NDLI: Functional domain structure of fibronectin.

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Functional domain structure of fibronectin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hakomori, S. Sekiguchi, K.
Abstract	Structural domains of fibronectin (FN) and their ability to associate with cell surface components have been systematically investigated. Plasma FN was cleaved into three structural domains (Mr 150,000-140,000, 40,000, and 32,000) by sequential digestion with trypsin and thermolysin. A single digestion with thermolysin alone generated Mr 150,000-140,000, 40,000, and smaller fragments. With the inclusion of thermolysin, but not with other proteases, one can, with a high yield dissect FN simultaneously into three clearly distinctive functional domains. Of three major fragments only the Mr 40,000 fragment bound to a gelatin column; this fragment contained essentially all of the carbohydrates present in the original FN. In contrast, heparin-binding sites were localized on both the Mr 150,000-140,000 and 32,000 fragments but not on the Mr 40,000 fragment. Only the Mr 150,000-140,000 fragments and intact FN promoted cell spreading, whereas the Mr 40,000 and 32,000 fragments could induce cell attachment but failed to promote cell spreading. These results indicate that FN is composed of (at least) three structural domains that are functionally distinct from each other.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	77
Language	English
Publisher	National Academy of Sciences
Publisher Date	1980-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Adhesion Collagen Metabolism Fibronectins Heparin Animals Binding Sites Cricetinae Peptide Fragments Peptide Hydrolases Protein Conformation Structure-Activity Relationship Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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