期刊
BIOCHEMICAL JOURNAL
卷 398, 期 -, 页码 515-519出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20060630
关键词
ADAMTS-2; bone morphogenetic protein 1 (BMP1); extracellular matrix; metalloproteinase; procollagen; tissue inhibitor of metalloproteinase (TIMP)
资金
- NIAMS NIH HHS [R01 AR040994, AR40994] Funding Source: Medline
- NIGMS NIH HHS [GM63471, R01 GM063471, R01 GM071679, GM71679] Funding Source: Medline
ADAMTS-2 is an extracellular metalloproteinase responsible for cleaving the N-propeptides of procollagens I-III; an activity necessary for the formation of collagenous ECM (extracellular matrix). The four TIMPs (tissue inhibitors of metalloprotemases) regulate the activities of matrix metalloproteinases, which are involved in degrading ECM components. Here we delineate the abilities of the TIMPs to affect biosynthetic processing of procollagens. TIMP-1, -2 and -4 show no inhibitory activity towards ADAMTS-2, in addition none of the TIMPs showed inhibitory activity towards bone morphogenetic protein 1, which is responsible for cleaving procollagen C-propeptides. In contrast, TIMP-3 is demonstrated to inhibit ADAMTS-2 in vitro with apparent K-i values of 160 and 602 nM, in the presence of heparin or without respectively; and TIMP-3 is shown to inhibit procollagen processing by cells.
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