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SYNDECAN-4 HEPARAN-SULFATE PROTEOGLYCAN IS A SELECTIVELY ENRICHED AND WIDESPREAD FOCAL ADHESION COMPONENT
Author(s): WOODS A, COUCHMAN JR
Source: MOLECULAR BIOLOGY OF THE CELL    Volume: 5    Issue: 2    Pages: 183-192    Published: FEB 1994  
Times Cited: 212     References: 43     
Abstract: Focal adhesion formation in fibroblasts results from complex transmembrane signaling processes initiated by extracellular matrix molecules. Although a role for integrins with attendant tyrosine kinases has been established, there is evidence that cell surface heparan sulfate proteoglycans (HSPGs) are also involved with an associated role of protein kinase C. The identity of the proteoglycan has remained elusive, but we now report that syndecan 4 (ryudocan/amphiglycan) is present in focal adhesions of a number of cell types. Affinity-purified antibodies raised against a unique portion of the cytoplasmic domain of syndecan 4 core protein recognized an HSPG of similar characteristics to those of syndecan 4. These antibodies stained focal adhesions only after cell permeabilization and recognized differing mammalian species. Syndecan 4 was associated with focal adhesions that contained either beta1 or beta3 integrin subunits and those that formed on substrates of fibronectin, laminin, vitronectin, or type I collagen. No focal adhesions were found that were vinculin-containing but lacked syndecan 4. In contrast, syndecan 2, whose cytoplasmic domain is closely homologous to syndecan 4, does not appear to be a focal adhesion component. Thus, syndecan 4 represents a new transmembrane focal adhesion component, probably involved in their assembly.
Document Type: Article
Language: English
Reprint Address: WOODS, A (reprint author), UNIV ALABAMA, DEPT CELL BIOL, BIRMINGHAM, AL 35294 USA
Publisher: AMER SOC CELL BIOLOGY, PUBL OFFICE, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814
Subject Category: Cell Biology
IDS Number: ND200
ISSN: 1059-1524
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