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PMID: 7378064 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Fibronectin-collagen binding and requirement during cellular adhesion.

The Biochemical journal ·Vol. 186 ·No. 2 ·1980-02-15 ·Pages 551-9

Gold LI, Pearlstein E

Abstract

Fibronectin isolated from human plasma and from the extracellular matrices of cell monolayers mediates the attachment in vitro and spreading of trypsin-treated cells on a collagen substratum. Fibronectin-dependent kinetics of cellular attachment to collagen were studied for several adherent cell types. It was shown that trypsin-treated human umbilical-cord cells, mouse sarcoma CMT81 cells, endothelial cells, and human fibroblasts from a patient with Glanzmann's disease were completely dependent on fibronectin for their attachment to collagen, whereas guinea-pig and monkey smooth-muscle cells and chick-embryo secondary fibroblasts displayed varying degrees of dependence on fibronectin for their attachment. Radiolabelled human plasma fibronectin possessed similar affinity for collagen types I, II and III from a variety of sources. The fibronectin bound equally well to the collagens with or without prior urea treatment. However, in the fibronectin-mediated adhesion assay using PyBHK fibroblasts, a greater number of cells adhered and more spreading was observed on urea-treated collagen. Fibronectin extracted from the extracellular matrix of chick-embryo fibroblasts and that purified from human plasma demonstrated very similar kinetics of complexing to collagencoated tissue-culture dishes. Fibronectin from both sources bound to collagen in the presence of 0.05-4.0m-NaCl and over the pH range 2.6-10.6. The binding was inhibited when fibronectin was incubated with 40-80% ethylene glycol, the ionic detergents sodium dodecyl sulphate and deoxycholate, and the non-ionic detergents Nonidet P-40, Tween 80 and Triton X-100, all at a concentration of 0.1%. From these results we proposed that fibronectin-collagen complexing is mainly attributable to hydrophobic interactions.

MeSH Terms
Animals Cell Adhesion/drug effects Cell Line Collagen/metabolism Detergents/pharmacology Ethylene Glycols/pharmacology Fibronectins/metabolism Humans Hydrogen-Ion Concentration Kinetics Protein Binding
Chemicals
Detergents Ethylene Glycols Fibronectins Collagen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gold L I
Pearlstein E
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1860551
Published
1980-02-15
Pages
551-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1161608
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1860551 PMC Full Text View journal details
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