Critical role of membrane-type 1 matrix metalloproteinase in collagen phagocytosis by fibroblasts.
Published: 2007
Language: eng
Number of pages: 89
ISBN-13: 9780494274323
Description: Degradation of collagen is important for the physiological remodelling of connective tissues during growth and development, as well as in wound healing, inflammatory diseases, and cancer cell invasion. In remodelling adult tissues, degradation of collagen occurs primarily through a phagocytic pathway. While various steps in this pathway have been characterized, the enzyme required to initially fragment collagen fibrils for subsequent phagocytosis has not been identified. Using laser confocal microscopy, TEM, and biochemical assays, fibroblasts were shown to initiate degradation of collagen through the collagenolytic activity of the membrane-bound metal lop roteinase, MT1-MMP. Degradation of natural and reconstituted collagen substrates correlated with the expression of MT1-MMP, which was localized at sites of collagen cleavage at the cell surface and also within the cells. In contrast, the gelatinolytic activity of MMP-2 was not required for collagen phagocytosis. These studies demonstrate a pivotal role of catalytically active MT1-MMP in preparing collagen fibrils for phagocytic degradation.
Notes: Source: Masters Abstracts International, Volume: 45-06, page: 3057.

Thesis (M.Sc.)--University of Toronto, 2007.

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