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Articles in PresS, published online ahead of print March 28, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.01085.2001
Submitted on December 10, 2001
Accepted on March 19, 2002
-Myosin Heavy Chain Promoter Activity
1 Division of Endocrinology, Department of Medicine, North Shore-LIJ Research Institute, Manhasset, NY, USA
* To whom correspondence should be addressed. E-mail: kojamaa{at}nshs.edu.
Contractile activity of the cardiac myocyte is required for maintaining cell mass and phenotype, including expression of the cardiac-specific -myosin heavy chain
(MHC) gene. An E box element (HME) located at position -47 within the -MHC promoter is both necessary and sufficient to confer contractile responsiveness to the gene and has been shown to bind upstream stimulatory factor-1 (USF1). When studied in spontaneously contracting cardiac myocytes there is enhanced binding of USF1 to the HME compared to quiescent cells, which correlates with a 3-fold increase in -MHC promoter activity. A molecular mechanism by which contractile function modulates -MHC transcriptional activity may involve signaling via phosphorylation of USF1. The present studies showed that purified rat USF1 was phosphorylated in vitro by protein kinase C (PKC) and cAMP-dependent protein kinase (PKA), but not casein kinase II. Phosphorylated USF1 by either PKC or PKA had increased DNA binding activity to the HME. PKCmediated phosphorylation also lead to the formation of USF1 multimers as assessed by gel shift assay. Analysis of in vivo phosphorylated nuclear proteins from cultured ventricular myocytes showed that USF1 was phosphorylated, and resolution by two dimensional gel electrophoresis identified at least two distinct phosphorylated isoforms of USF1. These results suggest that endogenous kinases can covalently modify USF1, and provides a potential molecular mechanism by which the contractile stimulus mediates changes in myocyte gene transcription.
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