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PMID: 522486 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cell surface fibronectin and oncogenic transformation.

Journal of supramolecular structure ·Vol. 11 ·No. 1 ·1979-00-00 ·Pages 95-104

Hynes RO, Destree AT, Perkins ME, Wagner DD

Abstract

Fibronectin is a large glycoprotein at the cell surface of many different cell types; a related protein is present in plasma. Fibronectin is a dimer of 230,000-dalton subunits and also occurs in larger aggregates; it forms fibrillar networks at the cell surface, between cells and substrata and between adjacent cells, and it is not a typical membrane protein. Cell surface fibronectin is reduced in amount or absent on transformed cells and in many cases its loss correlates with acquisition of tumorigenicity and, in particular, metastatic ability. Exceptions to the correlations with transformation and tumorigenicity exist. Loss of fibronectin and the resulting reduced adhesion appear to be involved in pleiotropic alterations in cell behavior and may be responsible for several aspects of the transformed phenotype in vitro. Fibronectin interacts with other macromolecules (collagen/gelatin, fibrin/fibrinogen, proteoglycans) and is apparently connected to microfilaments inside the cell.

MeSH Terms
Animals Cell Membrane/ultrastructure Cell Transformation, Neoplastic Fibroblasts/ultrastructure Fibronectins Membrane Proteins/metabolism Protein Binding
Chemicals
Fibronectins Membrane Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hynes R O
Destree A T
Perkins M E
Wagner D D
Article Info
Journal
Journal of supramolecular structure
Abbr.
J Supramol Struct
ISSN
0091-7419
Published
1979-00-00
Pages
95-104
Language
English
Region
United States
NLM ID
0330464
Subset
IM
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