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Acute activation of AMP-activated protein kinase (AMPK) increases monocarboxylate transporter (MCT) expression in skeletal muscle. However, the impact of chronic activation of AMPK on MCT expression in skeletal muscle is unknown. To investigate, MCT1, MCT2, and MCT4 mRNA expression and protein abundance were measured in the longissimus lumborum (glycolytic), masseter (oxidative), and heart from wild-type (control) and AMPK γ3 pigs. The AMPK γ3 gain in function mutation results in AMPK being constitutively active in glycolytic skeletal muscle and increases energy producing pathways. The MCT1 and MCT2 mRNA expression in muscle was lower ( &lt; 0.05) from both wild-type and AMPK γ3 animals compared to other tissues. However, in both genotypes, MCT1 and MCT2 mRNA expression was greater ( &lt; 0.05) in the masseter than the longissimus lumborum. The MCT1 protein was not detected in skeletal muscle, but MCT2 was greater ( &lt; 0.05) in muscles with an oxidative muscle phenotype. Monocarboxylate transporter 2 was also detected in muscle mitochondria and may explain the differences between muscles. The MCT4 mRNA expression was intermediate among all tissues tested and greater ( &lt; 0.05) in the longissimus lumborum than the masseter. Furthermore, MCT4 protein expression in the longissimus lumborum from AMPK γ3 animals was greater ( &lt; 0.05) than in the longissimus lumborum from wild-type animals. In totality, these data indicate that chronic AMPK activation simultaneously increases MCT2 and MCT4 expression in skeletal muscle.

Chronic activation of AMP-activated protein kinase increases monocarboxylate transporter 2 and 4 expression in skeletal muscle1