JACC: Basic to Translational Science (Sep 2019)

Platelet Acetyl-CoA Carboxylase Phosphorylation

  • Shakeel Kautbally, MD,
  • Sophie Lepropre, PhD,
  • Marie-Blanche Onselaer, PhD,
  • Astrid Le Rigoleur, MD,
  • Audrey Ginion, MS,
  • Christophe De Meester de Ravenstein, PhD,
  • Jerome Ambroise, PhD,
  • Karim Z. Boudjeltia, PhD,
  • Marie Octave, MS,
  • Odile Wéra, MS,
  • Alexandre Hego, BSc,
  • Joël Pincemail, PhD,
  • Jean-Paul Cheramy-Bien,
  • Thierry Huby, PhD,
  • Martin Giera, PhD,
  • Bernhard Gerber, MD, PhD,
  • Anne-Catherine Pouleur, MD, PhD,
  • Bruno Guigas, PhD,
  • Jean-Louis Vanoverschelde, MD, PhD,
  • Joelle Kefer, MD, PhD,
  • Luc Bertrand, PhD,
  • Cécile Oury, PhD,
  • Sandrine Horman, PhD,
  • Christophe Beauloye, MD, PhD

Journal volume & issue
Vol. 4, no. 5
pp. 596 – 610


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Summary: 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. Key Words: AMPK, acetyl-CoA carboxylase, coronary artery disease, lipidomics, platelet