Fluorescence studies of the blood platelet membranes associated with fibrinogen.
To follow microviscosity changes in membranes associated with fibrinogen binding to human platelets, specific fluorescent probes were used and their fluorescence anisotropy was analysed. The degree of fluorescence anisotropy of diphenylhexatriene, anilinonaphthalene sulfonate (ANS) and fluorescamine increased significantly when fibrinogen reacted with its membrane receptors. Fluorescence polarization analyses showed that fibrinogen binding to platelet membranes is accompanied by an increase in the membrane lipid rigidity. On the other hand, changes in the fluorescence anisotropy of membrane tryptophans and N-(3-pyrene)maleimide suggest augmented mobility of the membrane proteins. The binding of fibrinogen to the membrane receptors is not accompanied by any change in the fluorescence intensity of ANS attached to the membranes. This may suggest that covering of platelets with fibrinogen molecules does not influence the surface membrane charge.
D001792:Blood Platelets / Q000378:metabolism / Q000648:ultrastructure*; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D005340:Fibrinogen / Q000378:metabolism*; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D006801:Humans; D014783:Viscosity
D005456:Fluorescent Dyes; D005340:Fibrinogen