Comparison of the kinetic properties of the pyruvate dehydrogenase complex from pig kidney cortex and medulla

• Autorzy: Pawelczyk T. , Olson M.S.
• Języki publikacji: EN

Abstrakty

The activity of the pyruvate dehydrogenase complex (PDC) purified from pig kidney medulla was affected by K+, Na+, CI", HCO3"", HP042" and changes in ionic strength. Increased ionic strength influenced the activity of PDC from medulla by decreasing the Vmax and S0.5 for pyruvate and increasing the Hill coefficient. The magnitude of these changes was smaller than the corresponding changes for PDC purified from the cortex. In the presence of K+ (80 mM), Na+ (20 mM), Cl~ (20 mM), HCO3" (20 mM), HPO42" (10 mM) and at ionic strength of 0.15 M the S0.5 for pyruvate of PDC from medulla was 117 nM and the enzyme complex was saturated by 1.1 mM pyruvate. Under these conditions the S0.5 for pyruvate of PDC derived from cortex was 159 nM and the enzyme was saturated at 4.5 mM pyruvate.

Słowa kluczowe

EN

pig; medulla; pyruvate dehydrogenase; kinetic property; kidney cortex; cortex

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1993
• Tom: 40
• Numer: 3
• Opis fizyczny: p.411-419,fig.

Twórcy

autor

Pawelczyk T.

• Medical Academy, Gdansk

autor

Olson M.S.

Bibliografia

• 1. Myers, C.E., Bulger, R.E., Tisher, C.C. & Trump, B.F. (1966) Human renal ultrastructure. IV. Collecting duct of healthy individuals. Lab. Inves. 15,1921.
• 2. Pfaller, W. & Rittinger, M. (1980) Quantitative morphology of the rat kidney. Int. J. Biochem. 12, 17-22.
• 3. Ross, B.D. & Guder, W.G. (1982) Heterogeneity and compartmentation in the kidney; in Heterogeneity and compartmentation in metabolism (Sies, H., ed.) pp. 363 - 409, London, Academic Press.
• 4. Lee, J.B., Vance, V.K. & Cahill, G.F. (1962) Metabolism of 14C labelled substrates by rabbit kidney cortex and medulla. Am. }. Physiol. 203, 27-36.
• 5. Weideman, M.J. & Krebs, H.A. (1969) The fuel of respiration of rat kidney cortex. Biochem. J. 112, 149 -166.
• 6. Klein, K.L., Wang, M.S., Torikai, S., Davidson, W.D. & Kurokawa, K. (1981) Substrate oxidation by defined nephron segments of rat kidney. Kidney Int. 20,29 -35.
• 7. Burch, H.B., Narius, R.G., Chu, C., Fagioli, S., Choi, S., McCarthy, W. & Lowry, O.H. (1978) Distribution along the rat nephron of three enzymes of gluconeogenesis in acidosis and starvation. Am. J. Physiol. 235, F246 - F253.
• 8. Kida, K., Nakajo, S., Kamiya, F., Toyama, Y., Nishio, T. & Nakagawa, H. (1978) Renal net glucose release in vivo and its contribution to blood glucose. J. Clin. Invest. 62, 721 - 726.
• 9. Besarab, A., Silva, P., Ross, B.D. & Epstein, F.H. (1975) Bicarbonate and sodium reabsorption. Am. ]. Physiol. 228,1525 -1530.
• 10. Silva, P., Ross, B.D., Charney, A.N., Besarab, A. & Epstein, F.H. (1975) Potassium transport by the isolated perfused kidney. ]. Clin. Invest. 56, 862 - 869.
• 11. Baines, A.D. & Ross, B.D. (1982) Nonoxidative glucose metabolism a prerequisite for formation of dilute urine. Am. ]. Physiol. 242, F491 - F498.
• 12. Frega, N.S., Weinberg, J.M., Ross, B.D. & Leaf, A. (1977) Stimulation of sodium transport by glucose in the perfused rat kidney. Am. J. Physiol. 233, F235 - F240.
• 13. Guder, W.G., Schmidt, U., Siess, E.A., Stukowski, B. & Wieland, O.H. (1973) Characterization of kidney carbohydrate metabolism by determination of phosphoenol- pyruvate carboxykinase and pyruvate dehydrogenase activities. Proceeding of 5th International Symposium on Clinical Enzymology 3,875 - 889.
• 14. Lee, J.B. & Peter, H.M. (1969) Effect of oxygen tension on glucose metabolism in rabbit kidney cortex and medulla. Am. }. Physiol. 217,1464 - 1471.
• 15. Eveloff, J., Haase, W. & Kinne, R. (1980) Separation of renal medullary cells: isolation of cells from the thick ascending limb of Henlefs loop. J. Cell Biol. 87,672 - 680.
• 16. Bernanke, D. & Epstein, F.H. (1965) Metabolism of the renal medulla. Am. J. Physiol. 208, 541- 545.
• 17. Ross, B.D., Epstein, F.H. & Leaf, A. (1973) Sodium reabsorption in the perfused rat kidney. Am. ]. Physiol. 225,1165 - 1171.
• 18. Ross, B.D., Espinal, J. & Silva, P. (1986) Glucose metabolism in renal tubular function. Kidney Int. 29,54 - 67.
• 19. Stoff, J.S., Epstein, F.H., Narins, R.G. & Relman, A.S. (1976) Recent advances in renal tubular biochemistry. Annu. Rev. Physiol. 38,46 - 48.
• 20. Beck, F., Dorge, A., Rick, R. & Thurau, (1984) Intra- and extracellular element concentrations of rat renal papilla in antidiuresis. Kidney Int. 25, 397-403.
• 21. Beck, F., Bauer, R., Bauer, V., Mason, J., Dorg, A., Rick, R. & Thurau, K. (1980) Electron microprobe analysis of intracellular elements in the rat kidney. Kidney Int. 17, 756 - 797.
• 22. Yancey, P.H. (1988) Osmotic effectors in kidneys of xeric and mesic rodents: corticomedullary distributions and changes with water availability. ]. Comp. Physiol. (B) 158,369 - 380.
• 23. Dell, R.B. & Winters, R.W. (1967) Lactate gradients in the kidney of the dog. Am. J. Physiol. 213,557 - 563.
• 24. Bagnasco, S., Balaban, R., Fales, H.M., Yang, Y.-M. & Burg, M. (1986) Predominant osmotica- lly active organic solutes in rat and rabbit renal medullas. ]. Biol. Chem. 261,5872 - 5877
• 25. Law, R.O. & Turner, D.P.J. (1987) Are ninhydrin-positive substances volume regulatory osmolytes in rat renal papilary cells. J.Physiol. 386,45-61.
• 26. Nakanishi, T., Uyama, O. & Sugita, M. (1991) Osmotically regulated taurine content in rat renal inner medulla. Am. ]. Physiol. 261, F957 - F962.
• 27. Wirthensohn, G., Beck, F.X. & Guder, W.G. (1987) Role and regulation of glycerophospho- rylcholine in rat renal papila. Pflugers Arch. 409, 411-415.
• 28. Wolff, S.D. & Balaban, R.S. (1990) Acute regulation of the predominant organic solutes of the rabbit renal inner medulla. Am. ]. Physiol. 257, F676 - F681.
• 29. Beck, F.X., Schmolke, M., Guder, W.G., Dorge, A. & Thurau, K. (1992) Osmolytes in renal medulla during rapid changes in papillary tonicity. Am. J. Physiol. 262, F849 - F856.
• 30. Garland, P.B. & Randl, P.J. (1964) Control of pyruvate dehydrogenase in perfused rat heart by the intracellular concentration of acetyl-coenzyme A. Biochem. J. 91,6c - 7c.
• 31. Wieland, O.H., Jagow-Westerman, B.U. & Stukowski, B. (1969) Kinetic and regulatory properties of heart muscle pyruvate dehydrogenase. Hoppe-Seyler's Z. Physiol. Chem. 350,329 - 334.
• 32. Linn, T.C., Pettit, F.H. & Reed, L.J. (1969) a-Keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc. Natl. Acad. Sci. U.S.A. 62,234 - 241.
• 33. Wieland, O.H. (1983) The mammalian pyruvate dehydrogenase complex: structure and regulation. Rev. Physiol. Biochem. Pharmacol. 96, 123 -170.
• 34. Yeaman, S.J. (1989) The 2-oxo acid dehydro­genase complexes: recent advances. Biochem. J. 257,625 - 632.
• 35. Wieland, O.H., Siess, E., Schulze-Wethmar, F.H., von Funcke, H.G. & Winton, B. (1971) Active and inactive forms of pyruvate dehydrogense in rat heart and kidney: Effect of diabetes, fasting, and refeeding on pyruvate dehydrogenase interconversion. Arch. Biochem. Biophys. 143,593 -601.
• 36. Guder, W.G., Stukowski, B., Siess, E.A. & Wieland, O.H. (1974) Metabolism of isolated kidney tubules. Regulation of pyruvate dehydrogenase by metabolic substrates. Eur. }. Biochem. 42,529-538.
• 37. Guder, W.G, Stukowski, B., Siess, E.A. & Wieland, O.H. (1975) Pyruvate dehydrogenase in rat kidney metabolism; in Biochemical aspects of kidney function (Angielski, S. & Dubach, U.C., eds.) pp. 70 - 75, Huber, Bern.
• 38. Pawelczyk, T., Eason, R.A. & Olson, M.S. (1988) The effect of various anions and cations on the regulation of pyruvate dehydrogenase complex from pig kidney cortex. Biochem. J. 253,819 - 825.
• 39. Pawelczyk, T., Eason, R.A. & Olson, M.S. (1992) Effect of ionic strength and pH on the activity of pyruvate dehydrogenase complex from pig kidney cortex. Arch. Biochem. Biophys. 294,44 -
• 40. Gornall, A.G., Bardawill, C.J. & David, M.M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751 - 766.
• 41. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680 - 685.
• 42. Perrin, D.D. & Dempsey, B. (1987) Buffers forpH and metal ion control. Chapman and Hall, London, New York.
• 43. Kresze, G.B. & Steber, L. (1979) Inactivation and disassembly of the pyruvate dehydrogenase multienzyme complex from bovine kidney by limited proteolysis with an enzyme from rat liver. Eur. J. Biochem. 95,569 - 578.
• 44. Kresze, G.B., Ronft, H. & Diett, B. (1980) Bovine kidney pyruvate dehydrogenase complex. Isolation of the component enzymes after limited proteolysis with papain. Eur. J. Biochem. 105,371-379.
• 45. Machicao, F. & Wieland, O.H. (1980) Subunit structure of lipoate acetyltransferase compo­nent of pyruvate dehydrogenase complex from bovine kidney. Hoppe-Seyler's Z. Physiol. Chem. 361,1093 -1106.
• 46. Pawelczyk, T. & Olson, M.S. (1993) The regulatory properties of kidney pyruvate dehy­drogenase complex components. Arch. Biochem. Biophys. 300,489 - 494.
• 47. Pawelczyk, T. & Olson, M.S. (1992) Regulation of the pyruvate dehydrogenase kinase activity from pig kidney cortex. Biochem.}. 288,369 - 373.
• 48. Frey, P.A., Flournoy, D.S., Gruys, K. & Yang, Y.-S. (1989) Intermediates in reductive transacetyla- tion catalyzed by pyruvate dehydrogenase complex. Ann. N.Y. Acad. Sci. 573,21 - 35.
• 49. Cate, R.L., Roche, T.E. & Davis, L. (1980) Rapid intersite transfer of acetyl groups and moveme­nt of pyruvate dehydrogenase component in the kidney pyruvate dehydrogenase complex. /. Biol. Chem. 255,7556 - 7562.