NO330682B1 - Fremgangsmate for fremstilling av et fysiologisk, aktivt IL-18 polypeptid - Google Patents
Fremgangsmate for fremstilling av et fysiologisk, aktivt IL-18 polypeptid Download PDFInfo
- Publication number
- NO330682B1 NO330682B1 NO20026002A NO20026002A NO330682B1 NO 330682 B1 NO330682 B1 NO 330682B1 NO 20026002 A NO20026002 A NO 20026002A NO 20026002 A NO20026002 A NO 20026002A NO 330682 B1 NO330682 B1 NO 330682B1
- Authority
- NO
- Norway
- Prior art keywords
- caspase
- pro
- polypeptide
- cells
- human
- Prior art date
Links
- 102000003810 Interleukin-18 Human genes 0.000 title claims description 77
- 108090000171 Interleukin-18 Proteins 0.000 title claims description 77
- 238000004519 manufacturing process Methods 0.000 title description 13
- 101710090333 Caspase-5 Proteins 0.000 claims description 66
- 101710090338 Caspase-4 Proteins 0.000 claims description 65
- 102100038916 Caspase-5 Human genes 0.000 claims description 65
- 102100025597 Caspase-4 Human genes 0.000 claims description 64
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 54
- 239000002243 precursor Substances 0.000 claims description 50
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 47
- 229920001184 polypeptide Polymers 0.000 claims description 45
- 238000000034 method Methods 0.000 claims description 34
- 101000960954 Homo sapiens Interleukin-18 Proteins 0.000 claims description 14
- 102000043959 human IL18 Human genes 0.000 claims description 14
- 230000004186 co-expression Effects 0.000 claims description 13
- 238000000746 purification Methods 0.000 claims description 10
- 230000008569 process Effects 0.000 claims description 7
- 230000002950 deficient Effects 0.000 claims description 6
- 108091029795 Intergenic region Proteins 0.000 claims description 3
- 239000013604 expression vector Substances 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 210000004027 cell Anatomy 0.000 description 59
- 108090000623 proteins and genes Proteins 0.000 description 43
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 28
- 230000014509 gene expression Effects 0.000 description 28
- 102000004169 proteins and genes Human genes 0.000 description 27
- 235000018102 proteins Nutrition 0.000 description 26
- 150000001413 amino acids Chemical group 0.000 description 24
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 24
- 238000001727 in vivo Methods 0.000 description 23
- 241000588724 Escherichia coli Species 0.000 description 22
- 230000004913 activation Effects 0.000 description 22
- 102000044159 Ubiquitin Human genes 0.000 description 21
- 108090000848 Ubiquitin Proteins 0.000 description 21
- 102000004190 Enzymes Human genes 0.000 description 18
- 108090000790 Enzymes Proteins 0.000 description 18
- 239000000872 buffer Substances 0.000 description 18
- 239000013598 vector Substances 0.000 description 17
- 108020004414 DNA Proteins 0.000 description 16
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 15
- 230000006698 induction Effects 0.000 description 15
- 230000004927 fusion Effects 0.000 description 14
- 239000011780 sodium chloride Substances 0.000 description 14
- 239000006228 supernatant Substances 0.000 description 14
- 102000018390 Ubiquitin-Specific Proteases Human genes 0.000 description 13
- 108010066496 Ubiquitin-Specific Proteases Proteins 0.000 description 12
- 235000001014 amino acid Nutrition 0.000 description 12
- 238000003776 cleavage reaction Methods 0.000 description 12
- 239000006166 lysate Substances 0.000 description 12
- 238000012545 processing Methods 0.000 description 12
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 11
- 229920000936 Agarose Polymers 0.000 description 11
- 239000007995 HEPES buffer Substances 0.000 description 11
- 230000000694 effects Effects 0.000 description 10
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 10
- 230000007017 scission Effects 0.000 description 10
- 238000013518 transcription Methods 0.000 description 10
- 230000035897 transcription Effects 0.000 description 10
- 102100037850 Interferon gamma Human genes 0.000 description 9
- 108010074328 Interferon-gamma Proteins 0.000 description 9
- 230000001939 inductive effect Effects 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 8
- 238000013519 translation Methods 0.000 description 8
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 8
- 102000035195 Peptidases Human genes 0.000 description 7
- 108091005804 Peptidases Proteins 0.000 description 7
- 239000004365 Protease Substances 0.000 description 7
- 210000005260 human cell Anatomy 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 6
- 239000007989 BIS-Tris Propane buffer Substances 0.000 description 6
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 101710137500 T7 RNA polymerase Proteins 0.000 description 6
- HHKZCCWKTZRCCL-UHFFFAOYSA-N bis-tris propane Chemical compound OCC(CO)(CO)NCCCNC(CO)(CO)CO HHKZCCWKTZRCCL-UHFFFAOYSA-N 0.000 description 6
- 230000002759 chromosomal effect Effects 0.000 description 6
- 230000014621 translational initiation Effects 0.000 description 6
- 101000933112 Homo sapiens Caspase-4 Proteins 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 239000012505 Superdex™ Substances 0.000 description 5
- 230000003213 activating effect Effects 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 238000004587 chromatography analysis Methods 0.000 description 5
- 239000013613 expression plasmid Substances 0.000 description 5
- 239000000833 heterodimer Substances 0.000 description 5
- 102000051832 human CASP4 Human genes 0.000 description 5
- 239000012535 impurity Substances 0.000 description 5
- 230000003834 intracellular effect Effects 0.000 description 5
- 239000012139 lysis buffer Substances 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 150000007523 nucleic acids Chemical group 0.000 description 5
- 239000008188 pellet Substances 0.000 description 5
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 4
- 102000004127 Cytokines Human genes 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000011541 reaction mixture Substances 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 4
- 241000701867 Enterobacteria phage T7 Species 0.000 description 3
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 3
- 101000741072 Homo sapiens Caspase-5 Proteins 0.000 description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 102000050388 human CASP5 Human genes 0.000 description 3
- 230000001320 lysogenic effect Effects 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000001742 protein purification Methods 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 238000004007 reversed phase HPLC Methods 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000002002 slurry Substances 0.000 description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 108010076667 Caspases Proteins 0.000 description 2
- 102000011727 Caspases Human genes 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 101710180319 Protease 1 Proteins 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 0.000 description 2
- 101710137710 Thioesterase 1/protease 1/lysophospholipase L1 Proteins 0.000 description 2
- 238000005377 adsorption chromatography Methods 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 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 2
- 238000004113 cell culture Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 239000012468 concentrated sample Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 238000001641 gel filtration chromatography Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 238000001155 isoelectric focusing Methods 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 238000010979 pH adjustment Methods 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 239000008177 pharmaceutical agent Substances 0.000 description 2
- 238000006722 reduction reaction Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 2
- FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
- 238000005185 salting out Methods 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108090000426 Caspase-1 Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 101100007328 Cocos nucifera COS-1 gene Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000000589 Interleukin-1 Human genes 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 108010054278 Lac Repressors Proteins 0.000 description 1
- 239000006391 Luria-Bertani Medium Substances 0.000 description 1
- 108090000143 Mouse Proteins Proteins 0.000 description 1
- 101100427359 Mus musculus Usp4 gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241001460678 Napo <wasp> Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 1
- 101900335766 Saccharomyces cerevisiae Ubiquitin Proteins 0.000 description 1
- 210000000447 Th1 cell Anatomy 0.000 description 1
- 102000005918 Ubiquitin Thiolesterase Human genes 0.000 description 1
- 108010005656 Ubiquitin Thiolesterase Proteins 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- MGSKVZWGBWPBTF-UHFFFAOYSA-N aebsf Chemical compound NCCC1=CC=C(S(F)(=O)=O)C=C1 MGSKVZWGBWPBTF-UHFFFAOYSA-N 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 229940088623 biologically active substance Drugs 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- UUVBYOGFRMMMQL-UHFFFAOYSA-N calcium;phosphoric acid Chemical compound [Ca].OP(O)(O)=O UUVBYOGFRMMMQL-UHFFFAOYSA-N 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 210000003321 cartilage cell Anatomy 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000009504 deubiquitination Effects 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 230000014828 interferon-gamma production Effects 0.000 description 1
- 210000002570 interstitial cell Anatomy 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 210000003757 neuroblast Anatomy 0.000 description 1
- 108010091212 pepstatin Proteins 0.000 description 1
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000000754 repressing effect Effects 0.000 description 1
- 229940102127 rubidium chloride Drugs 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 210000004988 splenocyte Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- 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]
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Wood Science & Technology (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Engineering & Computer Science (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US21183200P | 2000-06-15 | 2000-06-15 | |
| US22412800P | 2000-08-10 | 2000-08-10 | |
| US26492301P | 2001-01-20 | 2001-01-20 | |
| PCT/US2001/018804 WO2001098455A2 (en) | 2000-06-15 | 2001-06-11 | Method for preparing a physiologically active il-18 polypeptide |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO20026002D0 NO20026002D0 (no) | 2002-12-13 |
| NO20026002L NO20026002L (no) | 2003-02-12 |
| NO330682B1 true NO330682B1 (no) | 2011-06-06 |
Family
ID=27395664
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO20026002A NO330682B1 (no) | 2000-06-15 | 2002-12-13 | Fremgangsmate for fremstilling av et fysiologisk, aktivt IL-18 polypeptid |
Country Status (24)
| Country | Link |
|---|---|
| US (2) | US7186528B2 (de) |
| EP (1) | EP1292697B1 (de) |
| JP (1) | JP5121109B2 (de) |
| KR (1) | KR20030022144A (de) |
| CN (1) | CN100390281C (de) |
| AR (1) | AR033979A1 (de) |
| AT (1) | ATE437234T1 (de) |
| AU (2) | AU2001280442B2 (de) |
| BR (1) | BR0111692A (de) |
| CA (1) | CA2412730C (de) |
| CZ (1) | CZ20024085A3 (de) |
| DE (1) | DE60139316D1 (de) |
| DK (1) | DK1292697T3 (de) |
| ES (1) | ES2329875T3 (de) |
| HU (1) | HUP0501002A3 (de) |
| IL (2) | IL153422A0 (de) |
| MX (1) | MXPA02012292A (de) |
| MY (1) | MY136526A (de) |
| NO (1) | NO330682B1 (de) |
| NZ (1) | NZ522845A (de) |
| PL (2) | PL208592B1 (de) |
| PT (1) | PT1292697E (de) |
| SI (1) | SI1292697T1 (de) |
| WO (1) | WO2001098455A2 (de) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SK12942002A3 (sk) * | 2000-02-10 | 2003-05-02 | Abbott Laboratories | Protilátky viažuce ľudský interleukín-18, spôsoby ich výroby a použitia |
| EP1613274B1 (de) | 2003-04-15 | 2010-03-03 | GlaxoSmithKline LLC | Humane il-18 substitutionsmutanten und deren konjugate |
| ATE495189T1 (de) | 2003-08-15 | 2011-01-15 | Univ Florida | Die identifikation von polynukleotiden von porphyromonas gingivalis-virulenz zur diagnose, behandlung und beobachtung von periodontalerkrankungen |
| US7968684B2 (en) * | 2003-11-12 | 2011-06-28 | Abbott Laboratories | IL-18 binding proteins |
| CA2545024A1 (en) * | 2003-11-24 | 2005-06-02 | Novo Nordisk A/S | Fusion proteins and methods of cleavage of such proteins |
| ATE526057T1 (de) * | 2004-08-20 | 2011-10-15 | Glaxosmithkline Llc | Wundheilung durch verabreichung von menschlichem il-18 |
| US20100061958A1 (en) | 2006-09-14 | 2010-03-11 | The Trustees Of The University Of Pennsylvania | Modulation of Regulatory T Cells by Human IL-18 |
| AR065803A1 (es) * | 2007-03-23 | 2009-07-01 | Smithkline Beecham Corp | Uso de un polipeptido de il- 18 humana y un anticuerpo anti- cd para preparar unmedicamento |
| US11219672B2 (en) | 2014-08-07 | 2022-01-11 | Haruki Okamura | Therapeutic agent for cancer which comprises combination of IL-18 and molecule-targeting antibody |
| JP2019023165A (ja) * | 2015-12-11 | 2019-02-14 | 国立大学法人京都大学 | インターロイキン−１８活性阻害剤 |
| JP7795181B2 (ja) | 2017-09-06 | 2026-01-07 | イェール ユニバーシティー | インターロイキン－１８バリアントとその利用法 |
| KR20200080749A (ko) * | 2018-12-27 | 2020-07-07 | 주식회사 폴루스 | N-말단의 메티오닌이 절단된 목적 단백질 발현용 유전자 발현 카세트 및 이를 이용하여 n-말단의 메티오닌이 절단된 목적 단백질을 생산하는 방법 |
| AU2023226512A1 (en) | 2022-02-23 | 2024-08-29 | Bright Peak Therapeutics Ag | Immune antigen specific il-18 immunocytokines and uses thereof |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6204261B1 (en) * | 1995-12-20 | 2001-03-20 | Vertex Pharmaceuticals Incorporated | Inhibitors of interleukin-1β Converting enzyme inhibitors |
| US5985863A (en) * | 1996-09-12 | 1999-11-16 | Vertex Pharmaceuticals, Inc. | Compositions and methods for decreasing IGIF and IFN-γ production by administering an ICE inhibitor |
| US5192324A (en) | 1982-02-18 | 1993-03-09 | Howmedica Inc. | Bone prosthesis with porous coating |
| EP0324789B1 (de) * | 1986-10-02 | 2003-08-20 | Massachusetts Institute Of Technology | Verfahren zur regulierung der metabolischen stabilität von proteinen |
| US5212058A (en) | 1990-05-09 | 1993-05-18 | Massachusetts Institute Of Technology | Nucleic acid encoding ubiquitin-specific proteases |
| ES2071315T3 (es) | 1990-05-09 | 1995-06-16 | Massachusetts Inst Technology | Proteasa especifica de ubiquitina. |
| US5914254A (en) * | 1993-08-02 | 1999-06-22 | Celtrix Pharmaceuticals, Inc. | Expression of fusion polypeptides transported out of the cytoplasm without leader sequences |
| US6110701A (en) | 1994-04-08 | 2000-08-29 | Merck Frosst Canada & Co. | DNA encoding precursor of interleukin-1β converting enzyme--related cysteine proteinase II (ICErel -II) |
| US5552536A (en) | 1994-04-08 | 1996-09-03 | Merck Frosst Canada, Inc. | DNA encoding precursor of interleukin-1 beta converting enzyme - related cysteine proteinase III (ice rel-III) |
| DE69519454T2 (de) | 1994-07-14 | 2001-05-03 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo, Okayama | Protein, das Interferon-Gamma Herstellung induziert und monoklonaler Antikörper dagegen |
| JP2724987B2 (ja) | 1994-11-15 | 1998-03-09 | 株式会社林原生物化学研究所 | インターフェロン−γの産生を誘導するポリペプチド |
| TW581771B (en) | 1994-11-15 | 2004-04-01 | Hayashibara Biochem Lab | Recombinant production of a polypeptide for inducing interferon-gamma production, and monoclonal antibody against the polypeptide |
| US6074050A (en) | 1997-12-03 | 2000-06-13 | Hewlett-Packard Company | Method and apparatus for venting an ink container |
| CA2238885A1 (en) | 1995-12-29 | 1997-07-10 | Incyte Pharmaceuticals, Inc. | Nucleic acids encoding interferon gamma inducing factor-2 |
| JPH1080270A (ja) * | 1996-07-19 | 1998-03-31 | Hayashibara Biochem Lab Inc | ポリペプチドをプロセッシングする酵素 |
| TW515843B (en) * | 1996-07-25 | 2003-01-01 | Hayashibara Biochem Lab | Process for producing an active polypeptide inducing interferon-γ production |
| JP4010606B2 (ja) * | 1996-07-25 | 2007-11-21 | 株式会社林原生物化学研究所 | ポリペプチドの製造方法 |
| US6054487A (en) * | 1997-03-18 | 2000-04-25 | Basf Aktiengesellschaft | Methods and compositions for modulating responsiveness to corticosteroids |
| WO1999037793A1 (en) * | 1998-01-23 | 1999-07-29 | Novo Nordisk A/S | Process for making desired polypeptides in yeast |
-
2001
- 2001-06-11 PL PL387774A patent/PL208592B1/pl not_active IP Right Cessation
- 2001-06-11 AU AU2001280442A patent/AU2001280442B2/en not_active Ceased
- 2001-06-11 PL PL01366134A patent/PL366134A1/xx not_active Application Discontinuation
- 2001-06-11 DK DK01958830T patent/DK1292697T3/da active
- 2001-06-11 NZ NZ522845A patent/NZ522845A/en not_active IP Right Cessation
- 2001-06-11 US US10/311,491 patent/US7186528B2/en not_active Expired - Lifetime
- 2001-06-11 PT PT01958830T patent/PT1292697E/pt unknown
- 2001-06-11 CZ CZ20024085A patent/CZ20024085A3/cs unknown
- 2001-06-11 KR KR1020027016834A patent/KR20030022144A/ko not_active Ceased
- 2001-06-11 WO PCT/US2001/018804 patent/WO2001098455A2/en not_active Ceased
- 2001-06-11 IL IL15342201A patent/IL153422A0/xx active IP Right Grant
- 2001-06-11 SI SI200130942T patent/SI1292697T1/sl unknown
- 2001-06-11 BR BR0111692-4A patent/BR0111692A/pt not_active IP Right Cessation
- 2001-06-11 DE DE60139316T patent/DE60139316D1/de not_active Expired - Lifetime
- 2001-06-11 EP EP01958830A patent/EP1292697B1/de not_active Expired - Lifetime
- 2001-06-11 ES ES01958830T patent/ES2329875T3/es not_active Expired - Lifetime
- 2001-06-11 AT AT01958830T patent/ATE437234T1/de active
- 2001-06-11 HU HU0501002A patent/HUP0501002A3/hu unknown
- 2001-06-11 CN CNB018112781A patent/CN100390281C/zh not_active Expired - Fee Related
- 2001-06-11 JP JP2002504604A patent/JP5121109B2/ja not_active Expired - Lifetime
- 2001-06-11 MX MXPA02012292A patent/MXPA02012292A/es active IP Right Grant
- 2001-06-11 CA CA2412730A patent/CA2412730C/en not_active Expired - Lifetime
- 2001-06-11 AU AU8044201A patent/AU8044201A/xx active Pending
- 2001-06-13 AR ARP010102818A patent/AR033979A1/es active IP Right Grant
- 2001-06-14 MY MYPI20012804A patent/MY136526A/en unknown
-
2002
- 2002-12-12 IL IL153422A patent/IL153422A/en not_active IP Right Cessation
- 2002-12-13 NO NO20026002A patent/NO330682B1/no not_active IP Right Cessation
-
2006
- 2006-04-11 US US11/402,187 patent/US7442526B2/en not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN102239183B (zh) | 大量分泌的蛋白的筛选和它们作为融合配偶体在重组蛋白制备中应用 | |
| CA2449747C (en) | Use of fkbp chaperones as expression tool | |
| KR100682185B1 (ko) | 생물학적 활성분자의 제조 | |
| JP4504014B2 (ja) | インスリン分泌性ｇｌｐ−１（７−３６）ポリペプチドおよび／またはｇｌｐ−１類似体を生成する方法 | |
| US7442526B2 (en) | Method for preparing a physiologically active IL-18 polypeptide | |
| KR20080030551A (ko) | 융합 단백질의 자가단백질분해성 절단에 의한 재조합단백질 생산 | |
| KR20130059404A (ko) | 원핵생물 발현 구축물 | |
| AU2001280442A1 (en) | Method for preparing a physiologically active IL-18 polypeptide | |
| KR20100086717A (ko) | 대장균에서 외래단백질을 분비 생산하는 방법 | |
| CN109136209B (zh) | 肠激酶轻链突变体及其应用 | |
| RU2453604C1 (ru) | Гибридный белок (варианты), штамм бактерий escherichia coli - продуцент гибридного белка (варианты) и способ получения безметионинового интерферона альфа-2 человека | |
| RU2441072C1 (ru) | ГИБРИДНЫЙ БЕЛОК, ШТАММ БАКТЕРИЙ ESCHERICHIA COLI - ПРОДУЦЕНТ ГИБРИДНОГО БЕЛКА И СПОСОБ ПОЛУЧЕНИЯ БЕЗМЕТИОНИНОВОГО ИНТЕРФЕРОНА АЛЬФА-2b ЧЕЛОВЕКА ИЗ ЭТОГО ГИБРИДНОГО БЕЛКА | |
| ZA200209955B (en) | Method for preparing a physiologically-18-polypeptide. | |
| HK1055138B (en) | Method for preparing a physiologically active il-18 polypeptide | |
| WO2005116220A1 (en) | Production of recombinant protein using heterologous prosequences | |
| JP4295508B2 (ja) | 繊毛虫テトラヒメナからの酵素ホスホリパーゼａ１のｄｎａ配列およびその使用 | |
| KR100843634B1 (ko) | 세포막투과 전달 펩타이드 및 이를 포함하는 생물제제 | |
| RU2143493C1 (ru) | Рекомбинантная плазмидная днк ppins16, кодирующая гибридный полипептид, содержащий проинсулин человека, рекомбинантная плазмидная днк ppins25, кодирующая гибридный полипептид, содержащий проинсулин человека, и штамм бактерий escherichia coli - продуцент гибридного полипептида, содержащего проинсулин человека | |
| EP0533913A1 (de) | Neue endopeptidase | |
| WO2009005201A1 (en) | A method for producing stromal cell-derived factor-1a as an active soluble protein form | |
| EP1523567A1 (de) | Verfahren zur verbesserung der ausbeuten an löslichen proteinen | |
| JPH01144978A (ja) | 新規組換えプラスミドｐＧＲＦ２−１５ | |
| CN107177575A (zh) | 超声波辅助酶法提取肠激酶工艺 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |