JP2002502611A5 - - Google Patents
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- JP2002502611A5 JP2002502611A5 JP2000530619A JP2000530619A JP2002502611A5 JP 2002502611 A5 JP2002502611 A5 JP 2002502611A5 JP 2000530619 A JP2000530619 A JP 2000530619A JP 2000530619 A JP2000530619 A JP 2000530619A JP 2002502611 A5 JP2002502611 A5 JP 2002502611A5
- Authority
- JP
- Japan
- Prior art keywords
- heparanase
- polypeptide
- dna
- human
- cells
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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- 108090000765 processed proteins & peptides Proteins 0.000 description 20
- 229920001184 polypeptide Polymers 0.000 description 19
- 102000004196 processed proteins & peptides Human genes 0.000 description 19
- 108010037536 heparanase Proteins 0.000 description 16
- 102100024025 Heparanase Human genes 0.000 description 12
- 108020004414 DNA Proteins 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 10
- 238000000034 method Methods 0.000 description 9
- 239000012634 fragment Substances 0.000 description 8
- 150000001413 amino acids Chemical class 0.000 description 6
- 210000002950 fibroblast Anatomy 0.000 description 6
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 239000002299 complementary DNA Substances 0.000 description 5
- 108091008146 restriction endonucleases Proteins 0.000 description 5
- 102400000498 Connective tissue-activating peptide III Human genes 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
- 108010035886 connective tissue-activating peptide Proteins 0.000 description 4
- 102000019034 Chemokines Human genes 0.000 description 3
- 108010012236 Chemokines Proteins 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 229920002971 Heparan sulfate Polymers 0.000 description 3
- 206010028980 Neoplasm Diseases 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
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- 239000002773 nucleotide Substances 0.000 description 3
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- 108090000623 proteins and genes Proteins 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
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- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 230000001766 physiological effect Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 239000013615 primer Substances 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 230000005030 transcription termination Effects 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- 102000004411 Antithrombin III Human genes 0.000 description 1
- 108090000935 Antithrombin III Proteins 0.000 description 1
- 206010061000 Benign pancreatic neoplasm Diseases 0.000 description 1
- 108050006947 CXC Chemokine Proteins 0.000 description 1
- 102000019388 CXC chemokine Human genes 0.000 description 1
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010060309 Glucuronidase Proteins 0.000 description 1
- 102000053187 Glucuronidase Human genes 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical class OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 208000036830 Normal foetus Diseases 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 206010037211 Psychomotor hyperactivity Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 208000031112 adenoma of pancreas Diseases 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 229960005348 antithrombin iii Drugs 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 102000008395 cell adhesion mediator activity proteins Human genes 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000002975 chemoattractant Substances 0.000 description 1
- 230000024321 chromosome segregation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
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- 239000008121 dextrose Substances 0.000 description 1
- 210000001840 diploid cell Anatomy 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
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- 238000005206 flow analysis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 210000003917 human chromosome Anatomy 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
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- 238000011835 investigation Methods 0.000 description 1
- 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 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000000503 lectinlike effect Effects 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000031864 metaphase Effects 0.000 description 1
- 238000003358 metastasis assay Methods 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- FVSUYFWWFUVGRG-UHFFFAOYSA-N naphthalen-1-ylurea Polymers C1=CC=C2C(NC(=O)N)=CC=CC2=C1 FVSUYFWWFUVGRG-UHFFFAOYSA-N 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
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- 210000005259 peripheral blood Anatomy 0.000 description 1
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- 102000020233 phosphotransferase Human genes 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
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- 238000012163 sequencing technique Methods 0.000 description 1
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- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- FIAFUQMPZJWCLV-UHFFFAOYSA-N suramin Chemical compound OS(=O)(=O)C1=CC(S(O)(=O)=O)=C2C(NC(=O)C3=CC=C(C(=C3)NC(=O)C=3C=C(NC(=O)NC=4C=C(C=CC=4)C(=O)NC=4C(=CC=C(C=4)C(=O)NC=4C5=C(C=C(C=C5C(=CC=4)S(O)(=O)=O)S(O)(=O)=O)S(O)(=O)=O)C)C=CC=3)C)=CC=C(S(O)(=O)=O)C2=C1 FIAFUQMPZJWCLV-UHFFFAOYSA-N 0.000 description 1
- 229960005314 suramin Drugs 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 230000006439 vascular pathology Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB9802725.3A GB9802725D0 (en) | 1998-02-09 | 1998-02-09 | Organic compounds |
| GB9802725.3 | 1998-02-09 | ||
| PCT/EP1999/000777 WO1999040207A1 (en) | 1998-02-09 | 1999-02-05 | HUMAN HEPARANASE POLYPEPTIDE AND cDNA |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2002502611A JP2002502611A (ja) | 2002-01-29 |
| JP2002502611A5 true JP2002502611A5 (https=) | 2006-03-30 |
Family
ID=10826705
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000530619A Pending JP2002502611A (ja) | 1998-02-09 | 1999-02-05 | ヒトヘパラナーゼポリペプチドおよびｃＤＮＡ |
Country Status (6)
| Country | Link |
|---|---|
| US (2) | US6461848B1 (https=) |
| EP (1) | EP1054980A1 (https=) |
| JP (1) | JP2002502611A (https=) |
| AU (1) | AU2831999A (https=) |
| GB (1) | GB9802725D0 (https=) |
| WO (1) | WO1999040207A1 (https=) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6348344B1 (en) * | 1997-09-02 | 2002-02-19 | Insight Strategy & Marketing Ltd. | Genetically modified cells and methods for expressing recombinant heparanase and methods of purifying same |
| US5968822A (en) | 1997-09-02 | 1999-10-19 | Pecker; Iris | Polynucleotide encoding a polypeptide having heparanase activity and expression of same in transduced cells |
| US6562950B2 (en) * | 1997-09-02 | 2003-05-13 | Insight Strategy & Marketing Ltd. | Heparanase activity neutralizing anti-heparanase monoclonal antibody |
| AU2759199A (en) * | 1998-02-24 | 1999-09-15 | Pharmacia & Upjohn Company | Human platelet heparanase polypeptides, polynucleotide molecules that encode them, and methods for the identification of compounds that alter heparanase activity |
| US20020068054A1 (en) * | 2000-09-11 | 2002-06-06 | Insight Strategy & Marketing Ltd. And Hadasit Medical Research Services And Development Ltd. | Therapeutic and cosmetic uses of heparanases |
| JP2003510053A (ja) * | 1999-09-23 | 2003-03-18 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | ヘパラナーゼ蛋白質ファミリーの１種、ヘパラナーゼ−２ |
| WO2001046392A2 (en) | 1999-12-22 | 2001-06-28 | Oxford Glycosciences (Uk) Ltd. | Homologues of human heparanase and splice variants thereof |
| EP1356083A2 (en) | 2000-09-15 | 2003-10-29 | Reddy US Therapeutics, Inc. | Methods and compositions for glycosidase assays |
| FR2818131B1 (fr) * | 2000-12-14 | 2005-02-11 | Oreal | Composition cosmetique comprenant de l'heparanase |
| CH696701A5 (de) | 2001-12-18 | 2007-10-15 | Hoffmann La Roche | Verfahren zum Testen eines Mittels auf dessen Fähigkeit, die Heparanaseaktivität zu hemmen. |
| EP1479764A1 (en) | 2003-05-19 | 2004-11-24 | Deutsches Krebsforschungszentrum Stiftung des öffentlichen Rechts | Heparanase-derived peptides for vaccination of tumor patients |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5362641A (en) * | 1989-08-23 | 1994-11-08 | Hadassah Medical Organization Kiryat Hadassah | Heparanase derived from human Sk-Hep-1 cell line |
| WO1995004158A1 (en) * | 1993-07-29 | 1995-02-09 | The Upjohn Company | Use of heparanase to identify and isolate anti-heparanase compound |
| AUPN261895A0 (en) | 1995-04-28 | 1995-05-18 | Australian National University, The | Preparation and use of sulfated oligosaccharides |
| US5968822A (en) * | 1997-09-02 | 1999-10-19 | Pecker; Iris | Polynucleotide encoding a polypeptide having heparanase activity and expression of same in transduced cells |
| US20040213789A1 (en) * | 1997-09-02 | 2004-10-28 | Oron Yacoby-Zeevi | Heparanase activity neutralizing anti-heparanase monoclonal antibody and other anti-heparanase antibodies |
| JP2002510462A (ja) * | 1997-10-28 | 2002-04-09 | ジ・オーストラリアン・ナショナル・ユニバーシティー | 哺乳類のエンドグルクロニダーゼをコードする単離された核酸分子およびその使用 |
-
1998
- 1998-02-09 GB GBGB9802725.3A patent/GB9802725D0/en not_active Ceased
-
1999
- 1999-02-05 EP EP99908854A patent/EP1054980A1/en not_active Withdrawn
- 1999-02-05 WO PCT/EP1999/000777 patent/WO1999040207A1/en not_active Ceased
- 1999-02-05 US US09/601,777 patent/US6461848B1/en not_active Expired - Fee Related
- 1999-02-05 AU AU28319/99A patent/AU2831999A/en not_active Abandoned
- 1999-02-05 JP JP2000530619A patent/JP2002502611A/ja active Pending
-
2002
- 2002-03-27 US US10/107,859 patent/US20020115183A1/en not_active Abandoned
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