Linked Life Data

15137052

Source:http://linkedlifedata.com/resource/pubmed/id/15137052

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-5-11
pubmed:abstractText
Matrix metalloproteinases (MMPs) are multidomain zinc-dependent proteolytic enzymes that play pivotal roles in many normal and pathological processes. Some members of the MMP family are anchored to the plasma membrane via specialized domains and thus are perfectly suited for pericellular proteolysis. Membrane-anchoring also confers the membrane type-MMPs (MT-MMPs) a unique and complex array of regulatory processes that endow cells with the ability to control MT-MMP-dependent proteolytic activity independently of the levels of endogenous protease inhibitors. Emerging evidence indicates that mechanisms as diverse as autocatalytic processing, ectodomain shedding, homodimerization and internalization can all contribute to the modulation of MT-MMP activity on the cell surface. How these distinct processes interact to attain the optimal level of enzyme activity in a particular setting and the molecular signals that trigger them constitute a new paradigm in MMP regulation. This review will discuss the recent findings concerning these diverse regulatory mechanisms in the context of MT1-MMP (MMP-14).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9541
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP).
pubmed:affiliation
Department of Pathology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review