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Articles in PresS, published online ahead of print August 22, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00278.2002
Submitted on June 18, 2002
Accepted on August 15, 2002
1 Biochemistry, School of Medicine, University of Missouri, Columbia, MO, USA; Biomedical Sciences, School of Veterinary Medicine, University of Missouri, Columbia, MO, USA; Dalton Cardiovascular Research Center, University of Missouri, Columbia, MO, USA
2 Biomedical Sciences, School of Veterinary Medicine, University of Missouri, Columbia, MO, USA
3 Biochemistry, School of Medicine, University of Missouri, Columbia, MO, USA
* To whom correspondence should be addressed. E-mail: tsikag{at}missouri.edu.
We examined the functional role of distinct MCAT elements during non-weight-bearing (NWB) regulation of a wild-type 293-base pair ßMyosin Heavy Chain (ßMyHC) transgene. Electrophoretic mobility shift assays (EMSA) revealed decreased NTEF-1, PARP and Max binding at the human distal-MCAT element when using NWB-soleus versus control soleus nuclear extract. When compared to 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 element revealed low levels of NTEF-1 binding that did not differ between control and NWB extract, whereas the rat proximal-MCAT element displayed robust NTEF-1 binding that decreased when using NWB-soleus extracts. Differences in binding between human and rat proximal-MCAT 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 proximal-MCAT elements, and 2) previously unrecognized ßMyHC proximal promoter elements contribute to NWB-regulation.
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