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Differential Expression of Calcineurin and SR Ca²⁺ Handling Proteins in Equine Muscle Fibers During Early Postnatal Growth

Karin Eizema, Dianne E. van der Wal, Maarten M.M. van den Burg, Henriëtte W. de Jonge and Maria E. Everts

Department of Pathobiology, Division of Anatomy and Physiology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands

Correspondence to: Karin Eizema, Division of Anatomy and Physiology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.158, NL-3508 TD, Utrecht, The Netherlands. E-mail: c.g.h.eizema{at}vet.uu.nl

During early postnatal development, the myosin heavy chain (MyHC) expression pattern in equine gluteus medius muscle shows adaptation to movement and load,resulting in a decrease in the number of fast MyHC fibers and an increase in the number of slow MyHC fibers. In the present study we correlated the expression of MyHC isoforms to the expression of sarcoplasmic(endo)reticulum Ca²⁺-ATPase 1 and 2a (SERCA), phospholamban (PLB), calcineurin A (CnA), and calcineurin B (CnB). Gluteus medius muscle biopsies were taken at 0, 2, 4, and 48 weeks and analyzed using immunofluorescence. Both SERCA isoforms and PLB were expressed in almost all fiber types at birth. From 4 weeks of age onward, SERCA1 was exclusively expressed in fast MyHC fibers and SERCA2a and PLB in slow MyHC fibers. At all time points, CnA and CnB proteins were expressed at a basal level in all fibers, but with a higher expression level in MyHC type 1 fibers. From 4 weeks onward, expression of only CnA was also higher in MyHC type 2a and 2ad fibers. We propose a double function of calcineurin in calcium homeostasis and maintenance of slow MyHC fiber type identity. Although equine muscle is already functional at birth, expression patterns of the monitored proteins still show adaptation, depending on the MyHC fiber type. (J Histochem Cytochem 55:247–254, 2007)

Key Words: myosin heavy chain • immunofluorescence • signal transduction • differentiation

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