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Originally published In Press as doi:10.1074/jbc.M003678200 on May 15, 2000

J. Biol. Chem., Vol. 275, Issue 30, 23005-23011, July 28, 2000
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Identification of Weight-bearing-responsive Elements in the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+ ATPase (SERCA1) Gene*

Heather Mitchell-Felton, R. Bridge Hunter, Eric J. Stevenson, and Susan C. KandarianDagger

From the Department of Health Sciences, Boston University, Boston, Massachusetts 02215

The skeletal muscle sarco(endo)plasmic reticulum calcium ATPase (SERCA1) gene is transactivated as early as 2 days after the removal of weight-bearing (Peters, D. G., Mitchell-Felton, H., and Kandarian, S. C. (1999) Am. J. Physiol. 276, C1218-C1225), but the transcriptional mechanisms are elusive. Here, the rat SERCA1 5' flank and promoter region (-3636 to +172 base pairs) was comprehensively examined using in vivo somatic gene transfer into rat soleus muscles (n = 804) to identify region(s) that are both necessary and sufficient for sensitivity to weight-bearing. In all, 40 different SERCA1 reporter plasmids were constructed and tested. Several different regions of the SERCA1 5' flank were sufficient to confer a transcriptional response to 7 days of muscle unloading when placed upstream of a heterologous promoter. Two of these regions were analyzed further because they were necessary for the unloading response of -3636 to +172, as demonstrated using internal deletion constructs. Deletion analysis of these regions (-1373 to -1158 and -330 to +172) suggested that unloading responsiveness corresponded to CACC sites and E-boxes. Mutagenesis of cis-elements in the first region showed that a specific CACC box (-1262) was involved in SERCA1 transactivation and a nearby E-box (-1248) was also implicated. Constructs containing trimerized CACC sites and E-boxes showed that the presence of both elements is required to activate transcription. This is the first identification of specific cis-elements required for the regulation of a Ca2+ handling gene by changes in muscle loading condition.

* This work was supported by National Institutes of Health Grant AR41705.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger An Established Investigator of the American Heart Association. To whom correspondence should be addressed: Boston University, Dept. of Health Sciences, 635 Commonwealth Ave., 4th Floor, Boston, MA 02215. Tel.: 617-353-5169; Fax: 617-353-7567; E-mail: skandar@bu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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