TY - JOUR
T1 - Utrophins compensate for Dp71 absence in mdx3cv in adhered platelets
AU - Cerecedo, Doris
AU - Mondragón, Ricardo
AU - Candelario, Aurora
AU - García-Sierra, Francisco
AU - Mornet, Dominique
AU - Rendón, Álvaro
AU - Martínez-Rojas, Dalila
PY - 2008/1
Y1 - 2008/1
N2 - Platelet adhesion is a critical step due to its hemostatic role in stopping bleeding after vascular damage. Short dystrophins are the most abundant dmd gene products in nonmuscle tissues, and in association with cytoskeleton proteins contribute to their intrinsic function; while utrophins are dystrophin-homologous related family proteins with structural and functional similarities. We previously demonstrated the presence of Dp71 isoforms, utrophins, and various dystrophin-associated proteins and their participation in cytoskeleton re-organization, filopodia and lamellipodia extension, and in centralizing cytoplasmic granules during the adhesion process of human platelets. To evaluate the morphologic changes and actin-based structures of mdx platelets during the adhesion process, we compared the topographic distribution of Dp71d/Dp71Δ110 and dystrophin-associated protein in adhered platelets from dystrophic mdx mouse. By confocal microscopy, we showed that absence of Dp71 isoforms in platelets from this animal model disrupted dystrophin- associated protein expression and distribution without modifying the platelet morphology displayed during the glass-adhesion process. By immunoprecipitation assays, we proved that up-regulated utrophins were associated with dystrophin-associated proteins to conform the dystrophin-associated protein complex corresponding to utrophins, which might compensate for Dp71 absence in mdx platelets.
AB - Platelet adhesion is a critical step due to its hemostatic role in stopping bleeding after vascular damage. Short dystrophins are the most abundant dmd gene products in nonmuscle tissues, and in association with cytoskeleton proteins contribute to their intrinsic function; while utrophins are dystrophin-homologous related family proteins with structural and functional similarities. We previously demonstrated the presence of Dp71 isoforms, utrophins, and various dystrophin-associated proteins and their participation in cytoskeleton re-organization, filopodia and lamellipodia extension, and in centralizing cytoplasmic granules during the adhesion process of human platelets. To evaluate the morphologic changes and actin-based structures of mdx platelets during the adhesion process, we compared the topographic distribution of Dp71d/Dp71Δ110 and dystrophin-associated protein in adhered platelets from dystrophic mdx mouse. By confocal microscopy, we showed that absence of Dp71 isoforms in platelets from this animal model disrupted dystrophin- associated protein expression and distribution without modifying the platelet morphology displayed during the glass-adhesion process. By immunoprecipitation assays, we proved that up-regulated utrophins were associated with dystrophin-associated proteins to conform the dystrophin-associated protein complex corresponding to utrophins, which might compensate for Dp71 absence in mdx platelets.
KW - Actin-based structures
KW - Adhesion
KW - Cytoskeleton
KW - Dystrophic model
KW - Utrophins
UR - http://www.scopus.com/inward/record.url?scp=37849002783&partnerID=8YFLogxK
U2 - 10.1097/MBC.0b013e3282f102d6
DO - 10.1097/MBC.0b013e3282f102d6
M3 - Artículo
SN - 0957-5235
VL - 19
SP - 39
EP - 47
JO - Blood Coagulation and Fibrinolysis
JF - Blood Coagulation and Fibrinolysis
IS - 1
ER -