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Am J Physiol Cell Physiol 283: C1761-C1775, 2002. First published August 22, 2002; doi:10.1152/ajpcell.00278.2002
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Vol. 283, Issue 6, C1761-C1775, December 2002

Divergence in species and regulatory role of beta -myosin heavy chain proximal promoter muscle-CAT elements

Richard W. Tsika1,2,3, John McCarthy2, Natalia Karasseva1, Yangsi Ou2, and Gretchen L. Tsika2

1 Department of Biochemistry, School of Medicine, 2 Department of Biomedical Sciences, School of Veterinary Medicine, and 3 Dalton Cardiovascular Research Center, University of Missouri-Columbia, Columbia, Missouri 65211

We examined the functional role of distinct muscle-CAT (MCAT) elements during non-weight-bearing (NWB) regulation of a wild-type 293-base pair beta -myosin heavy chain (beta MyHC) transgene. Electrophoretic mobility shift assays (EMSA) revealed decreased NTEF-1, poly(ADP-ribose) polymerase, and Max binding at the human distal MCAT element when using NWB soleus vs. control soleus nuclear extract. Compared with the wild-type transgene, expression assays revealed that distal MCAT element mutation decreased basal transgene expression, which was decreased further in response to NWB. EMSA analysis of the human proximal MCAT (pMCAT) element revealed low levels of NTEF-1 binding that did not differ between control and NWB extract, whereas the rat pMCAT element displayed robust NTEF-1 binding that decreased when using NWB soleus extracts. Differences in binding between human and rat pMCAT elements were consistent whether using rat or mouse nuclear extract or in vitro synthesized human TEF-1 proteins. Our results provide the first evidence that 1) different binding properties and likely regulatory functions are served by the human and rat pMCAT elements, and 2) previously unrecognized beta MyHC proximal promoter elements contribute to NWB regulation.

skeletal muscle hypertrophy; skeletal muscle atrophy; fiber-type transitions; chloramphenicol acetyltransferase


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