Thromb Haemost 2005; 94(06): 1203-1212
DOI: 10.1160/TH04-11-0765
Platelets and Blood Cells
Schattauer GmbH

Platelet adhesion: Structural and functional diversity of short dystrophin and utrophins in the formation of dystrophinassociated-protein complexes related to actin dynamics

Doris Cerecedo*
1   Departamento Bioquímica, CINVESTAV, D.F., México
,
Dalila Martínez-Rojas
2   Departamento Fisiología, Biofísica y Neurociencias, CINVESTAV
,
Oscar Chávez
2   Departamento Fisiología, Biofísica y Neurociencias, CINVESTAV
,
Francisco Martínez-Pérez
2   Departamento Fisiología, Biofísica y Neurociencias, CINVESTAV
,
Francisco García-Sierra
3   Departamento Biología Celular, CINVESTAV, México
,
Álvaro Rendon
4   Laboratoire de Physiopathologie Cellulaire et Moléculaire de la Rétine, INSERM-U592, Hopital Saint-Antoine, Paris, France
,
Dominique Mornet
5   Muscles et Pathologies Chroniques, Institut de Biologie, Montpellier, France
,
Ricardo Mondragón
1   Departamento Bioquímica, CINVESTAV, D.F., México
› Author Affiliations
Further Information

Publication History

Received 26 November 2004

Accepted after resubmission 17 September 2005

Publication Date:
07 December 2017 (online)

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Summary

Platelets are dynamic cell fragments that modify their shape during activation. Utrophin and dystrophins are minor actin-binding proteins present in muscle and non-muscle cytoskeleton. In the present study, we characterised the pattern of Dp71 isoforms and utrophin gene products by immunoblot in human platelets. Two new dystrophin isoforms were found, Dp71f and Dp71d, as well as the Up71 isoform and the dystrophin-associated proteins, α and β-dystrobrevins. Distribution of Dp71d/Dp71Δ110 m, Up400/Up71 and dystrophin-associated proteins in relation to the actin cytoskeleton was evaluated by confocal microscopy in both resting and platelets adhered on glass. Formation of two dystrophin-associated protein complexes (Dp71d/Dp71Δ110 m ~DAPC and Up400/Up71~DAPC) was demonstrated by co-immunoprecipitation and their distribution in relation to the actin cytoskeleton was characterised during platelet adhesion. The Dp71d/Dp71Δ110 m ~DAPC is maintained mainly at the granulomere and is associated with dynamic structures during activation by adhesion to thrombin-coated surfaces. Participation of both Dp71d/Dp71Δ110 m ~DAPC and Up400/Up71~DAPC in the biological roles of the platelets is discussed.

* Present address: Departamento Morfología. Escuela Nacional de Ciencias Biológicas, IPN, D.F., México