Membrane dynamic alterations associated with activation of human platelets by thrombin

I. Nathan, G. Fleisher, A. Dvilansky, A. Livne, A. H. Parola

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Two fluorescent probes, N-carboxymethylisatoic anhydride, which binds to membrane proteins, and 1,6-diphenyl-1,3,5-hexatriene, a lipophilic label, have been used to follow membrane microenvironmental changes. Activation of human platelets by thrombin resulted in a simultaneous increase in values of fluorescence polarization (P) of both probes during the stages of shape change and secretion, which further increased during platelet aggregation. The similar pattern of changes in P for both probes indicates the interdependence of lipids and proteins in the activated platelet membrane.

Original languageEnglish
Pages (from-to)417-421
Number of pages5
JournalBiochimica et Biophysica Acta - Biomembranes
Volume598
Issue number2
DOIs
StatePublished - 23 May 1980

Keywords

  • Aggregation
  • Fluorescence polarization
  • Membrane protein
  • Platelet
  • Secretion
  • Thrombin

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