Abstract
The stability and integrity of blood vessels is maintained by many factors in the blood and by an important extracellular layer, the basement membrane, which underlies the endothelium of the vessels. Basement membranes are composed of an organized network of collagen (type IV), heparan sulfate proteoglycan, and glycoproteins such as entactin, fibronectin, and laminin. Laminin is one of the most important and abundant substances in basement membranes. It has a direct role in cell attachment, migration, and induction of the differentiated phenotype of many cells. We have examined and defined the role(s) of laminin and its specific cell-binding sites at the biochemical level using an in vitro angiogenic model. This model involves the differentiation of cultured endothelial cells on a laminin rich reconstituted basement membrane matrix, Matrigel, into capillary-like structures. Synthetic peptides derived from sequences in the laminin A and B1 chains (CTFALRGDNP and CDPGYIGSR) were able to block cell attachment to Matrigel and cell-cell alignment (early events in vessel formation), respectively, and thus inhibit subsequent tube formation. The third biologically active site CSRARKQAASIKVAVSADR) induced the endothelial cells to become migratory and invade into the Matrigel, forming sprouts from the primary capillary-like network. This site also induces angiogenesis in the chick chorioallantoic membrane (CAM) assay. Thus, endothelial cells interact with at least three different sites in laminin and these interactions are important in vessel maintenance and repair.
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Grant, D.S., Kinsella, J., Cid, M.C., Kleinman, H.K. (1992). Specific Laminin Domains Mediate Endothelial Cell Adhesion, Alignment and Angiogenesis. In: Maragoudakis, M.E., Gullino, P., Lelkes, P.I. (eds) Angiogenesis in Health and Disease. NATO ASI Series, vol 227. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3358-0_9
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