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Fibronectin potentiates actin polymerization in thrombin‐activated platelets
Author(s) -
Cierniewski Czeslaw S.,
Karczewski Jerzy,
Kowalska Maria A.
Publication year - 1986
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240300108
Subject(s) - fibronectin , chemistry , polymerization , actin , cytoskeleton , microbiology and biotechnology , actin cytoskeleton , thrombin , actin remodeling , biophysics , actin binding protein , platelet , biochemistry , biology , immunology , cell , polymer , organic chemistry
The effect of fibronectin on the polymerization state of actin was studied. Triton X‐100‐insoluble cytoskeleton was prepared from thrombin‐activated platelets, and the conversion of G‐actin into F‐actin was monitored by an assay involving DNase I inhibition by G‐actin. It was found that fibronectin bound to membrane receptors decreased the level of platelet G‐actin. This observation suggests that in the presence of fibronectin a larger amount of F‐actin becomes incorporated into the Triton X‐100‐insoluble cytoskeleton. At the same molar concentration, fibrinogen only slightly increased actin polymerization, whereas bovine serum albumin at a much higher concentration caused a small inhibition of actin immobilization. Our data show that fibronectin, through interaction with the platelet actomyosin fibrillar system, facilitates actin polymerization into the cytoskeleton.