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PMID: 17702616 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis.

Seminars in cell & developmental biology ·Vol. 19 ·No. 1 ·2008-02-00 ·Pages 24-33

Barbolina MV, Stack MS

Abstract

Enzymes in the matrix metalloproteinase (MMP) family have been linked to key events in developmental biology for almost 50 years. Biochemical, cellular and in vivo analyses have established that pericellular proteolysis contributes to numerous aspects of ontogeny including ovulation, fertilization, implantation, cellular migration, tissue remodeling and repair. Surface anchoring of proteinase activity provides spatial restrictions on substrate targeting. This review will utilize membrane type 1 MMP (MT1-MMP) as an example to highlight substrate diversity in pericellular proteolysis catalyzed by a membrane anchored MMP.

MeSH Terms
Animals Cell Adhesion Molecules/metabolism Extracellular Matrix/metabolism Extracellular Space/metabolism Humans Matrix Metalloproteinase 14/metabolism Membrane Glycoproteins/metabolism Models, Biological Protein Processing, Post-Translational Proteoglycans/metabolism Substrate Specificity
Chemicals
Cell Adhesion Molecules Membrane Glycoproteins Proteoglycans Matrix Metalloproteinase 14
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Barbolina Maria V
Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208, USA.
Stack M Sharon
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Article Info
Journal
Seminars in cell & developmental biology
Abbr.
Semin Cell Dev Biol
ISSN
1084-9521
DOI
10.1016/j.semcdb.2007.06.008
Published
2008-02-00
Epub
2007-00-10
Pages
24-33
Language
English
Region
England
NLM ID
9607332
PMCID
PMC2685078
Subset
IM
Grants
NCI NIH HHS · R01 CA086984 · United States
NCI NIH HHS · R01 CA086984-10 · United States
NCI NIH HHS · R01CA86984 · United States
External Links
PubMed source DOI: 10.1016/j.semcdb.2007.06.008 PMC Full Text View journal details
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