Organization of extracellular proteins on the connective tissue cell surface: relevance to cell-matrix interactions in vitro and in vivo.
A model has been developed that proposes a cell surface-associated protein meshwork, composed in part of fibronectin and collagen, for a connective tissue cell attached to a substratum. In support of this model are the observations that collagen and fibronectin interact and that these proteins are similarly distributed on the fibroblast cell surface. We suggest that this external meshwork interacts directly or indirectly with the internal cytoskeleton and with the extracellular matrix and thereby mediates several cellular properties, including adhesion, shape, and motility. Loss of cell surface fibronectin as a result of viral transformation, or due to treatment of normal cells with tunicamycin, an inhibitor of protein glycosylation, may contribute to the reduced adhesion and altered morphology observed in these circumstances. We therefore predict that the changes in these properties observed with virally transformed cells, mitotic cells, and cells treated with proteolytic enzymes are related to alterations in the external protein meshwork.
D000818:Animals; D002448:Cell Adhesion; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism; D003238:Connective Tissue / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D005110:Extracellular Space / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological
D005353:Fibronectins; D003094:Collagen