Pyruvate dehydrogenase kinase 1 controls triacylglycerol hydrolysis in cardiomyocytes.

• Tác giả: Armando Alcazar, Michael G Atser, Haoning Howard Cen, Peter Crawford, Leonard J Foster, James D Johnson, Connie L K Leung, Leo T Liu, Renata Moravcova, David Perrin, Eric D Queathem, Jason Rogalski, Elyn M Rowe, Chelsea D Wenyonu
• Ngôn ngữ: eng
• Thông tin xuất bản: United States : bioRxiv : the preprint server for biology , 2025
• Bộ sưu tập: NCBI
• ID: 495840

Tóm tắt

Pyruvate dehydrogenase kinase (PDK) 1 is one of four isozymes that inhibit the oxidative decarboxylation of pyruvate to acetyl-CoA via pyruvate dehydrogenase. PDK activity is elevated in fasting or starvation conditions to conserve carbohydrate reserves. PDK has also been shown to increase mitochondrial fatty acid utilization. In cardiomyocytes, metabolic flexibility is crucial for the fulfillment of high energy requirements. The PDK1 isoform is abundant in cardiomyocytes, but its specific contribution to cardiomyocyte metabolism is unclear. Here we show that PDK1 regulates cardiomyocyte fuel preference by mediating triacylglycerol turnover in differentiated H9c2 myoblasts using lentiviral shRNA to knockdown