TY - JOUR
T1 - Platelet adhesion
T2 - Structural and functional diversity of short dystrophin and utrophins in the formation of dystrophin-associated-protein complexes related to actin dynamics
AU - Cerecedo, Doris
AU - Martinez-Rojas, Dalila
AU - Chávez, Oscar
AU - Martínez-Pérez, Francisco
AU - García-Sierra, Francisco
AU - Rendon, Álvaro
AU - Mornet, Dominique
AU - Mondragón, Ricardo
PY - 2005/12
Y1 - 2005/12
N2 - 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/Dp71Δ110m, 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/Dp71Δ110m -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/Dp71Δ110m-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/Dp71Δ110m-DAPC and Up400/Up71-DAPC in the biological roles of the platelets is discussed.
AB - 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/Dp71Δ110m, 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/Dp71Δ110m -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/Dp71Δ110m-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/Dp71Δ110m-DAPC and Up400/Up71-DAPC in the biological roles of the platelets is discussed.
KW - Actin structures
KW - Adhesion
KW - Cytoskeleton
KW - Dystrophin-associated protein complexes
KW - Platelet activation
UR - http://www.scopus.com/inward/record.url?scp=29244451826&partnerID=8YFLogxK
U2 - 10.1160/TH04-11-0765
DO - 10.1160/TH04-11-0765
M3 - Artículo
SN - 0340-6245
VL - 94
SP - 1203
EP - 1212
JO - Thrombosis and Haemostasis
JF - Thrombosis and Haemostasis
IS - 6
ER -