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Changes in Exercise-Induced Gene Expression in 5'-AMP–Activated Protein Kinase 3–Null and 3 R225Q Transgenic Mice

¹ Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden
² Department of Surgical Sciences, Karolinska Institutet, Stockholm, Sweden
³ Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China
⁴ Department of Human Physiology, Copenhagen Muscle Research Centre, Institute of Exercise and Sport Sciences, University of Copenhagen, Copenhagen, Denmark
⁵ Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Uppsala, Sweden
⁶ Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala Biomedical Center, Uppsala, Sweden

5'-AMP–activated protein kinase (AMPK) is important for metabolic sensing. We used AMPK3 mutant–overexpressing Tg-Prkag3^225Q and AMPK3-knockout Prkag3^–/– mice to determine the role of the AMPK3 isoform in exercise-induced metabolic and gene regulatory responses in skeletal muscle. Mice were studied after 2 h swimming or 2.5 h recovery. Exercise increased basal and insulin-stimulated glucose transport, with similar responses among genotypes. In Tg-Prkag3^225Q mice, acetyl-CoA carboxylase (ACC) phosphorylation was increased and triglyceride content was reduced after exercise, suggesting that this mutation promotes greater reliance on lipid oxidation. In contrast, ACC phosphorylation and triglyceride content was similar between wild-type and Prkag3^–/– mice. Expression of genes involved in lipid and glucose metabolism was altered by genetic modification of AMPK3. Expression of lipoprotein lipase 1, carnitine palmitoyl transferase 1b, and 3-hydroxyacyl–CoA dehydrogenase was increased in Tg-Prkag3^225Q mice, with opposing effects in Prkag3^–/– mice after exercise. GLUT4, hexokinase II (HKII), and glycogen synthase mRNA expression was increased in Tg-Prkag3^225Q mice after exercise. GLUT4 and HKII mRNA expression was increased in wild-type mice and blunted in Prkag3^–/– mice after recovery. In conclusion, the Prkag3^225Q mutation, rather than presence of a functional AMPK3 isoform, directly promotes metabolic and gene regulatory responses along lipid oxidative pathways in skeletal muscle after endurance exercise.

Abbreviations: ACC, acetyl-CoA carboxylase; AMPK, 5'-AMP–activated protein kinase; CPT1b, carnitine palmitoyl transferase 1b; EDL, extensor digitorum longus; HAD, 3-hydroxyacyl–CoA dehydrogenase; HKII, hexokinase II; IMTG, intramuscular triglyceride; KHBB, Krebs-Henseleit bicarbonate buffer; LPL1, lipoprotein lipase 1

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