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Papers In Press, published online ahead of print April 14, 2004
J. Biol. Chem, 10.1074/jbc.M402036200
Submitted on February 24, 2004
Revised on April 7, 2004
Accepted on April 14, 2004

A potential new role for muscle in blood glucose homeostasis

Jeng-Jer Shieh, Chi-Jiunn Pan, Brian C. Mansfield, and Janice Y. Chou

Heritable Disorders Branch, NICHD, NIH, Bethesda, MD 20892-1830

Corresponding Author: Chouja{at}mail.nih.gov

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 (G6P) is transported into the endoplasmic reticulum where it is hydrolyzed to glucose by glucose-6-phosphatase (G6Pase). While the majority of body glycogen is stored in the muscle, the current dogma holds that G6Pase (now named G6Pase-alpha) 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 G6P hydrolase, G6Pase-beta. G6Pase-beta shares kinetic and structural similarities to G6Pase-alpha, and couples with the G6P transporter (G6PT) to form an active G6Pase complex. Here we demonstrate that muscle expresses both G6Pase-beta and G6PT and that they can couple to form an active G6Pase complex. Our data suggest that muscle may have a previously unrecognized role in interprandial glucose homeostasis.


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