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A more recent version of this article appeared on November 1, 2006

Papers In Press, published online ahead of print August 12, 2006
J. Lipid Res., doi:10.1194/jlr.M600247-JLR200
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Submitted on June 7, 2006
Revised on July 28, 2006
Accepted on August 11, 2006

Decrease in intramuscular lipid droplets and translocation of hormone-sensitive lipase in response to muscle contraction and epinephrine

Clara Prats, Morten Donsmark, Klaus Qvortrup, Constantine Londos, Carole Sztalryd, Cecilia Holm, Henrik Galbo, and Thorkil Ploug

Medical Physiology, Copenhagen University. Panum Institute., Copenhagen 2200 N

Corresponding Author: cprats{at}mfi.ku.dk

A better understanding of skeletal muscle lipid metabolism is needed in order to identify the molecular mechanisms relating intramuscular triglyceride (IMTG) to muscle metabolism and insulin sensitivity. An increasing number of proteins have been reported to be associated with intracellular triglyceride (TG), among them the PAT family members; Perilipin, ADRP and Tip47. Hormone-sensitive lipase (HSL) is thought to be the major enzyme responsible for IMTG hydrolysis in skeletal muscle. In adipocytes, regulation of HSL by intracellular redistribution has been demonstrated. The existence of such regulatory mechanism in skeletal muscle has long been hypothesized but never been demonstrated. The aim of this study was to characterize the PAT family proteins associated to IMTG, and to investigate the effect of epinephrine stimulation or muscle contraction on skeletal muscle TG content and HSL intracellular distribution. Rat soleus muscles were either incubated with epinephrine or electrically stimulated for 15 min. Single muscle fibers were used for morphological analysis by confocal and transmission electron microscopy. We show a decrease in IMTG in response to both lipolytic stimuli. Furthermore, we identify two PAT family proteins, ADRP and TIP47, associated with IMTG. Finally, we demonstrate HSL translocation to IMTG and ADRP after stimulation with epinephrine or contraction.


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