 claims description 16
- 239000012634 fragment Substances 0.000 claims description 11
- 239000001963 growth medium Substances 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 2
- 231100000255 pathogenic effect Toxicity 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 2
- 239000004480 active ingredient Substances 0.000 claims 1
- 239000013256 coordination polymer Substances 0.000 claims 1
- 239000000945 filler Substances 0.000 claims 1
- 238000002955 isolation Methods 0.000 claims 1
- 229940126601 medicinal product Drugs 0.000 claims 1
- 206010035226 Plasma cell myeloma Diseases 0.000 abstract description 9
- 201000000050 myeloid neoplasm Diseases 0.000 abstract description 9
- 239000005557 antagonist Substances 0.000 abstract description 8
- 239000003814 drug Substances 0.000 abstract description 4
- 208000023275 Autoimmune disease Diseases 0.000 abstract description 3
- 208000001132 Osteoporosis Diseases 0.000 abstract description 3
- 208000007452 Plasmacytoma Diseases 0.000 abstract description 3
- 230000001613 neoplastic effect Effects 0.000 abstract description 3
- 238000002560 therapeutic procedure Methods 0.000 abstract description 2
- 230000003389 potentiating effect Effects 0.000 abstract 1
- 108090000623 proteins and genes Proteins 0.000 description 39
- 230000027455 binding Effects 0.000 description 38
- 210000004027 cell Anatomy 0.000 description 31
- 102000004169 proteins and genes Human genes 0.000 description 30
- 235000018102 proteins Nutrition 0.000 description 29
- 230000003993 interaction Effects 0.000 description 26
- 102000005962 receptors Human genes 0.000 description 25
- 108020003175 receptors Proteins 0.000 description 25
- 150000001413 amino acids Chemical class 0.000 description 21
- 239000003446 ligand Substances 0.000 description 18
- 235000001014 amino acid Nutrition 0.000 description 17
- 230000014509 gene expression Effects 0.000 description 14
- 102000015696 Interleukins Human genes 0.000 description 12
- 108010063738 Interleukins Proteins 0.000 description 12
- 108020004707 nucleic acids Proteins 0.000 description 12
- 102000039446 nucleic acids Human genes 0.000 description 12
- 150000007523 nucleic acids Chemical class 0.000 description 11
- 102000008300 Mutant Proteins Human genes 0.000 description 10
- 108010021466 Mutant Proteins Proteins 0.000 description 10
- 230000035755 proliferation Effects 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 7
- 230000007423 decrease Effects 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 108090000765 processed proteins & peptides Proteins 0.000 description 6
- 102000018997 Growth Hormone Human genes 0.000 description 5
- 108010051696 Growth Hormone Proteins 0.000 description 5
- 125000000539 amino acid group Chemical group 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 239000000122 growth hormone Substances 0.000 description 5
- 210000005260 human cell Anatomy 0.000 description 5
- 229920001184 polypeptide Polymers 0.000 description 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 5
- 238000006467 substitution reaction Methods 0.000 description 5
- 102000014702 Haptoglobin Human genes 0.000 description 4
- 108050005077 Haptoglobin Proteins 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 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 4
- 235000003704 aspartic acid Nutrition 0.000 description 4
- 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 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 4
- 230000000977 initiatory effect Effects 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 102100022111 rRNA-processing protein FCF1 homolog Human genes 0.000 description 4
- 241000894007 species Species 0.000 description 4
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 102220484130 Testis-specific serine/threonine-protein kinase 6_K54M_mutation Human genes 0.000 description 3
- 230000000692 anti-sense effect Effects 0.000 description 3
- 230000032823 cell division Effects 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 229940047122 interleukins Drugs 0.000 description 3
- 210000003205 muscle Anatomy 0.000 description 3
- 239000013600 plasmid vector Substances 0.000 description 3
- 239000002464 receptor antagonist Substances 0.000 description 3
- 229940044551 receptor antagonist Drugs 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 102000003839 Human Proteins Human genes 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000001886 ciliary effect Effects 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 230000003394 haemopoietic effect Effects 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 210000000663 muscle cell Anatomy 0.000 description 2
- 230000008506 pathogenesis Effects 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000004224 protection Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 102000034285 signal transducing proteins Human genes 0.000 description 2
- 108091006024 signal transducing proteins Proteins 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- IJJWOSAXNHWBPR-HUBLWGQQSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-n-(6-hydrazinyl-6-oxohexyl)pentanamide Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)NCCCCCC(=O)NN)SC[C@@H]21 IJJWOSAXNHWBPR-HUBLWGQQSA-N 0.000 description 1
- 206010048998 Acute phase reaction Diseases 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102100034613 Annexin A2 Human genes 0.000 description 1
- 108090000668 Annexin A2 Proteins 0.000 description 1
- 108090000669 Annexin A4 Proteins 0.000 description 1
- 102100034612 Annexin A4 Human genes 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000195940 Bryophyta Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000214054 Equine rhinitis A virus Species 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241000152447 Hades Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101001078385 Homo sapiens Haptoglobin Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000003815 Interleukin-11 Human genes 0.000 description 1
- 108090000177 Interleukin-11 Proteins 0.000 description 1
- 241001026509 Kata Species 0.000 description 1
- 102000004058 Leukemia inhibitory factor Human genes 0.000 description 1
- 108090000581 Leukemia inhibitory factor Proteins 0.000 description 1
- 241000234435 Lilium Species 0.000 description 1
- 241001436793 Meru Species 0.000 description 1
- 244000004005 Nypa fruticans Species 0.000 description 1
- 235000005305 Nypa fruticans Nutrition 0.000 description 1
- 102000004140 Oncostatin M Human genes 0.000 description 1
- 108090000630 Oncostatin M Proteins 0.000 description 1
- 241001631646 Papillomaviridae Species 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 244000111306 Torreya nucifera Species 0.000 description 1
- 235000006732 Torreya nucifera Nutrition 0.000 description 1
- 101710175177 Very-long-chain 3-oxoacyl-CoA reductase Proteins 0.000 description 1
- 101710187138 Very-long-chain 3-oxoacyl-CoA reductase-A Proteins 0.000 description 1
- 101710187143 Very-long-chain 3-oxoacyl-CoA reductase-B Proteins 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000004658 acute-phase response Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 208000027697 autoimmune lymphoproliferative syndrome due to CTLA4 haploinsuffiency Diseases 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 102000003675 cytokine receptors Human genes 0.000 description 1
- 108010057085 cytokine receptors Proteins 0.000 description 1
- UQHKFADEQIVWID-UHFFFAOYSA-N cytokinin Natural products C1=NC=2C(NCC=C(CO)C)=NC=NC=2N1C1CC(O)C(CO)O1 UQHKFADEQIVWID-UHFFFAOYSA-N 0.000 description 1
- 239000004062 cytokinin Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 230000011132 hemopoiesis Effects 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 235000012907 honey Nutrition 0.000 description 1
- 102000050796 human HP Human genes 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229940074383 interleukin-11 Drugs 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 125000003588 lysine group Chemical class [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 1
- 238000013507 mapping Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 210000003593 megakaryocyte Anatomy 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- SUJOIPVTNUVDCB-UHFFFAOYSA-N mutactin Natural products CC1=CC(O)=C2C(=O)CC(O)CC2=C1C1=CC(O)=CC(=O)O1 SUJOIPVTNUVDCB-UHFFFAOYSA-N 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 239000003076 neurotropic agent Substances 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 102220020942 rs80357327 Human genes 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- -1 tin nucleic acid Chemical class 0.000 description 1
- 238000001890 transfection 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
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 235000014101 wine Nutrition 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/5412—IL-6
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Physical Education & Sports Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Rheumatology (AREA)
- Toxicology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Compounds Of Unknown Constitution (AREA)
- Details Of Television Scanning (AREA)
- Diaphragms For Electromechanical Transducers (AREA)
- Amplifiers (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CA002251355A CA2251355C (en) | 1996-04-09 | 1996-04-09 | Il-6 mutein |
CN96180247A CN1131309C (zh) | 1996-04-09 | 1996-04-09 | 白细胞介素-6突变蛋白 |
PCT/EP1996/001506 WO1997038103A1 (en) | 1996-04-09 | 1996-04-09 | Il-6 mutein |
Publications (1)
Publication Number | Publication Date |
---|---|
UA72426C2 true UA72426C2 (en) | 2005-03-15 |
Family
ID=27170853
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
UA98115904A UA72426C2 (en) | 1996-04-09 | 1996-09-04 | Human mutant interleukin-6, dna molecule coding it, vector, host cell, and also a method for obtaining and use of mutant il-6 for treatment of diseases with which il-6 has a pathogenic influence |
Country Status (19)
Country | Link |
---|---|
US (1) | US6280975B1 (pt) |
EP (1) | EP0907737B1 (pt) |
JP (1) | JP4189866B2 (pt) |
CN (1) | CN1131309C (pt) |
AT (1) | ATE291087T1 (pt) |
AU (1) | AU728267B2 (pt) |
BR (1) | BR9708648B1 (pt) |
CA (1) | CA2251355C (pt) |
DE (1) | DE69634497T2 (pt) |
DK (1) | DK0907737T3 (pt) |
EA (1) | EA000852B1 (pt) |
ES (1) | ES2238690T3 (pt) |
FI (1) | FI982198A0 (pt) |
HK (1) | HK1019770A1 (pt) |
IL (1) | IL126484A0 (pt) |
NO (1) | NO322479B1 (pt) |
PT (1) | PT907737E (pt) |
UA (1) | UA72426C2 (pt) |
WO (2) | WO1997038103A1 (pt) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
PT1074268E (pt) | 1998-03-17 | 2008-02-28 | Chugai Pharmaceutical Co Ltd | Agentes profilácticos ou terapêuticos para doenças intestinais inflamatórias contendo anticorpos antagonistas do receptor il-6 |
KR20060119412A (ko) * | 2005-05-20 | 2006-11-24 | 아주대학교산학협력단 | IL-6 발현 억제를 위한 siRNA 및 이를 함유하는조성물 |
US8522915B2 (en) * | 2007-12-19 | 2013-09-03 | Westerngeco L.L.C. | Method and system for selecting parameters of a seismic source array |
CN102101885B (zh) * | 2010-09-01 | 2013-06-05 | 南京发士达生物科技有限公司 | 低诱导抑制性t细胞的人白细胞介素ⅱ突变体及其用途 |
-
1996
- 1996-04-09 EP EP96914885A patent/EP0907737B1/en not_active Expired - Lifetime
- 1996-04-09 AT AT96914885T patent/ATE291087T1/de active
- 1996-04-09 US US09/155,941 patent/US6280975B1/en not_active Expired - Lifetime
- 1996-04-09 AU AU56864/96A patent/AU728267B2/en not_active Expired
- 1996-04-09 JP JP53576597A patent/JP4189866B2/ja not_active Expired - Lifetime
- 1996-04-09 EA EA199800914A patent/EA000852B1/ru not_active IP Right Cessation
- 1996-04-09 ES ES96914885T patent/ES2238690T3/es not_active Expired - Lifetime
- 1996-04-09 CA CA002251355A patent/CA2251355C/en not_active Expired - Lifetime
- 1996-04-09 WO PCT/EP1996/001506 patent/WO1997038103A1/en active IP Right Grant
- 1996-04-09 DE DE69634497T patent/DE69634497T2/de not_active Expired - Lifetime
- 1996-04-09 PT PT96914885T patent/PT907737E/pt unknown
- 1996-04-09 DK DK96914885T patent/DK0907737T3/da active
- 1996-04-09 CN CN96180247A patent/CN1131309C/zh not_active Expired - Lifetime
- 1996-09-04 UA UA98115904A patent/UA72426C2/uk unknown
-
1997
- 1997-04-08 IL IL12648497A patent/IL126484A0/xx active IP Right Grant
- 1997-04-08 WO PCT/EP1997/001736 patent/WO1997038104A1/en active Application Filing
- 1997-04-08 BR BRPI9708648-7A patent/BR9708648B1/pt not_active IP Right Cessation
-
1998
- 1998-10-08 NO NO19984697A patent/NO322479B1/no not_active IP Right Cessation
- 1998-10-09 FI FI982198A patent/FI982198A0/fi not_active Application Discontinuation
-
1999
- 1999-11-02 HK HK99104952A patent/HK1019770A1/xx not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
EA000852B1 (ru) | 2000-06-26 |
IL126484A0 (en) | 1999-08-17 |
CA2251355C (en) | 2009-06-09 |
JP2000508164A (ja) | 2000-07-04 |
NO984697L (no) | 1998-10-08 |
FI982198A (fi) | 1998-10-09 |
NO984697D0 (no) | 1998-10-08 |
WO1997038103A1 (en) | 1997-10-16 |
CN1131309C (zh) | 2003-12-17 |
AU728267B2 (en) | 2001-01-04 |
FI982198A0 (fi) | 1998-10-09 |
US6280975B1 (en) | 2001-08-28 |
JP4189866B2 (ja) | 2008-12-03 |
CN1216063A (zh) | 1999-05-05 |
DE69634497D1 (de) | 2005-04-21 |
CA2251355A1 (en) | 1997-10-16 |
ES2238690T3 (es) | 2005-09-01 |
DK0907737T3 (da) | 2005-06-27 |
HK1019770A1 (en) | 2000-02-25 |
EP0907737B1 (en) | 2005-03-16 |
EA199800914A1 (ru) | 1999-04-29 |
ATE291087T1 (de) | 2005-04-15 |
DE69634497T2 (de) | 2006-01-26 |
EP0907737A1 (en) | 1999-04-14 |
BR9708648A (pt) | 1999-08-03 |
WO1997038104A1 (en) | 1997-10-16 |
AU5686496A (en) | 1997-10-29 |
BR9708648B1 (pt) | 2011-02-08 |
PT907737E (pt) | 2005-05-31 |
NO322479B1 (no) | 2006-10-09 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Wuyts et al. | Differential usage of the CXC chemokine receptors 1 and 2 by interleukin‐8, granulocyte chemotactic protein‐2 and epithelial‐cell‐derived neutrophil attractant‐78 | |
Van Damme et al. | Identification of the human 26-kD protein, interferon beta 2 (IFN-beta 2), as a B cell hybridoma/plasmacytoma growth factor induced by interleukin 1 and tumor necrosis factor. | |
EP1553182B1 (en) | Regulated genes and uses thereof | |
EP1097173B1 (en) | The use of peptides of il-2 and derivatives thereof as therapeutic agents | |
US5733730A (en) | Telomere repeat binding factor and diagnostic and therapeutic use thereof | |
Qian et al. | Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells. | |
Kume et al. | Probability that the commitment of murine erythroleukemia cell differentiation is determined by the c-myc level | |
US7956161B2 (en) | Interferons of rhesus and cynomolgus origin and uses thereof | |
Michishita et al. | Induction of tumor necrosis factor-alpha and its receptors during differentiation in myeloid leukemic cells along the monocytic pathway. A possible regulatory mechanism for TNF-alpha production. | |
US5217864A (en) | Replication initiator protein complex and methods of use thereof | |
Lowe et al. | Chimeric proteins define variable and essential regions of Ha-ras-encoded protein. | |
ZA200401001B (en) | Bv8 nucleic acids and polypeptides with mitogenic activity. | |
UA72426C2 (en) | Human mutant interleukin-6, dna molecule coding it, vector, host cell, and also a method for obtaining and use of mutant il-6 for treatment of diseases with which il-6 has a pathogenic influence | |
US7704490B2 (en) | Method for inducing selected useful activities of IL-2 in a patient with peptides from IL-2 | |
Vosatka et al. | Dynamic interactions of c‐fos protein in serum‐stimulated 3T3 cells | |
Clark-Lewis et al. | Molecular structure and biological activities of P cell-stimulating factor (interleukin 3) | |
Hughes et al. | Heterodimerization with c-Fos is not required for cell transformation of chicken embryo fibroblasts by Jun | |
US20070048302A1 (en) | Peptides of IL-2 | |
Van Damme et al. | IDENTIFICATION OF THE HUMAN 26-kD PROTEIN, INTERFERON 02 (IFN-N2), AS AB CELL HYBRIDOMA/PLASMACYTOMA GROWTH FACTOR INDUCED BY INTERLEUKIN 1 AND TUMOR NECROSIS FACTOR | |
WO2020162582A1 (en) | Methods of treating non-virally-induced cancers | |
Cusi et al. | Harlequin granulocyte-colony stimulating factor interleukin 6 molecules with bifunctional and antagonistic activities | |
CN117715648A (zh) | 靶向uPAR的抗原识别受体和其用途 | |
Baier et al. | Interleukin-16 for the gene therapy of HIV infection | |
JPH10316582A (ja) | 血管細胞調節剤 | |
ROBERTS | Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor f3 on endothelial cells |