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J. Biol. Chem., Vol. 279, Issue 25, 26215-26219, June 18, 2004
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From the Section on Cellular Differentiation, Heritable Disorders Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892
The breakdown of tissue glycogen into glucose is critical for blood glucose homeostasis between meals. In the final steps of glycogenolysis, intracellular glucose 6-phosphate (Glc-6-P) is transported into the endoplasmic reticulum where it is hydrolyzed to glucose by glucose-6-phosphatase (Glc-6-Pase). Although the majority of body glycogen is stored in the muscle, the current dogma holds that Glc-6-Pase (now named Glc-6-Pase-
) is expressed only in the liver, kidney, and intestine, implying that muscle glycogen cannot contribute to interprandial blood glucose homeostasis. Recently we reported a second Glc-6-P hydrolase, Glc-6-Pase-
. Glc-6-Pase-
shares kinetic and structural similarities to Glc-6-Pase-
and couples with the Glc-6-P transporter to form an active Glc-6-Pase complex (Shieh, J.-J., Pan, C.-J., Mansfield, B. C., and Chou, J. Y. (2003) J. Biol. Chem. 278, 4709847103). Here we demonstrate that muscle expresses both Glc-6-Pase-
and Glc-6-P transporter and that they can couple to form an active Glc-6-Pase complex. Our data suggest that muscle may have a previously unrecognized role in interprandial glucose homeostasis.
Received for publication, February 24, 2004 , and in revised form, April 7, 2004.
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Both authors contributed equally to this work.
To whom correspondence should be addressed: Bldg. 10, Rm. 9S241, NIH, 9000 Rockville Pike, Bethesda, MD 20892-1830. Tel.: 301-496-1094; Fax: 301-402-6035; E-mail: chouja{at}mail.nih.gov.
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