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Membrane associated matrix metalloproteinases in metastasis
Author(s) -
Ellerbroek Shawn M.,
Stack M. Sharon
Publication year - 1999
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199911)21:11<940::aid-bies6>3.0.co;2-j
Subject(s) - matrix metalloproteinase , metastasis , basement membrane , microbiology and biotechnology , gelatinase a , metalloproteinase , biology , extracellular matrix , proteolytic enzymes , context (archaeology) , cell , gelatinase , cancer research , chemistry , enzyme , biochemistry , cancer , genetics , paleontology
Hematogenous metastasis is postulated to involve tumor cell‐initiated degradation of basement membrane barriers and underlying connective tissue matrices. Matrix metalloproteinases (MMP) are zinc‐dependent endopeptidases that have been implicated in the proteolytic events of tumor cell invasion. Research has revealed a class of membrane‐anchored metalloproteinases (MT‐MMPs) and has provided convincing evidence that these enzymes activate latent MMP‐2 (72 kDa gelatinase A) on the cell surface. The activation of plasma membrane associated MMP is a potential mechanism for facilitation of cellular metastasis and requires consideration when addressing potential roles of MMPs in tumor progression. This review focuses on potential in vivo regulatory mechanisms of membrane‐associated MMP activity in the context of tumor cell interaction with matrix macromolecules. BioEssays 1999;21:940–949. © 1999 John Wiley & Sons, Inc.