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Am J Physiol Endocrinol Metab (January 13, 2004). doi:10.1152/ajpendo.00455.2003
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Submitted on October 9, 2003
Accepted on January 6, 2004

Selective Stimulation of G6Pase Catalytic Subunit but not G6P Transporter Gene Expression by Glucagon In Vivo and cAMP In Situ

Lauri A. Hornbuckle1, Carrie A. Everett1, Cyrus C. Martin1, Stephanie S. Gustavson1, Christina A. Svitek1, James K. Oeser1, Doss W. Neal1, Alan D. Cherrington1, and Richard M. O'Brien1*

1 Department of Molecular Physiology and Biophysics, Vanderbilt University Medical School, Nashville, TN, USA

* To whom correspondence should be addressed. E-mail: richard.obrien{at}mcmail.vanderbilt.edu.

We recently compared the regulation of glucose-6-phosphatase (G6Pase) catalytic subunit and glucose-6-phosphate (G6P) transporter gene expression by insulin in conscious dogs in vivo (Hornbuckle et al. Am. J. Physiol. Endocrinol. Metab. 281:E713-725, 2001). In pancreatic-clamped, euglycemic conscious dogs, a 5 hr period of hypoinsulinemia led to a marked increase in hepatic G6Pase catalytic subunit mRNA; however, G6P transporter mRNA was unchanged. Here we demonstrate, again using pancreatic-clamped, conscious dogs, that glucagon is a candidate for the factor responsible for this selective induction. Thus, glucagon stimulated G6Pase catalytic subunit but not G6P transporter gene expression in vivo. Furthermore, cAMP stimulated endogenous G6Pase catalytic subunit gene expression in HepG2 cells but had no effect on G6P transporter gene expression. The cAMP response element (CRE) that mediates this induction was identified through transient transfection of HepG2 cells with G6Pase catalytic subunit-chloramphenicol acetyltransferase (CAT) fusion genes. Gel retardation assays demonstrate that this CRE binds several transcription factors including CREB and C/EBP.




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