| Literature DB >> 17702616 |
Maria V Barbolina1, M Sharon Stack.
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.Entities:
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Year: 2007 PMID: 17702616 PMCID: PMC2685078 DOI: 10.1016/j.semcdb.2007.06.008
Source DB: PubMed Journal: Semin Cell Dev Biol ISSN: 1084-9521 Impact factor: 7.727