Membrane dynamic alterations associated with activation of human platelets by thrombin.
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.
D001792:Blood Platelets / Q000187:drug effects / Q000648:ultrastructure*; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure; D004161:Diphenylhexatriene; D004492:Edetic Acid; D006801:Humans; D010078:Oxazines; D010974:Platelet Aggregation / Q000187:drug effects; D013050:Spectrometry, Fluorescence; D013917:Thrombin / Q000494:pharmacology*
D010078:Oxazines; D004161:Diphenylhexatriene; C025456:N-carboxymethylisatoic anhydride; D004492:Edetic Acid; D013917:Thrombin