Ontogeny of the Murine Glucose-6-Phosphatase System |
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| Affiliation: | 1. Heritable Disorders Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, 20892;2. Veterinary and Tumor Pathology Section, Office of Laboratory Animal Science, National Cancer Institute, Frederick, Maryland, 21702;1. Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan;2. Japan Atomic Energy Agency, Rokkasho, Aomori 039-3212, Japan;3. Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan;3. Department of In Vitro Pharmacology, Merck Research Laboratories, West Point, Pennsylvania 19486;4. Department of Bone Biology, Merck Research Laboratories, West Point, Pennsylvania 19486;5. Department of Structural Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486;6. Department of Medicinal Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486;1. Division of Translational and Regenerative Medicine, Department of Medicine, The University of Arizona Cancer Center, Tucson, AZ;2. Division of Hematology and Oncology, Department of Medicine, The University of Arizona Cancer Center, Tucson, AZ;1. Institute for Agricultural and Fisheries Research (ILVO), Technology and Food Science Unit (T&V), Food Pilot, Brusselsesteenweg 370, 9090 Melle, Belgium;2. Flemish Institute for Technological Research (VITO), Business Unit for Separation and Conversion Technology (SCT), Boeretang 200, 2400 Mol, Belgium;3. Institute for Agricultural and Fisheries Research (ILVO), Technology and Food Sciences Unit, Product Quality and Innovation Research Area, Burgemeester Van Gansberghelaan 115/1, 9820 Merelbeke, Belgium;4. Hasselt University, Interuniversity Institute for Biostatistics and Statistical Bioinformatics, Agoralaan 1, 3590 Diepenbeek, Belgium;5. Flemish Institute for Technological Research (VITO), Business Unit Quality of the Environment (MRG), Boeretang 200, 2400 Mol, Belgium |
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| Abstract: | A deficiency in microsomal glucose-6-phosphatase (G6Pase) activity causes glycogen storage disease type 1 (GSD-1), a clinically and biochemically heterogeneous group of diseases. It has been suggested that catalysis by G6Pase involves multiple components, with defects in the G6Pase catalytic unit causing GSD-1a and defects in the putative substrate and product translocases causing GSD-1b, 1c, and 1d. However, this model is open to debate. To elucidate the G6Pase system, we have examinedG6PasemRNA expression, G6Pase activity, and glucose 6-phosphate (G6P) transport activity in the murine liver and kidney during normal development. In the liver,G6PasemRNA and enzymatic activity were detected at 18 days gestation and increased markedly at parturition, before leveling off to adult levels. In the kidney,G6PasemRNA and enzymatic activity appeared at 19 days gestation and peaked at weaning, suggesting that kidney G6Pase may have a different metabolic role.In situhybridization analysis demonstrated that, in addition to the liver and kidney, the intestine expressedG6Pase.Despite the expression ofG6Pasein the embryonic liver, microsomal G6P transport activity was not detectable until birth, peaking at about age 4 weeks. Our study strongly supports the multicomponent model for the G6Pase system. |
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