Proteolytic modification of laminins: functional consequences.
The laminin family contains a number of complex, multi-domain proteins that participate in a large variety of biologic processes. Limited proteolysis has been utilized extensively as a tool with which to determine laminin structure/function relationships. In addition, proteolytic modification of laminins may occur as a component of heterotrimer assembly and secretion, or may follow incorporation of mature laminin into the extracellular matrix. Conversely, laminin binding to cellular receptors may also influence proteinase expression. This review will highlight specific examples to demonstrate the functional interplay between laminins and proteinases in the regulation of laminin structure and function as well as in the subsequent control of proteinase expression.
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Department of Obstetrics and Gynecology, Northwestern University Medical School, Chicago, Illinois 60611, USA. mss130@nwu.edu
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D000818:Animals; D015815:Cell Adhesion Molecules / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D007797:Laminin / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D013329:Structure-Activity Relationship; D000097794:Kalinin
D015815:Cell Adhesion Molecules; D010450:Endopeptidases; D007797:Laminin; D000097794:Kalinin; C121346:laminin 1