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J Biol Chem, Vol. 274, Issue 20, 14270-14279, May 14, 1999

Segregated Regulatory Elements Direct -Myosin Heavy Chain Expression in Response to Altered Muscle Activity

John J. McCarthy, Dharmesh R. Vyas, Gretchen L. Tsika, and Richard W. Tsika^§¶

From the  Department of Veterinary Biomedical Sciences, School of Veterinary Medicine, the ^§ Department of Biochemistry, School of Medicine, and ^¶ Dalton Cardiovascular Research Center, University of Missouri, Columbia, Missouri 65211

Our previous transgenic analyses revealed that a 600-base pair -myosin heavy chain (MyHC) promoter conferred mechanical overload (MOV) and non-weight-bearing (NWB) responsiveness to a chloramphenicol acetyltransferase reporter gene. Whether the same DNA regulatory element(s) direct MyHC expression following MOV or NWB activity in vivo remains unknown. We now show that a 293-base pair MyHC promoter fused to chloramphenicol acetyltransferase (293) responds to MOV, but not NWB activity, indicating a segregation of these two diverse elements. Inclusion of the MyHC negative regulatory element (332 to 300; NRE) within transgene 350 repressed expression in all transgenic lines. Electrophoretic mobility shift assays showed highly enriched binding activity only in NWB soleus nuclear extracts that was specific to the distal region of the NRE sense strand (dNRE-S; 332 to 311). Supershift electrophoretic mobility shift assay revealed that the binding at the distal region of the NRE sense strand was antigenically distinct from cellular nucleic acid-binding protein and Y-box-binding factor 1, two proteins shown to bind this element. Two-dimensional UV cross-linking and shift Southwestern blotting analyses detected two proteins (50 and 52 kDa) that bind to this element. These in vivo results demonstrate that segregated MyHC promoter elements transcriptionally regulate MyHC transgene expression in response to two diverse modes of neuromuscular activity.

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