Platelet adhesion: Structural and functional diversity of short dystrophin and utrophins in the formation of dystrophinassociated- protein complexes related to actin dynamics
Doris Cerecedo1*, Dalila Martínez-Rojas 2 , Oscar Chávez2 , Francisco Martínez-Pérez 2 , Francisco García-Sierra 3 , Álvaro Rendon 4 , Dominique Mornet 5 , Ricardo Mondragón1
* Present address: Departamento Morfología. Escuela Nacional de Ciencias Biológicas, IPN, D.F., México; 1 Departamento Bioquímica, CINVESTAV, D.F., México, 2 Departamento Fisiología, Biofísica y Neurociencias, CINVESTAV; 3 Departamento Biología Celular,
Summary
Platelets are dynamic cell fragments that modify their shape duringactivation. Utrophin and dystrophins are minor actin-bindingproteins present in muscle and non-muscle cytoskeleton. In thepresent study, we characterised the pattern of Dp71 isoformsand utrophin gene products by immunoblot in human platelets.Two new dystrophin isoforms were found, Dp71f and Dp71d, aswell as the Up71 isoform and the dystrophin-associated proteins,a and ß -dystrobrevins. Distribution of Dp71d/Dp71δ110m ,Up400/Up71 and dystrophin-associated proteins in relation tothe actin cytoskeleton was evaluated by confocal microscopy in both resting and platelets adhered on glass. Formation of twodystrophin-associated protein complexes (Dp71d/Dp71δ110m~DAPC and Up400/Up71~DAPC) was demonstrated by co-immunoprecipitationand their distribution in relation to the actincytoskeleton was characterised during platelet adhesion. TheDp71d/Dp71δ110m ~DAPC is maintained mainly at the granulomereand is associated with dynamic structures during activationby adhesion to thrombin-coated surfaces.Participation ofboth Dp71d/Dp71δ110m~DAPC and Up400/Up71~DAPC in thebiological roles of the platelets is discussed. DOI
http://dx.doi.org/10.1160/TH04-11-0765