Matrix metalloproteinases in skin
TLDR
The role of MMPs and TIMPs in human skin based on new observations on the regulation of the expression of M MPs, on their substrate specificily, and MMP expression in physiologic and pathologic conditions of skin involving matrix remodeling are discussed.Abstract:
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases collectively capable of degrading essentially all extracellular matrix components. These enzymes can be produced by several different types of cells in skin such as fibroblasts, keratinocytes, macrophages, endothelial cells, mast cells, and eosinophils and their activity can be specifically inhibited by TIMPs (tissue inhibitors of metalloproteinases), which bind to active MMPs with 1:1 stoichiometry. In general, MMPs are not constitutively expressed in skin but are induced temporarily in response to exogenous signals such as various cytokines, growth factors, cell matrix interactions and altered cell-cell contacts. At present, more evidence is accumulating that MMPs play an important role in proteolytic remodeling of extracellular matrix in various physiologic situations, including developmental tissue morphogenesis, tissue repair, and angiogenesis. On the other hand, MMPs play an important pathogenetic role in excessive breakdown of connective tissue components, e.g. in rheumatoid arthritis, osteoarthritis, chronic ulcers, dermal photoageing, and periodontitis, as well as in tumor cell invasion and metastasis. In this review we discuss the role of MMPs and TIMPs in human skin based on new observations on the regulation of the expression of MMPs, on their substrate specificity, and MMP expression in physiologic and pathologic conditions of skin involving matrix remodeling. Furthermore, therapeutic modalities based on regulating MMP activity will be reviewed.read more
Citations
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References
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Matrix Metalloproteinases: A Review
Henning Birkedal-Hansen,William G. I. Moore,M.K. Bodden,L.J. Windsor,B. Birkedal-Hansen,Arthur A. Decarlo,Jeffrey A. Engler +6 more
TL;DR: The present review discusses in detail the primary structures and the overlapping yet distinct substrate specificities of MMPs as well as the mode of activation of the unique MMP precursors.
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AP-1 function and regulation.
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Journal ArticleDOI
A matrix metalloproteinase expressed on the surface of invasive tumour cells
Hiroshi Sato,Takahisa Takino,Yasunori Okada,Jian Cao,Akira Shinagawa,Etsuhide Yamamoto,Motoharu Seiki +6 more
TL;DR: The cloning of the complemen-tary DNA encoding a new matrix metalloproteinase with a potential transmembrane domain is reported, which may trigger invasion by tumour cells by activating pro-gelatinase A on the tumour cell surface.
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Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase ISOLATION OF THE ACTIVATED FORM OF THE MEMBRANE METALLOPROTEASE
Alex Y. Strongin,Ivan E. Collier,Gregory A. Bannikov,Barry L. Marmer,Gregory A. Grant,Gregory I. Goldberg +5 more
TL;DR: Activation of 72T4Cl on the cell membrane provides a basic mechanism for spatially regulated extracellular proteolysis and presents a new target for prognosis and treatment of metastatic disease.
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Localization of Matrix Metalloproteinase MMP-2 to the Surface of Invasive Cells by Interaction with Integrin αvβ3
Peter C. Brooks,Staffan Strömblad,Luraynne C. Sanders,Tami von Schalscha,Ronald T. Aimes,William G. Stetler-Stevenson,James P. Quigley,David A. Cheresh +7 more
TL;DR: These findings define a single cell-surface receptor that regulates both matrix degradation and motility, thereby facilitating directed cellular invasion.