IL92938A - A polypeptide that has a mutagenic activity on monocytes and AND that encodes it - Google Patents

A polypeptide that has a mutagenic activity on monocytes and AND that encodes it

Info

Publication number: IL92938A
Authority: IL; Israel
Prior art keywords: polypeptide; thr; ala; lys; gin
Prior art date: 1989-01-01

Application number

IL9293889A

Other languages

English (en)

Hebrew (he)

Other versions

IL92938A0 (en

Original Assignee

Us Commerce

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1989-01-01

Filing date

1989-12-31

Publication date

1998-08-16

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=26332976&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=IL92938(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1989-01-01 Priority claimed from JP64000065A external-priority patent/JP2893112B2/ja

1989-02-03 Priority claimed from JP1026438A external-priority patent/JP2992640B2/ja

1989-12-31 Application filed by Us Commerce filed Critical Us Commerce

1990-09-17 Publication of IL92938A0 publication Critical patent/IL92938A0/xx

1998-08-16 Publication of IL92938A publication Critical patent/IL92938A/en

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 121
229920001184 polypeptide Polymers 0.000 title claims abstract description 120
102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 120
102000014962 Monocyte Chemoattractant Proteins Human genes 0.000 title claims abstract description 28
108010064136 Monocyte Chemoattractant Proteins Proteins 0.000 title claims abstract description 28
239000005482 chemotactic factor Substances 0.000 title claims abstract description 28
238000000034 method Methods 0.000 claims abstract description 37
230000000694 effects Effects 0.000 claims abstract description 36
210000004027 cell Anatomy 0.000 claims abstract description 20
239000013604 expression vector Substances 0.000 claims abstract description 11
108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 8
150000001413 amino acids Chemical group 0.000 claims description 45
239000012634 fragment Substances 0.000 claims description 43
239000002243 precursor Substances 0.000 claims description 17
239000013598 vector Substances 0.000 claims description 12
230000014509 gene expression Effects 0.000 claims description 5
108010009298 lysylglutamic acid Proteins 0.000 claims description 5
ZDBWKBCKYJGKGP-DCAQKATOSA-N Arg-Leu-Ala Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(O)=O ZDBWKBCKYJGKGP-DCAQKATOSA-N 0.000 claims description 4
NUHQMYUWLUSRJX-BIIVOSGPSA-N Asn-Ala-Pro Chemical compound C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CC(=O)N)N NUHQMYUWLUSRJX-BIIVOSGPSA-N 0.000 claims description 4
WSXDIZFNQYTUJB-SRVKXCTJSA-N Asp-His-Leu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(C)C)C(O)=O WSXDIZFNQYTUJB-SRVKXCTJSA-N 0.000 claims description 4
UAXIKORUDGGIGA-DCAQKATOSA-N Asp-Pro-Lys Chemical compound C1C[C@H](N(C1)C(=O)[C@H](CC(=O)O)N)C(=O)N[C@@H](CCCCN)C(=O)O UAXIKORUDGGIGA-DCAQKATOSA-N 0.000 claims description 4
OFYVKOXTTDCUIL-FXQIFTODSA-N Asp-Ser-Met Chemical compound CSCC[C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)N OFYVKOXTTDCUIL-FXQIFTODSA-N 0.000 claims description 4
IWVNIQXKTIQXCT-SRVKXCTJSA-N Cys-Tyr-Asn Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CS)N)O IWVNIQXKTIQXCT-SRVKXCTJSA-N 0.000 claims description 4
241000880493 Leptailurus serval Species 0.000 claims description 4
ZFNYWKHYUMEZDZ-WDSOQIARSA-N Lys-Trp-Val Chemical compound CC(C)[C@@H](C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](CCCCN)N ZFNYWKHYUMEZDZ-WDSOQIARSA-N 0.000 claims description 4
XZQYIJALMGEUJD-OEAJRASXSA-N Phe-Lys-Thr Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XZQYIJALMGEUJD-OEAJRASXSA-N 0.000 claims description 4
JHSRGEODDALISP-XVSYOHENSA-N Phe-Thr-Asn Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(O)=O JHSRGEODDALISP-XVSYOHENSA-N 0.000 claims description 4
UTAUEDINXUMHLG-FXQIFTODSA-N Pro-Asp-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1 UTAUEDINXUMHLG-FXQIFTODSA-N 0.000 claims description 4
FGBLCMLXHRPVOF-IHRRRGAJSA-N Ser-Tyr-Arg Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O FGBLCMLXHRPVOF-IHRRRGAJSA-N 0.000 claims description 4
ILVGMCVCQBJPSH-WDSKDSINSA-N Ser-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@@H](N)CO ILVGMCVCQBJPSH-WDSKDSINSA-N 0.000 claims description 4
GFRIEEKFXOVPIR-RHYQMDGZSA-N Thr-Pro-Lys Chemical compound C[C@@H](O)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(O)=O GFRIEEKFXOVPIR-RHYQMDGZSA-N 0.000 claims description 4
WPSKTVVMQCXPRO-BWBBJGPYSA-N Thr-Ser-Ser Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O WPSKTVVMQCXPRO-BWBBJGPYSA-N 0.000 claims description 4
RUCNAYOMFXRIKJ-DCAQKATOSA-N Val-Ala-Lys Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CCCCN RUCNAYOMFXRIKJ-DCAQKATOSA-N 0.000 claims description 4
BZDGLJPROOOUOZ-XGEHTFHBSA-N Val-Thr-Cys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](C(C)C)N)O BZDGLJPROOOUOZ-XGEHTFHBSA-N 0.000 claims description 4
108010062796 arginyllysine Proteins 0.000 claims description 4
108010092854 aspartyllysine Proteins 0.000 claims description 4
108010004073 cysteinylcysteine Proteins 0.000 claims description 4
125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 4
KSFQPRLZAUXXPT-GARJFASQSA-N Lys-Cys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CS)NC(=O)[C@H](CCCCN)N)C(=O)O KSFQPRLZAUXXPT-GARJFASQSA-N 0.000 claims description 3
GJJQCBVRWDGLMQ-GUBZILKMSA-N Lys-Glu-Ala Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(O)=O GJJQCBVRWDGLMQ-GUBZILKMSA-N 0.000 claims description 3
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 3
230000004071 biological effect Effects 0.000 claims description 3
JBVSSSZFNTXJDX-YTLHQDLWSA-N Ala-Ala-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](C)N JBVSSSZFNTXJDX-YTLHQDLWSA-N 0.000 claims description 2
PAWIVEIWWYGBAM-YUMQZZPRSA-N Gly-Leu-Ala Chemical compound NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(O)=O PAWIVEIWWYGBAM-YUMQZZPRSA-N 0.000 claims description 2
IFMPDNRWZZEZSL-SRVKXCTJSA-N Leu-Leu-Cys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(O)=O IFMPDNRWZZEZSL-SRVKXCTJSA-N 0.000 claims description 2
KDGBLMDAPJTQIW-RHYQMDGZSA-N Thr-Met-Lys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)O)N)O KDGBLMDAPJTQIW-RHYQMDGZSA-N 0.000 claims description 2
DEGUERSKQBRZMZ-FXQIFTODSA-N Val-Ser-Ala Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(O)=O DEGUERSKQBRZMZ-FXQIFTODSA-N 0.000 claims description 2
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108020004414 DNA Proteins 0.000 abstract description 63
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239000002773 nucleotide Substances 0.000 description 27
125000003729 nucleotide group Chemical group 0.000 description 27
239000000872 buffer Substances 0.000 description 16
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 15
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239000002299 complementary DNA Substances 0.000 description 10
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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 9
239000013612 plasmid Substances 0.000 description 9
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238000013519 translation Methods 0.000 description 8
RGWHQCVHVJXOKC-SHYZEUOFSA-N dCTP Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OP(O)(O)=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-N 0.000 description 7
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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 6
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238000002741 site-directed mutagenesis Methods 0.000 description 6
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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
- C07K14/521—Chemokines
- C07K14/523—Beta-chemokines, e.g. RANTES, I-309/TCA-3, MIP-1alpha, MIP-1beta/ACT-2/LD78/SCIF, MCP-1/MCAF, MCP-2, MCP-3, LDCF-1, LDCF-2
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/545—IL-1

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Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Genetics & Genomics (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Toxicology (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
General Chemical & Material Sciences (AREA)
Animal Behavior & Ethology (AREA)
Chemical Kinetics & Catalysis (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

IL9293889A 1989-01-01 1989-12-31 A polypeptide that has a mutagenic activity on monocytes and AND that encodes it IL92938A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
JP64000065A JP2893112B2 (ja)	1989-01-01	1989-01-01	ヒト単球走化性因子活性を有するポリペプチド及びそれをコードするｄｎａ
JP1026438A JP2992640B2 (ja)	1989-02-03	1989-02-03	ヒト単球走化性因子活性を有するポリペプチド及びそれをコードするｄｎａ並びにそれらの製法

Publications (2)

Publication Number	Publication Date
IL92938A0 IL92938A0 (en)	1990-09-17
IL92938A true IL92938A (en)	1998-08-16

Family

ID=26332976

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL9293889A IL92938A (en)	1989-01-01	1989-12-31	A polypeptide that has a mutagenic activity on monocytes and AND that encodes it

Country Status (10)

Country	Link
EP (1)	EP0452391B1 (fr)
JP (1)	JPH04501961A (fr)
AT (1)	ATE155526T1 (fr)
AU (1)	AU642399B2 (fr)
CA (1)	CA2006969C (fr)
DE (1)	DE69031071T2 (fr)
DK (1)	DK0452391T3 (fr)
ES (2)	ES2056753A6 (fr)
IL (1)	IL92938A (fr)
WO (1)	WO1990007863A1 (fr)

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL92937A0 (en)	1989-01-31	1990-09-17	Us Health	Human derived monocyte attracting protein,pharmaceutical compositions comprising it and dna encoding it
US5212073A (en) *	1989-05-12	1993-05-18	Genetics Institute, Inc.	Process for producing human JE cytokine
US6767535B1 (en)	1989-05-12	2004-07-27	Dana-Farber Cancer Institute, Inc.	Suppressing tumor formation using cells expressing JE/monocyte chemoattractant protein-1
ATE228164T1 (de) *	1990-09-05	2002-12-15	Heart Res Inst Ltd	Chemotaktische faktoren
US6001649A (en) *	1990-11-29	1999-12-14	Societe Anonyme: Elf Sanofi	Chemokine NC28 (monocyte chemotactic protein-3, MCP-3) polypeptides and their recombinant production
WO1992019737A1 (fr) *	1991-05-09	1992-11-12	Dainippon Pharmaceutical Co., Ltd.	Procede de preparation d'un polypeptide de facteur chimiotactique de monocyte et souche utilisee pour cette preparation
JPH0782169A (ja) *	1993-09-13	1995-03-28	Toray Ind Inc	創傷治療剤
US7265201B1 (en)	1995-06-23	2007-09-04	Millennium Pharmaceuticals, Inc.	Human chemotactic cytokine
US6989435B2 (en)	1997-09-11	2006-01-24	Cambridge University Technical Services Ltd.	Compounds and methods to inhibit or augment an inflammatory response
US7067117B1 (en)	1997-09-11	2006-06-27	Cambridge University Technical Services, Ltd.	Compounds and methods to inhibit or augment an inflammatory response
US7238711B1 (en)	1999-03-17	2007-07-03	Cambridge University Technical Services Ltd.	Compounds and methods to inhibit or augment an inflammatory response
WO2007021807A1 (fr)	2005-08-12	2007-02-22	Schering Corporation	Fusions de mcp1
US8524217B2 (en)	2010-05-11	2013-09-03	Merck Sharp & Dohme Corp.	MCP1-Ig fusion variants

1989
- 1989-12-31 IL IL9293889A patent/IL92938A/en not_active IP Right Cessation
1990
- 1990-01-02 ES ES09050005A patent/ES2056753A6/es not_active Expired - Fee Related
- 1990-01-02 AU AU48450/90A patent/AU642399B2/en not_active Expired
- 1990-01-02 DE DE69031071T patent/DE69031071T2/de not_active Expired - Lifetime
- 1990-01-02 AT AT90901711T patent/ATE155526T1/de not_active IP Right Cessation
- 1990-01-02 EP EP90901711A patent/EP0452391B1/fr not_active Expired - Lifetime
- 1990-01-02 CA CA002006969A patent/CA2006969C/fr not_active Expired - Lifetime
- 1990-01-02 DK DK90901711.3T patent/DK0452391T3/da active
- 1990-01-02 ES ES90901711T patent/ES2104600T3/es not_active Expired - Lifetime
- 1990-01-02 WO PCT/US1990/000040 patent/WO1990007863A1/fr not_active Ceased
- 1990-01-02 JP JP2502276A patent/JPH04501961A/ja active Pending

Also Published As

Publication number	Publication date
JPH04501961A (ja)	1992-04-09
AU642399B2 (en)	1993-10-21
EP0452391A1 (fr)	1991-10-23
EP0452391A4 (en)	1992-06-03
DE69031071D1 (de)	1997-08-21
DE69031071T2 (de)	1998-02-05
CA2006969C (fr)	2000-03-14
WO1990007863A1 (fr)	1990-07-26
IL92938A0 (en)	1990-09-17
ES2104600T3 (es)	1997-10-16
CA2006969A1 (fr)	1990-07-01
AU4845090A (en)	1990-08-13
DK0452391T3 (da)	1997-10-20
EP0452391B1 (fr)	1997-07-16
ES2056753A6 (es)	1994-10-01
ATE155526T1 (de)	1997-08-15

Legal Events

Date	Code	Title
1998-12-27	FF	Patent granted
1999-06-20	KB	Patent renewed
2000-06-29	KB	Patent renewed
2004-02-19	KB	Patent renewed
2008-01-22	KB	Patent renewed
2010-11-30	EXP	Patent expired

Publication	Publication Date	Title
Wallner et al.	1986	Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity
CA1341240C (fr)	2001-06-05	Adn codant pour le facteur de necrose tumorale humain, ainsi qu'un polypeptide agissant comme facteur de necrose tumorale humain
DK172276B1 (da)	1998-02-16	Rekombinant derivat af human tumornekrosefaktor (hTNF), strukturelt gen, som koder for det rekombinante derivat, ekspressionsvektor, værtsceller, transformeret E. coli, fremgangsmåder til fremstilling af det rekombinante derivat og det strukturelle gen, oligonukleotid til brug ved fremstilling af genet, terapeutiske sammensætninger og formuleringer
CA2024629C (fr)	2001-07-24	Proteine morphogenique osseuse dactylethre laevis, adn l'encodant et son utilisation
US4677064A (en)	1987-06-30	Human tumor necrosis factor
EP0188920B1 (fr)	1993-09-29	Interleukine 1 et son dérivé
Rajavashisth et al.	1987	Cloning and tissue-specific expression of mouse macrophage colony-stimulating factor mRNA.
HU202287B (en)	1991-02-28	Process for producing human immune interferon
HU196457B (en)	1988-11-28	Process for producing interferons
IL92938A (en)	1998-08-16	A polypeptide that has a mutagenic activity on monocytes and AND that encodes it
Kluve-Beckerman et al.	1986	DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA)
DK168048B1 (da)	1994-01-24	Renset human interleukin-1, dets fremstilling og anvendelse i farmaceutiske praeparater
AU589919B2 (en)	1989-10-26	Human tumor necrosis factor
EP0413818B1 (fr)	1994-12-28	Procede de production d'un polypeptide du facteur chimiotactique neutrophile humain
HU202922B (en)	1991-04-29	Process for producing new limphotoxin-polypeptides
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EP0297833B1 (fr)	1995-03-22	Lymphotoxine physiologiquement active
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KR960016705B1 (ko)	1996-12-20	신규폴리펩티드 및 그것을 코우드하는 dna
US5290917A (en)	1994-03-01	Modified polypeptides of IL-1α
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JPH051800B2 (fr)	1993-01-11
NZ203661A (en)	1986-07-11	Recombinant dna method for production of human immune interferon
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