par Kautbally, Shakeel;Lepropre, Sophie;Onselaer, Marie Blanche;Le Rigoleur, Astrid;Ginion, Audrey;De Meester de Ravenstein, Christophe;Ambroise, Jerome;Zouaoui Boudjeltia, Karim 
;Octave, Marie;Wéra, Odile;Hego, Alexandre;Pincemail, Joël;Cheramy-Bien, Jean Paul;Huby, Thierry;Giera, Martin;Gerber, Bernhard;Pouleur, Anne-Catherine;Guigas, Bruno;Vanoverschelde, Jean-Louis;Kefer, Joelle;Bertrand, Luc;Oury, Cecile;Horman, Sandrine ;Beauloye, Christophe
Référence JACC: Basic to Translational Science, 4, 5, page (596-610)
Publication Publié, 2019-09
;Octave, Marie;Wéra, Odile;Hego, Alexandre;Pincemail, Joël;Cheramy-Bien, Jean Paul;Huby, Thierry;Giera, Martin;Gerber, Bernhard;Pouleur, Anne-Catherine;Guigas, Bruno;Vanoverschelde, Jean-Louis;Kefer, Joelle;Bertrand, Luc;Oury, Cecile;Horman, Sandrine ;Beauloye, ChristopheRéférence JACC: Basic to Translational Science, 4, 5, page (596-610)
Publication Publié, 2019-09
Article révisé par les pairs
| Résumé : | Adenosine monophosphate–activated protein kinase (AMPK) acetyl-CoA carboxylase (ACC) signaling is activated in platelets by atherogenic lipids, particularly by oxidized low-density lipoproteins, through a CD36-dependent pathway. More interestingly, increased platelet AMPK–induced ACC phosphorylation is associated with the severity of coronary artery calcification as well as acute coronary events in coronary artery disease patients. Therefore, AMPK–induced ACC phosphorylation is a potential marker for risk stratification in suspected coronary artery disease patients. The inhibition of ACC resulting from its phosphorylation impacts platelet lipid content by down-regulating triglycerides, which in turn may affect platelet function. |
