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Journal of Lipid Research, Vol. 46, 2614-2623, December 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology

Transcriptome and proteome analysis of soleus muscle of hormone-sensitive lipase-null mice

Ola Hansson^1,*, Morten Donsmark, Charlotte Ling, Pernilla Nevsten^**, Mikael Danfelter^*, Jesper L. Andersen, Henrik Galbo and Cecilia Holm^*

^* Department of Experimental Medical Science, Lund University, Lund, Sweden
Copenhagen Muscle Research Center, Department of Medical Physiology, The Panum Institute, University of Copenhagen, Copenhagen, Denmark
Department of Clinical Sciences, Lund University, Malmoe, Sweden
^** National Center for High-Resolution Electron Microscopy, Lund University, Lund, Sweden
Copenhagen Muscle Research Center, Department of Molecular Muscle Biology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

Published, JLR Papers in Press, September 30, 2005. DOI 10.1194/jlr.M500028-JLR200

¹ To whom correspondence should be addressed. e-mail: ola.hansson{at}med.lu.se

Hormone-sensitive lipase (HSL), a key enzyme in fatty acid mobilization in adipocytes, has been demonstrated also in skeletal muscle. To gain further insight into the role and importance of HSL in skeletal muscle, a transcriptome analysis of soleus muscle of HSL-null mice was performed. A total of 161 transcripts were found to be differentially expressed. Increased mRNA levels of fructose-1,6-bisphosphatase, fructose-2,6-bisphosphatase, and phosphorylase kinase 1A suggest a higher glycogen flux in soleus muscle of HSL-null mice. An observed increase in the utilization of glycogen stores supports this finding. Moreover, an increased amount of intramyocellular lipid droplets, observed by transmission electron microscopy, suggests decreased mobilization of lipid stores in HSL-null mice. To complement the transcriptome data, protein expression analysis was performed. Five spots were found to be differentially expressed: pyruvate dehydrogenase E1, creatine kinase (CK), ankyrin-repeat domain 2, glyceraldehyde-3-phosphate dehydrogenase, and one protein yet to be identified. The increased protein level of CK indicates creatine phosphate degradation to be of increased importance in HSL-null mice.

The results of this study suggest that in the absence of HSL, a metabolic switch from reliance on lipid to carbohydrate energy substrates takes place, supporting an important role of HSL in soleus muscle lipid metabolism.

Supplementary key words skeletal muscle • metabolic switch • glycogen • proteomics

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