《Am J Physiol Cell Physiol 303 C65》.pdf

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《Am J Physiol Cell Physiol 303 C65》.pdf

Am J Physiol Cell Physiol 303: C654–C665, 2012. First published July 3, 2012; doi:10.1152/ajpcell.00180.2012. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers Noni T. Larkins, Robyn M. Murphy, and Graham D. Lamb Department of Zoology, La Trobe University, Melbourne, Victoria, Australia Submitted 31 May 2012; accepted in final form 30 June 2012 Larkins NT, Murphy RM, Lamb GD. Influences of temperature, ing of three important HSPs present in rat skeletal muscle oxidative stress, and phosphorylation on binding of heat shock proteins in fibers, namely B-crystallin, HSP25 (also known as HSP27), skeletal muscle fibers. Am J Physiol Cell Physiol 303: C654–C665, 2012. and HSP72 (also known as HSP70). First published July 3, 2012; doi:10.1152/ajpcell.00180.2012.—Heat In nonstressed muscle fibers the majority (80% to 95%) of shock proteins (HSPs) help maintain cellular function in stressful each of these HSPs is readily diffusible within the cytoplasmic situations, but the processes controlling their interactions with target proteins are not well defined. This study examined the binding of space (2, 16, 20, 21, 26, 39). Following various stress inter- HSP72, HSP25, and B-crystallin in skeletal muscle fibers following ventions the two small HSPs, HSP25 and B-crystallin, have various stresses. Rat soleus (SOL) and extensor digitorum longus been found to bind to a wide variety of different cytoskeletal/ (EDL) muscles were subjected in vitro to heat stress or strongly myofibrillar proteins (2, 16), including desmin (15, 19, 20, 38), fatiguing stimulation. Superficial fibers were “skinned” by microdis- titin (15), actin (28, 43)

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