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TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2.

Abstract:

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 metalloproteinases) 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 ...

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Publication status:
Published

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Publisher copy:
10.1042/bj20060630

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Greenspan, DS More by this author
Journal:
The Biochemical journal
Volume:
398
Issue:
3
Pages:
515-519
Publication date:
2006-09-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:f4124577-8f14-463b-8546-7f643ab30d60
Source identifiers:
226536
Local pid:
pubs:226536

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