JP2009509532A5 - - Google Patents
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- JP2009509532A5 JP2009509532A5 JP2008533536A JP2008533536A JP2009509532A5 JP 2009509532 A5 JP2009509532 A5 JP 2009509532A5 JP 2008533536 A JP2008533536 A JP 2008533536A JP 2008533536 A JP2008533536 A JP 2008533536A JP 2009509532 A5 JP2009509532 A5 JP 2009509532A5
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- chondroitinase
- chondroitin
- michelacci
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- 101700032815 GALNS Proteins 0.000 description 6
- 102100020232 GALNS Human genes 0.000 description 6
- 229920001287 Chondroitin sulfate Polymers 0.000 description 5
- 101700063555 HYAL Proteins 0.000 description 5
- KXKPYJOVDUMHGS-OSRGNVMNSA-N Chondroitin sulfate Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](OS(O)(=O)=O)[C@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](C(O)=O)O1 KXKPYJOVDUMHGS-OSRGNVMNSA-N 0.000 description 4
- 108090000819 Chondroitin-sulfate-ABC endolyases Proteins 0.000 description 4
- 102000036765 Chondroitin-sulfate-ABC endolyases Human genes 0.000 description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 229940059329 chondroitin sulfate Drugs 0.000 description 4
- 230000004059 degradation Effects 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 210000003050 Axons Anatomy 0.000 description 3
- 229920002567 Chondroitin Polymers 0.000 description 3
- DLGJWSVWTWEWBJ-HGGSSLSASA-N Chondroitin Chemical compound CC(O)=N[C@@H]1[C@H](O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@H](O)C=C(C(O)=O)O1 DLGJWSVWTWEWBJ-HGGSSLSASA-N 0.000 description 3
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- 241000588724 Escherichia coli Species 0.000 description 2
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- 241000588767 Proteus vulgaris Species 0.000 description 2
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- 238000010369 molecular cloning Methods 0.000 description 2
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- 238000011084 recovery Methods 0.000 description 2
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- 108010059480 Chondroitin Sulfate Proteoglycans Proteins 0.000 description 1
- 229940107200 Chondroitin Sulfates Drugs 0.000 description 1
- 108050003353 Chondroitin sulfate ABC lyase Proteins 0.000 description 1
- 102000021765 Chondroitin sulfate ABC lyase Human genes 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
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- 206010061431 Glial scar Diseases 0.000 description 1
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- ZFGMDIBRIDKWMY-PASTXAENSA-N Heparin Chemical compound CC(O)=N[C@@H]1[C@@H](O)[C@H](O)[C@@H](COS(O)(=O)=O)O[C@@H]1O[C@@H]1[C@@H](C(O)=O)O[C@@H](O[C@H]2[C@@H]([C@@H](OS(O)(=O)=O)[C@@H](O[C@@H]3[C@@H](OC(O)[C@H](OS(O)(=O)=O)[C@H]3O)C(O)=O)O[C@@H]2O)CS(O)(=O)=O)[C@H](O)[C@H]1O ZFGMDIBRIDKWMY-PASTXAENSA-N 0.000 description 1
- 241000605114 Pedobacter heparinus Species 0.000 description 1
- 102000035443 Peptidases Human genes 0.000 description 1
- 108091005771 Peptidases Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 240000002057 Secale cereale Species 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 230000003376 axonal Effects 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
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- 238000010192 crystallographic characterization Methods 0.000 description 1
- 238000011013 endotoxin removal Methods 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
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Description
コンドロイチナーゼの細菌標本が様々なコンドロイチン硫酸（ｃｈｏｎｄｒｏｉｔｉｎ ｓｕｌｆａｔｅ：ＣｈＳ）基質と対比して特徴付けられた際に、一連の明確に異なるコンドロイチナーゼが発見されたが、それは、主にコンドロイチンＡ（ｃｈｏｎｄｒｉｔｉｎ Ａ：ＣｈＡ）とコンドロイチンＣ（ｃｈｏｎｄｒｏｉｔｉｎ Ｃ：ＣｈＣ）を分解するコンドロイチナーゼＡＣ（Ｙａｍａｇａｔａら、１９６８年）、コンドロイチンＢ（ｃｈｏｎｄｒｏｉｔｉｎ Ｂ：ＣｈＢ）を分解するコンドロイチナーゼＢ（ＭｉｃｈｅｌａｃｃｉおよびＤｅｉｔｒｉｃｈ、１９７６年）、主にＣｈＣに作用するコンドロイチナーゼＣ（Ｍｉｃｈｅｌａｃｃｉ ＹＭおよびＤｉｅｔｒｉｃｈ ＣＰ、１９７６）であり、コンドロイチナーゼＡＢＣは３種類の基質ＣｈＳ−Ａ、ＣｈＳ−Ｂ、ＣｈＳ−Ｃすべてに特異性を示す（Ｙａｍａｇａｔａら、１９６８、Ｍｉｃｈｅｌａｃｃｉら、１９８７年）。
この出願の発明に関連する先行技術文献情報としては、以下のものがある（国際出願日以降国際段階で引用された文献及び他国に国内移行した際に引用された文献を含む）。
米国特許第５，７９２，７４３号明細書
米国特許第６，３１３，２６５号明細書
米国特許第５，９９７，８６３号明細書
米国特許第５，５７８，４８０号明細書
米国特許第６，００７，８１０号明細書
米国特許第５，４９８，５３６号明細書
国際公開第２００５／１１２９８６号
ＳＡＴＯ ｅｔ ａｌ．，Ｃｌｏｎｉｎｇ ａｎｄ ｅｘｐｒｅｓｓｉｏｎ ｉｎ Ｅｓｃｈｅｒｉｃｈｉａ ｃｏｌｉ ｏｆ ｔｈｅ ｇｅｎｅ ｅｎｃｏｄｉｎｇ ｔｈｅ Ｐｒｏｔｅｕｓ ｖｕｌｇａｒｉｓ ｃｈｏｎｄｒｏｉｔｉｎ ＡＢＣ ｌｙａｓｅ，１９９４，Ａｐｐｌ．Ｍｉｃｒｏｂｉｏｌ．Ｂｉｏｔｅｃｈｎｏｌ．４１：３９−４６
ＣＡＧＧＩＡＮＯ ｅｔ ａｌ．，Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ ＡＢＣＩ Ｉｍｐｒｏｖｅｓ Ｌｏｃｏｍｏｔｉｏｎ ａｎｄ Ｂｌａｄｄｅｒ Ｆｕｎｃｔｉｏｎ ｆｏｌｌｏｗｉｎｇ Ｃｏｎｔｕｓｉｏｎ Ｉｎｊｕｒｙ ｏｆ ｔｈｅ Ｒａｔ Ｓｐｉｎａｌ Ｃｏｒｄ，２００５，Ｊ．Ｎｅｕｒｏｔｒａｕｍａ ２２（２）：２２６−２３９
Ａｃｃｅｓｓｉｏｎ Ｐ５９８０７，Ａｕｇｕｓｔ １５，２００３
ＦＡＷＣＥＴＴ ｅｔ ａｌ．，Ｔｈｅ ｇｌｉａｌ ｓｃａｒ ａｎｄ ｃｅｎｔｒａｌ ｎｅｒｖｏｕｓ ｓｙｓｔｅｍ ｒｅｐａｉｒ，１９９９，Ｂｒａｉｎ Ｒｅｓ．Ｂｕｌｌ．４９（６）：３７７−３９１
ＢＲＡＤＢＵＲＹ ｅｔ ａｌ．，Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ ＡＢＣ ｐｒｏｍｏｔｅｓ ｆｕｎｃｔｉｏｎａｌ ｒｅｃｏｖｅｒｙ ａｆｔｅｒ ｓｐｉｎａｌ ｃｏｒｄ ｉｎｊｕｒｙ，２００２，Ｎａｔｕｒｅ ４１６：６３６−６４０
ＨＯＦＦＭＡＮ ｅｔ ａｌ．，Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅｓ，１９５８，Ｆｅｄｅｒａｔｉｏｎ Ｐｒｏｃ．１７：１０７８−１０８２
ＹＡＭＡＧＡＴＡ ｅｔ ａｌ．，Ｐｕｒｉｆｉｃａｔｉｏｎ ａｎｄ Ｐｒｏｐｅｒｔｉｅｓ ｏｆ Ｂａｃｔｅｒｉａｌ Ｃｈｏｎｄｒｏｉｔｉｎａｓｅｓ ａｎｄ Ｃｈｏｎｄｒｏｓｕｌｆａｔａｓｅｓ，１９６８，Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．２４３（７）：１５２３−１５３５
ＭＩＣＨＥＬＡＣＣＩ ｅｔ ａｌ．，Ｉｓｏｌａｔｉｏｎ ａｎｄ ｃｈａｒａｃｔｅｒｉｚａｔｉｏｎ ｏｆ ａｎ ｉｎｄｕｃｅｄ Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ ＡＢＣ，１９８７，Ｂｉｏｃｈｅｍ．Ｂｉｏｐｈｙｓ．Ａｃｔａ ９２３：２９１−３０１
ＢＡＮＫＥＲ ｅｔ ａｌ．，Ｍｏｄｅｒｎ Ｐｈａｒｍａｃｅｕｔｉｃｓ，１９７９，Ｍａｒｃｅｌ Ｄｅｋｋｅｒ，Ｉｎｃ．（ＴＯＣ）
ＧＯＯＤＭＡＮ ｅｔ ａｌ．，Ｔｈｅ Ｐｈａｒｍａｃｏｌｏｇｉｃａｌ Ｂａｓｉｓ ｏｆ Ｔｅｒａｐｅｕｔｉｃｓ，６ｔｈｅｄ．１９８０，ＭａｃＭｉｌｌａｎ Ｐｕｂ．，Ｎｅｗ Ｙｏｒｋ，（ＴＯＣ）
ＭＩＣＨＥＬＡＣＣＩ ｅｔ ａｌ．，Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ Ｃ ｆｒｏｍ Ｆｌａｖｏｂａｃｔｅｒｉｕｍ ｈａｐａｒｉｎｕｍ，１９７６，Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．２５１（４）：１１５４−１１５８
ＺＵＯ ｅｔ ａｌ．，Ｄｅｇｒａｄａｔｉｏｎ ｏｆ Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅ Ｐｒｏｔｅｏｇｌｙｃａｎ Ｅｎｈａｎｃｅｓ ｔｈｅ Ｎｅｕｒｉｔｅ−Ｐｒｏｍｏｔｉｎｇ Ｐｏｔｅｎｔｉａｌ ｏｆ Ｓｐｉｎａｌ Ｃｏｒｄ Ｔｉｓｓｕｅ，１９９８，Ｅｘｐ．Ｎｅｕｒｏｌ．１５４（２）：６５４−６６２
ＺＵＯ ｅｔ ａｌ．，Ｒｅｇｅｎｅｒａｔｉｏｎ ｏｆ Ａｘｏｎｓ ａｆｔｅｒ Ｎｅｒｖｅ Ｔｒａｎｓａｃｔｉｏｎ Ｒｅｐａｉｒ ｉｓ Ｅｎｈａｎｃｅｄ ｂｙ Ｄｅｇｒａｄａｔｉｏｎ ｏｆ Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅ Ｐｒｏｔｅｏｇｌｙｃａｎ，２００２，Ｅｘｐ．Ｎｅｕｒｏｌ．１７６３（１）：２２１−２２８
ＫＲＥＫＯＳＫＩ ｅｔ ａｌ．，Ａｘｏｎａｌ Ｒｅｇｅｎｅｒａｔｉｏｎ ｉｎｔｏ Ａｃｅｌｌｕｌａｒ Ｎｅｒｖｅ Ｇｒａｆｔｓ ｉｓ Ｅｎｈａｎｃｅｄ ｂｙ Ｄｅｇｒａｄａｔｉｏｎ ｏｆ Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅ Ｐｒｏｔｅｏｇｌｙｃａｎ，２００１，Ｊ．Ｎｅｕｒｏｓｃｉ．１５：２１（１６）：６２０６−６２１３
ＢＬＩＧＨＴ ｅｔ ａｌ．，Ａｎｉｍａｌ ｍｏｄｅｌｓ ｏｆ ｓｐｉｎａｌ ｃｏｒｄ ｉｎｊｕｒｙ，２００２，Ｔｏｐ Ｓｐｉｎａｌ Ｃｏｒｄ Ｉｎｊ．Ｒｅｈａｂｉ．６（２）：１−１３
ＫＷＯＮ ｅｔ ａｌ．，Ａｎｉｍａｌ Ｍｏｄｅｌｓ Ｕｓｅｄ ｉｎ Ｓｐｉｎａｌ Ｃｏｒｄ Ｒｅｇｅｎｅｒａｔｉｏｎ Ｒｅｓｅａｒｃｈ，２００２，Ｓｐｉｎｅ ２７（１４）：１５０４−１５１０
ＨＩＲＳＣＨＢＥＲＧ ｅｔ ａｌ．，Ｉｎｆｌａｍｍａｔｉｏｎ ａｆｔｅｒ ａｘｏｎａｌ ｉｎｊｕｒｙ ｈａｓ ｃｏｎｆｌｉｃｔｉｎｇ ｃｏｎｓｅｑｕｅｓｎｃｅｓ ｆｏｒ ｒｅｃｏｖｅｒｙ ｏｆ ｆｕｎｃｔｉｏｎ：ｒｅｓｃｕｅ ｏｆ ｓｐａｒｅｄ ａｘｏｎｓ ｉｓ ｉｍｐａｉｒｅｄ ｂｕｔ ｒｅｇｅｎｅｒａｔｉｏｎ ｉｓ ｓｕｐｐｏｒｔｅｄ，Ｊ．Ｎｅｕｒｏｉｍｍｕｎｏｌ．１９９４，５０（１）：９−１６（ＡＢＳＴＲＡＣＴ）
ＨＯＵ ｅｔ ａｌ．，Ｅｎｄｏｔｏｘｉｎ Ｒｅｍｏｖａｌ ｂｙ Ａｎｉｏｎ−Ｅｘｃｈａｎｇｅ Ｐｏｌｙｍｅｒｉｃ Ｍａｔｒｉｘ，１９９０，Ｂｉｏｔｅｃｈ．Ａｐｐｌ．Ｂｉｏｃｈｅｍ．１２：３１５−３２４
ＨＡＭＡＩ ｅｔ ａｌ．，Ｔｗｏ Ｄｉｓｔｉｎｃｔ Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅ ＡＢＣ Ｌｙａｓｅｓ，１９９７，Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．２７２（１４）：９１２３−９１３０
ＢＲＯＡＣＨ ｅｔ ａｌ．，Ｅｘｐｅｒｉｍｅｎｔａｌ Ｍａｎｉｐｕｌａｔｉｏｎ ｏｆ Ｇｅｎｅ Ｅｘｐｒｅｓｓｉｏｎ，Ｍ．Ｉｎｏｕｙｅ ｅｄ．，Ａｃａｄｅｍｉｃ Ｐｒｅｓｓ，Ｎｅｗ Ｙｏｒｋ，ｐｐ．８３−１１７
ＳＡＭＢＲＯＯＫ ｅｔ ａｌ．，Ｍｏｌｅｃｕｌａｒ Ｃｌｏｎｉｎｇ，２ｎｄｅｄ．，Ｃｏｌｄ Ｓｐｒｉｎｇ Ｈａｒｂｏｒ Ｌａｂｏｒａｔｏｒｙ Ｐｒｅｓｓ，１９８９ Ｃｈ．１６ ａｎｄ １７
ＳＡＭＢＲＯＯＫ ｅｔ ａｌ．，Ｍｏｌｅｃｕｌａｒ Ｃｌｏｎｉｎｇ，２ｎｄｅｄ．，Ｃｏｌｄ Ｓｐｒｉｎｇ Ｈａｒｂｏｒ Ｌａｂｏｒａｔｏｒｙ Ｐｒｅｓｓ，１９８９（ＴＯＣ）
ＢＥＮ−ＢＡＳＳＡＴ ｅｔ ａｌ．，Ｐｒｏｃｅｓｓｉｎｇ ｏｆ ｔｈｅ Ｉｎｉｔｉａｔｉｏｎ Ｍｅｔｈｉｏｎｉｎｅ ｆｒｏｍ Ｐｒｏｔｅｉｎｓ：Ｐｒｏｐｅｒｔｉｅｓ ｏｆ ｔｈｅ Ｅｓｃｈｅｒｉｃｈｉａ ｃｏｌｉ Ｍｅｔｈｉｏｎｉｎｅ Ａｍｉｎｏｐｅｐｔｉｄａｓｅ ａｎｄ Ｉｔｓ Ｇｅｎｅ Ｓｔｒｕｃｔｕｒｅ，１９８７，Ｊ．Ｂａｃｔｅｒｉｏｌ．１６９（２）：７５１−７５７
ＭＩＬＬＥＲ ｅｔ ａｌ．，Ｎ−ｔｅｒｍｉｎａｌ ｍｅｔｈｉｏｎｉｎｅ−ｓｐｅｃｉｆｉｃ ｐｅｐｔｉｄａｓｅ ｉｎ Ｓａｌｍｏｎｅｌｌａ ｔｙｐｈｉｍｕｒｉｕｍ，１９８７，ＰＮＡＳ ８４：２７１８−２７２２
ＫＯＲＮ，１９５７，Ｔｈｅ Ｄｅｇｒａｄａｔｉｏｎ ｏｆ Ｈｅｐａｒｉｎ ｂｙ Ｂａｃｔｅｒｉａｌ Ｅｎｚｙｍｅｓ，Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．２２６：８４１−８４４
ＭＡＲＴＩＮＥＺ ｅｔ ａｌ．，Ｐｕｒｉｆｉｃａｔｉｏｎ ａｎｄ Ｐｒｏｐｅｒｔｉｅｓ ｏｆ ｔｈｅ Ｅｎｚｙｍｅ Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ，１９５９，Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．２３４（９）：２２３６−２２３９
ＨＵＡＮＧ ｅｔ ａｌ．，Ｃｒｙｓｔａｌ Ｓｔｒｕｃｔｕｒｅ ｏｆ Ｐｒｏｔｅｕｓ ｖｕｌｇａｒｉｓ Ｃｈｏｎｄｒｏｉｔｉｎ Ｓｕｌｆａｔｅ ＡＢＣ Ｌｙａｓｅ Ｉ ａｔ １．９ Ａ Ｒｅｓｏｌｕｔｉｏｎ，２００３，Ｊ．Ｍｏｌ．Ｂｉｏｌ．３２８：６２３−６３４
ＭＩＣＨＥＬＡＣＣＩ ｅｔ ａｌ．，Ａ Ｃｏｍｐａｒａｔｉｖｅ Ｓｔｕｄｙ Ｂｅｔｗｅｅｎ ａ Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ Ｂ ａｎｄ ａ Ｃｈｏｎｄｒｏｉｔｉｎａｓｅ ＡＣ ｆｒｏｍ Ｆｌａｖｏｂａｃｔｅｒｉｕｍ ｈｅｐａｒｉｎｕｍ，１９７５，Ｂｉｏｃｈｅｍ．Ｊ．１５１：１２１−１２９
この出願の発明に関連する先行技術文献情報としては、以下のものがある（国際出願日以降国際段階で引用された文献及び他国に国内移行した際に引用された文献を含む）。
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| PCT/US2006/037554 WO2007038548A2 (en) | 2005-09-26 | 2006-09-26 | Compositions and methods of using chondroitinase abci mutants |
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