On the involvement of a glucose 6-phosphate transport system in the function of microsomal glucose 6-phosphatase
- 167 Downloads
- 128 Citations
Summary
A model for microsomal glucose 6-phosphatase (EC 3.1.3.9) is presented. Glucose 6-phosphatase is postulated to be resultant of the coupling of two components of the microsomal membrane: 1) a glucose 6-phosphate — specific transport system which functions to shuttle the sugar phosphate from the cytoplasm to the lumen of the endoplasmic reticulum; and 2) a catalytic component, glucose-6-P phosphohydrolase, bound to the luminal surface of the membrane. A large body of existing data was shown to be consistent with this hypothesis. In particular, the model reconciles well-documented differences in the kinetic properties of the enzyme of untreated and modified microsomal preparations. Characteristic responses of the enzyme to changes in nutritional and hormonal states may be attributed to adaptations which alter the relative capacities of the transport and catalytic components.
Keywords
Luminal Transport System Characteristic Response Kinetic Property Hormonal StatePreview
Unable to display preview. Download preview PDF.
References
- 1.R. C. Nordlie, in The enzymes (P. D. Boyer, ed.) Vol. 4. pp. 543–610, Academic Press, Inc. New York (1971).Google Scholar
- 2.B. E. Ryman and W. J. Whelan, Adv. Enzymol. 34, 298–311 (1971).Google Scholar
- 3.J. Ashmore and G. Weber, Vitamins and Hormones 17, 91–132 (1959).Google Scholar
- 4.R. C. Nordlie, Ann. N.Y. Acad. Sci. 166, 699–718 (1969).Google Scholar
- 5.W. J. Arion, P. W. Carlson, B. K. Wallin and A. J. Lange, J. Biol. Chem. 247, 2551–2557 (1972).Google Scholar
- 6.W. J. Arion, B. K. Wallin, P. W. Carlson and A. J. Lange, J. Biol. Chem. 247, 2558–2565 (1972).Google Scholar
- 7.E. Palade and P. Siekevitz, J. Biophys. Biochem. Cytol, 2, 171–198 (1956).Google Scholar
- 8.R. Nilsson, E. Peterson and G. Dallner, J. Cell. Biol. 56, 762–776 (1973).Google Scholar
- 9.G. Kreibich and D. D. Sabatini, Fed. Proceeding 32, 2133–2138 (1973).Google Scholar
- 10.J. S. Little and C. C. Widnell, Fed. Proceedings 31, 880Abs (1972).Google Scholar
- 11.R. C. Nordlie and W. J. Arion, Methods Enzymol. 9, 619–625 (1966).Google Scholar
- 12.W. J. Arion and B. K. Wallin, J. Biol. Chem. 248, 2372–2379 (1973).Google Scholar
- 13.B. K. Wallin and W. J. Arion, Biochem. Biophys. Res. Commun. 48, 694–699 (1972).Google Scholar
- 14.R. C. Nordlie and W. J. Arion, J. Biol. Chem. 240, 2155–2164 (1965).Google Scholar
- 15.M. R. Stetten and F. F. Burnett, Biochem. Biophys. Acta. 139, 138–147 (1967).Google Scholar
- 16.R. C. Nordlie, W. J. Arion, T. L. Hanson, J. R. Gilsdorf and R. N. Horne, J. Biol. Chem. 243, 1140–1146 (1968).Google Scholar
- 17.B. K. Wallin, Ph.D. Thesis, Cornell University, pp. 116–126 (1973).Google Scholar
- 18.S. Orrenius, J. L. E. Ericsson and L. Ernster, J. Cell Biol. 25, 627–639 (1965).Google Scholar
- 19.P. N. Pandhi and H. Baum, Life Sciences 9, 87–92 (1970).Google Scholar
- 20.R. C. Nordlie, W. J. Arion and E. A. Glende, Jr., J. Biol. Chem. 240, 3479–3484 (1965).Google Scholar
- 21.S. V. Jakobsson and G. Dallner, Biochem. Biophys. Acta, 165, 380–392 (1968).Google Scholar
- 22.R. C. Nordlie and R. E. Snoke, Biochem. Biophys, Acta 148, 222–232 (1967).Google Scholar
- 23.T. L. Hanson and R. C. Nordlie, Biochem. Biophys. Acta 198, 66–75 (1970).Google Scholar
- 24.H. L. Segal and M. E. Washko, J. Biol. Chem. 234, 1937–1941 (1959).Google Scholar
- 25.B. K. Wallin and W. J. Arion, J. Biol. Chem. 248, 2380–2386 (1973).Google Scholar
- 26.F. Feldman and L. G. Butler, Biochem. Biophys. Res. Commun. 36, 119–125 (1969).Google Scholar
- 27.J. H. Johnson and H. Tedeschi, Arch. Biochem. Biophys. 124, 58–69 (1968).Google Scholar
- 28.D. L. Oxender, Ann. Rev. Biochem. 41, 777–814 (1972).Google Scholar
- 29.R. J. Levin, The Living Barrier, William Heinemann Medical Books Ltd. London, pp. 74–75 (1969).Google Scholar
- 30.A. Kotyk and K. Janacek, Cell Membrane Transport, Plenum Press, New York (1970).Google Scholar
- 31.D. M. Regen and H. L. Tarpley, Biochem. Biophys. Acta. 339, 218–233 (1974).Google Scholar
- 32.A. Leskes, P. Siekevitz and G. E. Palade, J. Cell Biol. 49, 264–287 (1971)Google Scholar
- 33.A. Leskes, P. Siekevitz and G. E. Palade, J. Cell Biol. 49, 288–302 (1971).Google Scholar
- 34.A. A. El-Aaser, J. T. R. Fitzsimons, R. H. Hinton, K. A. Norris and E. Reid, Histochemical J. 5, 199–223 (1973).Google Scholar
- 35.J. A. Lewis and J. R. Tata, Biochem. J. 134, 69–78 (1973).Google Scholar
- 36.A. L. Vianna and R. C. Nordlie, J. Biol. Chem. 244, 4027–4032 (1969).Google Scholar
- 37.P. Mitchell, Advances in Enzymology, 29, 33–88 (1967).Google Scholar
- 38.P. Mitchell, Nature, 180, 134–136 (1957).Google Scholar
- 39.P. Siekevitz, Ciba Foundation Symposium on Regulation of Cell Metabolism (G. E. W. Wolstenholme and C. M. O'Connor, eds.) Little Brown and Co., Boston, pp. 36–37 (1959).Google Scholar