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Fibronectin and its Receptors

Fibronectin and its Receptors PERSPECTIVES AND SUMMARY Fibronectin is a multifunctional extracellular matrix and plasma protein that plays a central role in cell adhesion. Intensive research on fibronectin has made it a prototype cell adhesion protein. These studies began with the discovery in the early 1970s by several laboratories of a fibroblast cell-surface protein that was absent at the surface of the transformed cells used for comparison and that had a counterpart circulating in plasma (1-8). The plasma form of this protein was subsequently shown (9) to be identical to a previously known plasma protein, "cold insoluble globulin," which had been 0066-4154/88/0701-0375$02.00 RUOSLAHTI identified independently in studies on fibrinogen and other blood-clotting proteins ( 1 0-12). The various forms of this protein were collectively named "fibronectin." The independent discovery of the cell attachment-promoting activity of a plasma protein ( 13) subsequently identified as fibronectin ( 1 4 , 15) gave fibronectin its most celebrated activity, its ability t o interact with cells to promote cell attachment. The realization that fibronectin was an extracellular matrix protein rather than a cell-surface protein (16), together with the discovery that fibronectin could bind to a number of other proteins­ most significantly collagen (17), glycosaminoglycans, and proteoglycans http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biochemistry Annual Reviews

Fibronectin and its Receptors

Ruoslahti, E
Annual Review of Biochemistry , Volume 57 (1) – Jul 1, 1988
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Publisher
Annual Reviews
Copyright
Copyright 1988 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0066-4154
eISSN
1545-4509
DOI
10.1146/annurev.bi.57.070188.002111
pmid
2972252
Publisher site
See Article on Publisher Site

Abstract

PERSPECTIVES AND SUMMARY Fibronectin is a multifunctional extracellular matrix and plasma protein that plays a central role in cell adhesion. Intensive research on fibronectin has made it a prototype cell adhesion protein. These studies began with the discovery in the early 1970s by several laboratories of a fibroblast cell-surface protein that was absent at the surface of the transformed cells used for comparison and that had a counterpart circulating in plasma (1-8). The plasma form of this protein was subsequently shown (9) to be identical to a previously known plasma protein, "cold insoluble globulin," which had been 0066-4154/88/0701-0375$02.00 RUOSLAHTI identified independently in studies on fibrinogen and other blood-clotting proteins ( 1 0-12). The various forms of this protein were collectively named "fibronectin." The independent discovery of the cell attachment-promoting activity of a plasma protein ( 13) subsequently identified as fibronectin ( 1 4 , 15) gave fibronectin its most celebrated activity, its ability t o interact with cells to promote cell attachment. The realization that fibronectin was an extracellular matrix protein rather than a cell-surface protein (16), together with the discovery that fibronectin could bind to a number of other proteins­ most significantly collagen (17), glycosaminoglycans, and proteoglycans

Journal

Annual Review of Biochemistry – Annual Reviews

Published: Jul 1, 1988

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