IMR Press / FBL / Volume 16 / Issue 2 / DOI: 10.2741/3713

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Cryptic activities of fibronectin fragments, particularly cryptic proteases
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1 Enzymology Laboratory, Research Unit Number 4, University Pierre and Marie Curie, Postal Case 256, 7 Quai Saint Bernard, 75252 Paris Cedex 05, France. maurice.pagano@upmc.fr
Academic Editor:Maurice Pagano
Front. Biosci. (Landmark Ed) 2011, 16(2), 698–706; https://doi.org/10.2741/3713
Published: 1 January 2011
Abstract

Fibronectin (FN) is a modular glycoprotein encoded by a single gene. A soluble form of this protein is found in the plasma of several animals. Alternative splicing of pre-mRNA at three sites produces cellular and plasma FNs. The plasma form contributes to blood clotting and thrombosis. Many extracellular matrices (ECM) contain an FN network associated with a variety of cell activities through binding to cell surface integrin receptors. Fragments of FN can have cryptic activities that are specific to these fragments rather than to the intact protein. The metalloprotease activity present in the basement membrane and plasma fibronectins has been intensively studied in humans, bovine and rats. Organic inhibitors that are selective for the human cryptic enzyme have been produced.

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