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Localizing matrix metalloproteinase activities in the pericellular environment
Author(s) -
Murphy Gillian,
Nagase Hideaki
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07918.x
Subject(s) - matrix metalloproteinase , extracellular matrix , microbiology and biotechnology , metalloproteinase , morphogenesis , cell , chemistry , wound healing , receptor , cell surface receptor , proteolytic enzymes , cell membrane , extracellular , disintegrin , function (biology) , biology , enzyme , biochemistry , immunology , gene
Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface‐bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane‐type MMPs (MT‐MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane‐anchored proteins or cell‐associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.