Fibronectins: multifunctional modular glycoproteins.

Fibronectins: multifunctional modular glycoproteins. Properties o f Fibronectins The basic properties of fibronectins are listed in Table II. The molecule is asymmetric and consists of two similar or identical subunits of molecular weight 220,000 +__20,000 daltons held together by disulfide-bonding near their carboxyl termini. Biophysical measurements indicate that, although the molecule as a whole is flexible, it contains compact globular domains (23, 24). Electron microscopic results confirm the idea that the molecule is extended and flexible (25-27), although the globular domains have not yet been observed by this technique. One important characteristic of fibronectins is that they are capable of interacting specifically with a wide variety of other macromolecules. Table III lists the various interactions, some of which have been studied in more detail than others. The best-established interactions, for which evidence exists both for their occurrence in vivo and for their specificity in vitro, are the interactions with gelatin and collagens, fibrin, factor XIIIa transglutaminase, heparin, and proteoglycans. In addition, it is clear that fibronectins interact with many cells; however, the molecular basis for this interaction remains unclear and is one of the major unanswered questions concerning fibronectins. The binding sites on fibronectins involved in many of these interactions have been http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

Fibronectins: multifunctional modular glycoproteins.

The Journal of Cell Biology, Volume 95 (2): 369 – Oct 1, 1982

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Publisher
Rockefeller University Press
Copyright
Copyright © 1982 by The Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.95.2.369
Publisher site
See Article on Publisher Site

Abstract

Properties o f Fibronectins The basic properties of fibronectins are listed in Table II. The molecule is asymmetric and consists of two similar or identical subunits of molecular weight 220,000 +__20,000 daltons held together by disulfide-bonding near their carboxyl termini. Biophysical measurements indicate that, although the molecule as a whole is flexible, it contains compact globular domains (23, 24). Electron microscopic results confirm the idea that the molecule is extended and flexible (25-27), although the globular domains have not yet been observed by this technique. One important characteristic of fibronectins is that they are capable of interacting specifically with a wide variety of other macromolecules. Table III lists the various interactions, some of which have been studied in more detail than others. The best-established interactions, for which evidence exists both for their occurrence in vivo and for their specificity in vitro, are the interactions with gelatin and collagens, fibrin, factor XIIIa transglutaminase, heparin, and proteoglycans. In addition, it is clear that fibronectins interact with many cells; however, the molecular basis for this interaction remains unclear and is one of the major unanswered questions concerning fibronectins. The binding sites on fibronectins involved in many of these interactions have been

Journal

The Journal of Cell BiologyRockefeller University Press

Published: Oct 1, 1982

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