Phosphoenolpyruvate Carboxykinase Is Necessary for the Integration of Hepatic Energy Metabolism

REFERENCES

• Araki, K., Araki, M., Miyazaki, J., and Vassalli, P.. 1995. Site-specific recombination of a transgene in fertilized eggs by transient expression of Cre recombinase. Proc. Natl. Acad. Sci. USA 92:160–164
   PubMed Web of Science ®Google Scholar
• Ballard, F. J., and Hanson, R. W.. 1967. Phosphoenolpyruvate carboxykinase and pyruvate carboxylase in developing rat liver. Biochem. J. 104:866–871
   PubMed Web of Science ®Google Scholar
• Bergmeyer, H. U.. and 1985. Methods of enzymatic analysis, 3rd ed. 4 to 6: VCH Verlagsgesllschaft, Weinheim, Germany
   Google Scholar
• Cersosimo, E., Molina, P. E., and Abumrad, N. N.. 1997. 1984. Renal glucose production during insulin-induced hypoglycemia. Diabetes 46:643–646 (Erratum, 46:1532.)
   PubMedGoogle Scholar
• Cimbala, M. A., Lamers, W. H., Nelson, K., Monahan, J. E., Yoo-Warren, H., and Hanson, R. W.. 1982. Rapid changes in the concentration of phosphoenolpyruvate carboxykinase mRNA in rat liver and kidney. Effects of insulin and cyclic AMP. J. Biol. Chem. 257:7629–7636
   PubMed Web of Science ®Google Scholar
• Consoli, A., Nurjhan, N., Capani, F., and Gerich, J.. 1989. Predominant role of gluconeogenesis in increased hepatic glucose production in NIDDM. Diabetes 38:550–557
   PubMed Web of Science ®Google Scholar
• DeFronzo, R. A., and Ferrannini, E.. 1991. Insulin resistance. A multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease. Diabetes Care 14:173–194
   PubMed Web of Science ®Google Scholar
• DiTullio, N. W., Berkoff, C. E., Blank, B., Kostos, V., Stack, E. J., and Saunders, H. L.. 1974. 3-Mercaptopicolinic acid, an inhibitor of gluconeogenesis. Biochem. J. 138:387–394
   PubMed Web of Science ®Google Scholar
• Ekberg, K., Landau, B. R., Wajngot, A., Chandramouli, V., Efendic, S., Brunengraber, H., and Wahren, J.. 1999. Contributions by kidney and liver to glucose production in the postabsorptive state and after 60 h of fasting. Diabetes 48:292–298
   PubMed Web of Science ®Google Scholar
• Exton, J. H., and Park, C. R.. 1969. Control of gluconeogenesis in liver. 3. Effects of l-lactate, pyruvate, fructose, glucagon, epinephrine, and adenosine 3′,5′-monophosphate on gluconeogenic intermediates in the perfused rat liver. J. Biol. Chem. 244:1424–1433
   PubMedGoogle Scholar
• Girard, J., Ferre, P., Pegorier, J. P., and Duee, P. H.. 1992. Adaptations of glucose and fatty acid metabolism during perinatal period and suckling-weaning transition. Physiol. Rev. 72:507–562
   PubMed Web of Science ®Google Scholar
• Granner, D., Andreone, T., Sasaki, K., and Beale, E.. 1983. Inhibition of transcription of the phosphoenolpyruvate carboxykinase gene by insulin. Nature 305:549–551
   PubMed Web of Science ®Google Scholar
• Groen, A. K., van Roermund, C. W., Vervoorn, R. C., and Tager, J. M.. 1986. Control of gluconeogenesis in rat liver cells. Flux control coefficients of the enzymes in the gluconeogenic pathway in the absence and presence of glucagon. Biochem. J. 237:379–389
   PubMedGoogle Scholar
• Halestrap, A. P.. 1989. The regulation of the matrix volume of mammalian mitochondria in vivo and in vitro and its role in the control of mitochondrial metabolism. Biochim. Biophys. Acta 973:355–382
   PubMed Web of Science ®Google Scholar
• Hashimoto, T., Fujita, T., Usuda, N., Cook, W., Qi, C., Peters, J. M., Gonzalez, F. J., Yeldandi, A. V., Rao, M. S., and Reddy, J. K.. 1999. Peroxisomal and mitochondrial fatty acid beta-oxidation in mice nullizygous for both peroxisome proliferator-activated receptor alpha and peroxisomal fatty acyl-CoA oxidase. Genotype correlation with fatty liver phenotype. J. Biol. Chem. 274:19228–19236
   PubMed Web of Science ®Google Scholar
• Jetton, T. L., and Magnuson, M. A.. 1992. Heterogeneous expression of glucokinase among pancreatic beta cells. Proc. Natl. Acad. Sci. USA 89:2619–2623
   PubMedGoogle Scholar
• John-Alder, H. B., McAllister, R. M., and Terjung, R. L.. 1986. Reduced running endurance in gluconeogenesis-inhibited rats. Am. J. Physiol. 251:R137–R142
   PubMedGoogle Scholar
• Katz, J., and Tayek, J. A.. 1998. Gluconeogenesis and the Cori cycle in 12-, 20-, and 40-h-fasted humans. Am. J. Physiol. 275:E537–E542
   PubMedGoogle Scholar
• Kraus-Freidmann, N., and Feng, L.. 1996. The role of intracellular Ca2+ in the regulation of gluconeogenesis. Metabolism 45:389–403
   PubMedGoogle Scholar
• Krebs, H. A.. 1954. Considerations concerning the pathways of synthesis in living matter. Synthesis of glycogen from non-carbohydrate precursors. Bull. Johns Hopkins Hosp. 95:19
   PubMedGoogle Scholar
• Kurtz, D. M., Rinaldo, P., Rhead, W. J., Tian, L., Millington, D. S., Vockley, J., Hamm, D. A., Brix, A. E., Lindsey, J. R., Pinkert, C. A., O'Brien, W. E., and Wood, P. A.. 1998. Targeted disruption of mouse long-chain acyl-CoA dehydrogenase gene reveals crucial roles for fatty acid oxidation. Proc. Natl. Acad. Sci. USA 95:15592–15597
   PubMed Web of Science ®Google Scholar
• Labosky, P. A., Winnier, G. E., Jetton, T. L., Hargett, L., Ryan, A. K., Rosenfeld, M. G., Parlow, A. F., and Hogan, B. L.. 1997. The winged helix gene, Mf3, is required for normal development of the diencephalon and midbrain, postnatal growth and the milk-ejection reflex. Development 124:1263–1274
   PubMedGoogle Scholar
• Landau, B. R., Wahren, J., Chandramouli, V., Schumann, W. C., Ekberg, K., and Kalhan, S. C.. 1996. Contributions of gluconeogenesis to glucose production in the fasted state. J. Clin. Investig. 98:378–385
   PubMed Web of Science ®Google Scholar
• Lei, K. J., Chen, H., Pan, C. J., Ward, J. M., Mosinger, B.Jr., Lee, E. J., Westphal, H., Mansfield, B. C., and Chou, J. Y.. 1996. Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type-1a mouse. Nat. Genet. 13:203–209
   PubMed Web of Science ®Google Scholar
• Magnuson, M. A., Quinn, P. G., and Granner, D. K.. 1987. Multihormonal regulation of phosphoenolpyruvate carboxykinase-chloramphenicol acetyltransferase fusion genes. Insulin's effects oppose those of cAMP and dexamethasone. J. Biol. Chem. 262:14917–14920
   PubMedGoogle Scholar
• McGarry, J. D., Leatherman, G. F., and Foster, D. W.. 1978. Carnitine palmitoyltransferase I. The site of inhibition of hepatic fatty acid oxidation by malonyl-CoA. J. Biol. Chem. 253:4128–4136
   PubMed Web of Science ®Google Scholar
• Meyers, E. N., Lewandoski, M., and Martin, G. R.. 1998. An Fgf8 mutant allelic series generated by Cre- and Flp-mediated recombination. Nat. Genet. 18:136–141
   PubMed Web of Science ®Google Scholar
• Niswender, K. D., Postic, C., Jetton, T. L., Bennett, B. D., Piston, D. W., Efrat, S., and Magnuson, M. A.. 1997. Cell-specific expression and regulation of a glucokinase gene locus transgene. J. Biol. Chem. 272:22564–22569
   PubMed Web of Science ®Google Scholar
• Niswender, K. D., Shiota, M., Postic, C., Cherrington, A. D., and Magnuson, M. A.. 1997. Effects of increased glucokinase gene copy number on glucose homeostasis and hepatic glucose metabolism. J. Biol. Chem. 272:22570–22575
   PubMed Web of Science ®Google Scholar
• Nordlie, R. C., and Lardy, H. A.. 1963. Mammalian liver P-enolpyruvate carboxykinase. J. Biol. Chem. 238:2259–2263
   PubMed Web of Science ®Google Scholar
• Nurjhan, N., Consoli, A., and Gerich, J.. 1992. Increased lipolysis and its consequences on gluconeogenesis in non-insulin-dependent diabetes mellitus. J. Clin. Investig. 89:169–175
   PubMed Web of Science ®Google Scholar
• Owen, M. R., and Halestrap, A. P.. 1993. The mechanisms by which mild respiratory chain inhibitors inhibit hepatic gluconeogenesis. Biochim. Biophys. Acta 1142:11–22
   PubMedGoogle Scholar
• Owen, O. E., Felig, P., Morgan, A. P., Wahren, J., Cahill, G. F.Jr.. 1969. Liver and kidney metabolism during prolonged starvation. J. Clin. Investig. 48:574–583
   PubMed Web of Science ®Google Scholar
• Pilkis, S. J., and Granner, D. K.. 1992. Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Annu. Rev. Physiol. 54:885–909
   PubMed Web of Science ®Google Scholar
• Postic, C., Shiota, M., Niswender, K. D., Jetton, T. L., Chen, Y., Moates, J. M., Shelton, K. D., Lindner, J., Cherrington, A. D., and Magnuson, M. A.. 1999. Dual roles for glucokinase in glucose homeostasis as determined by liver and pancreatic beta cell-specific gene knock-outs using Cre recombinase. J. Biol. Chem. 274:305–315
   PubMed Web of Science ®Google Scholar
• Randle, P. J., Garland, P. B., Halers, C. N., and Newsholme, E. A.. 1963. The glucose-fatty acid cycle: its role in insulin sensitivity and the metabolic disturbance of diabetes mellitus. Lancet I:785–789
   Google Scholar
• Rosella, G., Zajac, J. D., Kaczmarczyk, S. J., Andrikopoulos, S., and Proietto, J.. 1993. Impaired suppression of gluconeogenesis induced by overexpression of a noninsulin-responsive phosphoenolpyruvate carboxykinase gene. Mol. Endocrinol. 7:1456–1462
   PubMedGoogle Scholar
• Saha, A. K., Laybutt, D. R., Dean, D., Vavvas, D., Sebokova, E., Ellis, B., Klimes, I., Kraegen, E. W., Shafrir, E., and Ruderman, N. B.. 1999. Cytosolic citrate and malonyl-CoA regulation in rat muscle in vivo. Am. J. Physiol. 276:E1030–E1037
   PubMed Web of Science ®Google Scholar
• Sauer, B.. 1993. Manipulation of transgenes by site-specific recombination: use of Cre recombination. Methods Enzymol. 225:890–901
   PubMedGoogle Scholar
• She, P., Hippen, A. R., Young, J. W., Lindberg, G. L., Beitz, D. C., Richardson, L. F., and Tucker, R. W.. 1999. Metabolic responses of lactating dairy cows to 14-day intravenous infusions of glucagon. J. Dairy Sci. 82:1118–1127
   PubMedGoogle Scholar
• Short, M. K., Clouthier, D. E., Schaefer, I. M., Hammer, R. E., Magnuson, M. A., and Beale, E. G.. 1992. Tissue-specific, developmental, hormonal, and dietary regulation of rat phosphoenolpyruvate carboxykinase-human growth hormone fusion genes in transgenic mice. Mol. Cell. Biol. 12:1007–1020
   PubMedGoogle Scholar
• Stumvoll, M., Chintalapudi, U., Perriello, G., Welle, S., Gutierrez, O., and Gerich, J.. 1995. Uptake and release of glucose by the human kidney. Postabsorptive rates and responses to epinephrine. J. Clin. Investig. 96:2528–2533
   PubMed Web of Science ®Google Scholar
• Turcotte, L. P., Rovner, A. S., Roark, R. R., and Brooks, G. A.. 1990. Glucose kinetics in gluconeogenesis-inhibited rats during rest and exercise. Am. J. Physiol. 258:E203–E211
   PubMedGoogle Scholar
• Valera, A., Pujol, A., Pelegrin, M., and Bosch, F.. 1994. Transgenic mice overexpressing phosphoenolpyruvate carboxykinase develop non-insulin-dependent diabetes mellitus. Proc. Natl. Acad. Sci. USA 91:9151–9154
   PubMed Web of Science ®Google Scholar
• Wiese, T. J., Lambeth, D. O., and Ray, P. D.. 1991. The intracellular distribution and activities of phosphoenolpyruvate carboxykinase isozymes in various tissues of several mammals and birds. Comp. Biochem. Physiol. B 100:297–302
   PubMedGoogle Scholar
• Williams, C. P., Postic, C., Robin, D., Robin, P., Parrinello, J., Shelton, K., Printz, R. L., Magnuson, M. A., Granner, D. K., Forest, C., and Chalkley, R.. 1999. Isolation and characterization of the mouse cytosolic phosphoenolpyruvate carboxykinase (GTP) gene: evidence for tissue-specific hypersensitive sites. Mol. Cell. Endocrinol. 148:67–77
   PubMedGoogle Scholar
• Wynshaw-Boris, A., Short, J. M., Loose, D. S., and Hanson, R. W.. 1986. Characterization of the phosphoenolpyruvate carboxykinase (GTP) promoter-regulatory region. I. Multiple hormone regulatory elements and the effects of enhancers. J. Biol. Chem. 261:9714–9720
   PubMedGoogle Scholar
• Zimmer, D. B., and Magnuson, M. A.. 1990. Immunohistochemical localization of phosphoenolpyruvate carboxykinase in adult and developing mouse tissues. J. Histochem. Cytochem. 38:171–178
   PubMedGoogle Scholar