Literature DB >> 141204

Platelet aggregation and the ouabain-insensitive ATPase. Ecto-ATPase, reflection of membrane integrity.

T Y Wang, C V Hussey, E A Sasse, L L Hause.   

Abstract

The ecto-ATPase activity of washed human platelets has been characterized by a higher-performance liquid chromatographic method. Mg++ was found to stimulate ecto-ATPase activity more strongly than Ca++. The combination of Mg++ and Ca++ at increasing concentrations caused diminishing activity levels. Elevated ecto-ATPase activity was also found in platelets incubated with prostaglandin E1 (PGE1) or potassium cyanide (KCN). It is proposed that the increase of ecto-ATPase activity is related to the extrusion or exposure of plasma membrane containing a ouabain-insensitive ATPase. The role of ecto-ATPase in platelet aggregation is discussed in light of these findings.

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Year:  1977        PMID: 141204     DOI: 10.1093/ajcp/67.6.528

Source DB:  PubMed          Journal:  Am J Clin Pathol        ISSN: 0002-9173            Impact factor:   2.493


  2 in total

1.  Effects of calcium, lanthanum, and temperature on the fluidity of spin-labeled human platelets.

Authors:  R D Sauerheber; T S Zimmermann; J A Esgate; W P VanderLaan; L M Gordon
Journal:  J Membr Biol       Date:  1980       Impact factor: 1.843

Review 2.  Origin, metabolism and function of extracellular adenine nucleotides in the blood.

Authors:  J Lüthje
Journal:  Klin Wochenschr       Date:  1989-03-15
  2 in total

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