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1 Medicine, Duke University Medical Center, Durham, NC, USA; Life Science, The University of Tokyo, Tokyo, Japan
2 Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC, USA
3 Medicine, Duke University Medical Center, Durham, NC, USA
* To whom correspondence should be addressed. E-mail: zhen.yan{at}duke.edu.
Mammalian skeletal muscles undergo adaptation in response to alteration in functional demands by means of a variety of cellular signaling events. Previous experiments in transgenic mice show that an active form of Ca2+/calmodulin-dependent protein kinase IV (CaMKIV) is capable of stimulating peroxisome proliferator activated receptor 
co-activator 1
(PGC-1) gene expression, promoting fast-to-slow fiber type switching and augmenting mitochondrial biogenesis in skeletal muscle. However, a role for endogenous CaMKIV in skeletal muscle has not been rigorously investigated. Here we report that genetically modified mice devoid of CaMKIV have relatively normal fiber type composition and mitochondrial enzyme expression in fast-twitch skeletal muscles and responded to long-term voluntary running (4 weeks) with increased expression of myosin heavy chain IIa (MHC IIa), myoglobin, PGC-1 and cytochrome c oxidase IV (COXIV) proteins in plantaris muscle in a manner similar to wild type mice. Short-term motor nerve stimulation (2 hr at 10 Hz) likewise increased PGC-1 mRNA expression in tibialis anterior muscles in both Camk4-/- and wild-type mice. In addition, we confirmed that no detectable CaMKIV protein is expressed in mouse skeletal muscle. Thus, CaMKIV is not required for the maintenance of slow muscle phenotype, and endurance training-induced mitochondrial biogenesis and IIb-to-IIa fiber type switching in mouse skeletal muscle. Other protein kinases sharing substrates with constitutively active CaMKIV may function as endogenous mediators of activity-dependent changes in myofiber phenotype.
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