TY - JOUR
T1 - Role of dystrophins and utrophins in platelet adhesion process
AU - Cerecedo, Doris
AU - Mondragón, Ricardo
AU - Cisneros, Bulmaro
AU - Martínez-Pérez, Francisco
AU - Martínez-Rojas, Dalila
AU - Rendón, Alvaro
PY - 2006/7
Y1 - 2006/7
N2 - Platelets are crucial at the site of vascular injury, adhering to the sub-endothelial matrix through receptors on their surface, leading to cell activation and aggregation to form a haemostatic plug. Platelets display focal adhesions as well as stress fibres to contract and facilitate expulsion of growth and pro-coagulant factors contained in the granules and to constrict the clot. The interaction of F-actin with different actin-binding proteins determines the properties and composition of the focal adhesions. Recently, we demonstrated the presence of dystrophin-associated protein complex corresponding to short dystrophin isoforms (Dp71d and Dp71Δ110m) and the uthophin gene family (Up400 and Up71), which promote shape change, adhesion, aggregation, and granule centralisation. To elucidate participation of both complexes during the platelet adhesion process, their potential association with integrin β-1 fraction and the focal adhesion system (α-actinin, vinculin and talin) was evaluated by immunofluorescence and immunoprecipitation assays. It was shown that the short dystrophin-associated protein complex participated in stress fibre assembly and in centralisation of cytoplasmic granules, while the utrophin-associated protein complex assembled and regulated focal adhesions. The simultaneous presence of dystrophin and utrophin complexes indicates complementary structural and signalling mechanisms to the actin network, improving the platelet haemostatic role.
AB - Platelets are crucial at the site of vascular injury, adhering to the sub-endothelial matrix through receptors on their surface, leading to cell activation and aggregation to form a haemostatic plug. Platelets display focal adhesions as well as stress fibres to contract and facilitate expulsion of growth and pro-coagulant factors contained in the granules and to constrict the clot. The interaction of F-actin with different actin-binding proteins determines the properties and composition of the focal adhesions. Recently, we demonstrated the presence of dystrophin-associated protein complex corresponding to short dystrophin isoforms (Dp71d and Dp71Δ110m) and the uthophin gene family (Up400 and Up71), which promote shape change, adhesion, aggregation, and granule centralisation. To elucidate participation of both complexes during the platelet adhesion process, their potential association with integrin β-1 fraction and the focal adhesion system (α-actinin, vinculin and talin) was evaluated by immunofluorescence and immunoprecipitation assays. It was shown that the short dystrophin-associated protein complex participated in stress fibre assembly and in centralisation of cytoplasmic granules, while the utrophin-associated protein complex assembled and regulated focal adhesions. The simultaneous presence of dystrophin and utrophin complexes indicates complementary structural and signalling mechanisms to the actin network, improving the platelet haemostatic role.
KW - Cytoskeleton
KW - Dystrophin-associated protein complex
KW - Focal complex
KW - Platelet adhesion
KW - Stress fibres
UR - http://www.scopus.com/inward/record.url?scp=33744823841&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2141.2006.06120.x
DO - 10.1111/j.1365-2141.2006.06120.x
M3 - Artículo
SN - 0007-1048
VL - 134
SP - 83
EP - 91
JO - British Journal of Haematology
JF - British Journal of Haematology
IS - 1
ER -