Literature DB >> 6265215

The state of actin in activated human platelets.

V Pribluda, F Laub, A Rotman.   

Abstract

The state of platelet actin was determined using a fluorescent method of DNAse I inhibition. Activation of human platelets resulted in mobilization of DNAse-available actin. When platelets were activated with ADP the change in the state of actin was gradual and preceded the secretion. When thrombin was used as an activator, a sharp and rapid decrease in the DNAse-available actin was observed which paralleled the secretion. Inhibition of ADP-induced aggregation (and secretion) by EDTA resulted in a decrease in the rate of change on actin. Inhibition of the thrombin-induced aggregation (but not secretion) by EDTA did not affect the change in the state of actin.

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Year:  1981        PMID: 6265215     DOI: 10.1111/j.1432-1033.1981.tb05332.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  4 in total

1.  The control of cellular shape and motility. Mg2+ and tropomyosin regulate the formation and the dissociation of microfilament bundles.

Authors:  E Grazi; P Cuneo; A Cataldi
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

2.  Isolation and partial characterization of proteins from platelet pseudopods.

Authors:  A Rotman; N Makov; E F Lüscher
Journal:  Proc Natl Acad Sci U S A       Date:  1982-07       Impact factor: 11.205

3.  Hormone-induced actin polymerization in rat hepatoma cells and human leucocytes.

Authors:  K M Rao; J M Betschart; M A Virji
Journal:  Biochem J       Date:  1985-09-15       Impact factor: 3.857

4.  Cytochalasins inhibit arachidonic acid metabolism in thrombin-stimulated platelets.

Authors:  W Siess; E G Lapetina; P Cuatrecasas
Journal:  Proc Natl Acad Sci U S A       Date:  1982-12       Impact factor: 11.205

  4 in total

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