2007年7月
Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and-9
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
- ,
- ,
- 巻
- 75
- 号
- 6
- 開始ページ
- 1285
- 終了ページ
- 1291
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1007/s00253-007-0952-6
- 出版者・発行元
- SPRINGER
To compare the substrate preferences of rat brain neurolysin and cancer-producing matrix metalloproteinases (MMPs), which have the same architecture in their catalytic domains, the cleavage activity of neurolysin toward MMP-specific fluorescence-quenching peptides was quantitatively measured. The results show that neurolysin effectively cleaved MOCAc [(7-methoxy coumarin-4-yl) acetyl]-RPKPYANvaWMK(Dnp[2,4-dinitrophenyl])-NH2, a specific substrate of MMP-2 and MMP-9, but hardly cleaved MOCAc-RPKPVENvaWRK(Dnp)-NH2, a specific substrate of MMP-3, suggesting that neurolysin has a similar substrate preference to MMP-2 and MMP-9. A structural comparison between neurolysin and MMP-9 showed the similar key amino acid residues for substrate recognition. The possible application of neurolysin displayed on the yeast cell surface, as a safe protein alternative to MMP-2 and MMP-9 which induce cancer cell growth, invasion, and metastasis, to analysis of properties of the MMPs, including the screening of inhibitors and analysis of inhibition mechanism etc., are also discussed.
- リンク情報
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- DOI
- https://doi.org/10.1007/s00253-007-0952-6
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902217740352033
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/17404728
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000247463100008&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1007/s00253-007-0952-6
- ISSN : 0175-7598
- J-Global ID : 200902217740352033
- PubMed ID : 17404728
- Web of Science ID : WOS:000247463100008