Ablation of Protein Kinase CK2β in Skeletal Muscle Fibers Interferes with Their Oxidative Capacity.

The tetrameric protein kinase CK2 was identified playing a role at neuromuscular junctions by studying CK2 beta-deficient muscle fibers in mice, and in cultured immortalized C2C12 muscle cells after individual knockdown of CK2 alpha and CK2 beta subunits. In muscle cells, CK2 activity appeared to be at least required for regular aggregation of nicotinic acetylcholine receptors, which serves as a hallmark for the presence of a postsynaptic apparatus. Here, we set out to determine whether any other feature accompanies CK2 beta-deficient muscle fibers. Hind limb muscles gastrocnemius, plantaris, and soleus of adult wildtype and CK2 beta-deficient mice were dissected, cross-sectioned, and stained histochemically by Gomori trichrome and for nicotinamide adenine dinucleotide (NADH) dehydrogenase and succinate dehydrogenase (SDH) enzymatic activities. A reduction of oxidative enzymatic activity was determined for CK2 beta-deficient muscle fibers in comparison with wildtype controls. Importantly, the CK2 beta-deficient fibers, muscle fibers that typically exhibit high NADH dehydrogenase and SDH activities, like slow-type fibers, showed a marked reduction in these activities. Altogether, our data indicate additional impairments in the absence of CK2 beta in skeletal muscle fibers, pointing to an eventual mitochondrial myopathy.