Warianty tytułu
Języki publikacji
Abstrakty
The highest amount of N-acetylneuraminic acid (AcNeu) was found in pyruvate kinase isoenzyme L from normal rat liver (24 moles/mole of enzyme tetramer), with the highest electrophoretic mobility. On the other hand, isoenzyme M2 from Morris hepatoma 7777, with the lowest electrophoretic mobility, had the lowest AcNeu content (5 moles/mole of enzyme tetramer). This tumour isoenzyme M2 of pyruvate kinase was, however, characterised by the highest phosphate content (12 moles/mole protein), in comparison to isoenzyme L (3 moles/mole protein) or normal liver isoenzyme M2 (6 moles/mole protein). This could indicate a regulatory change caused by reversible enzyme phosphorylation and dephosphorylation or sialization and desialization. Despite these differences, the sum of the two negatively charged residues was lower in tumour pyruvate kinase isoenzyme M2, with the slowest migration rate, than in normal rat liver isoenzyme M2. Moreover, isoenzyme M2 from tumour material, in comparison with isoenzyme M2 from normal rat liver, had a twice as high content of thiol groups (20 moles/mole protein), especially of free and superficially located ones, than the isoenzyme M2 from normal liver (10 moles/mole protein). This may explain abnormal susceptibility of tumour isoenzyme M2 to stereospecific inhibition by exogenous L-cysteine, and indicate genetically dependent changes in amino-acid content of tumour enzyme which take place during cell tumourigenic transformation.
Twórcy
Bibliografia
- 1. Weber, G. (1969) Regulation of pyruvate kinase. Adv. Enzyme Regul. 7, 15-40.
- 2. Ibsen, K.H. (1977) Interrelationships and functions of the pyruvate kinase isozymes and their variant forms. A review. Cancer Res. 37, 341-353.
- 3. Guminska, M. & Ignacak, J. (1996) Electro- phoretic pattern of cytosolic pyruvate kinase (PK) fractions A and B (Type L and M2) from normal rat liver and Morris hepatoma 7777. Biochim. Biophys. Acta 1292, 99-105.
- 4. Ignacak, J. & Guminska, M. (1993) Comparison of pyruvate kinase variants from rat liver and Morris hepatoma 7777, obtained by an affinity chromatography on Blue Sepharose CL-6B. Acta Biochim. Polon. 40, 261-267.
- 5. Guminska, M., Stachurska, M.B. & Ignacak, J. (1988) Pyruvate kinase (PK) isoenzymes in chromatin extracts of Ehrlich ascites tumour, Morris hepatoma 7777 and normal mouse and rat livers. Biochim. Biophys. Acta 966, 207-213.
- 6. Guminska, M., K?dryna, T. & Marchut, E. (1986) The effect of levamisole on energy metabolism in Ehrlich ascites tumour cells in vitro. Biochem. Pharmacol. 35, 4369-4374.
- 7. Kędryna, T„ Guminska, M. & Marchut, E. (1990) Pyruvate kinase from cytosolic fractions of the Ehrlich ascites tumour, normal mouse liver and skeletal muscle. Biochim. Biophys. Acta 1039, 130-133.
- 8. Marchut, E., Guminska, M., K^dryna, T., Radzikowski, Cz. & Kusmierczyk, H. (1988) A pyruvate kinase variant in different mouse transplanted tumours. Experientia 44.25-27.
- 9. Bucher, T. & Pfleiderer, G. (1955) Pyruvate kinase from muscle. Methods Enzymol. 1, 435—440.
- 10. Guminska, M., Ptak, W. & Zembala, M. (1975) Macrophage metabolism. Phagocytosis and digestion of normal and IgG antibody-coated sheep erythrocytes. Enzyme 19, 24-37.
- 11. Warren, L. (1959) The thiobarbituric acid assay of sialic acids. J. Biol. Chem. 234, 1971-1975.
- 12. Lowry, O.H. & Upez, J.A. (1946) The determination of inorganic phosphate in the presence of labile phosphate esters. J. Biol. Chem. 162, 421-428.
- 13. Kraush, F., Klinman, N.R. & Marks, R. (1964) An assay method for disulfide groups by fluorescence quenching. Anal. Biochem. 9, 100- 114.
- 14. Ellman, G.L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 264-273.
- 15. Robyt, J.F., Ackerman, R.J. & Chittenden, C.G. (1971) Reaction of protein disulfide groups with Ellman's reagent: A case study of the number of sulfhydryl and disulfide groups in Aspergillus oryzae a-amylase, papain and lysozyme. Arch. Biochem. Biophys. 147, 262-269.
- 16. Laidler, P.M., Taga, E.M. & Van Etten, R.L. (1982) Human liver acid phosphatase: Cysteine residues of the low-molecular-weight enzyme. Arch. Biochem. Biophys. 216, 512-521.
- 17. Waheed, A., I^idler, P.M., Wo, Y.P. & Van Etten, R.L. (1988) Purification and physico- chemical characterization of a human placental acid phosphatase possessing phosphotyro- syl protein phosphatase activity. Biochemistry 27, 4265-4273.
- 18. Lowry, O.H., Rosebrough, N.I., Farr, A.L. & Randall, R.I. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-273.
- 19. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227, 680-685.
- 20. Eigenbrodt, E., Abdel-Fattah Mostafa, M. & Schoner, W. (1977) Inactivation of pyruvate kinase type M from chicken liver by phosphorylation catalyzed by a cAMP-independent protein kinase. Hoppe-Seyler's Z. Physiol. Chem. 358, 1047-1067.
- 21. Presck, P., Glossmann, H., Eigenbrodt, E., Schoner, W., Riibsamen, H., Friis, R.R. & Bauer, H. (1980) Similarities between a phos-phoprotein pp60-associated protein kinase of Rous sarcoma virus and a cyclic adenosine 3':5'-monophosphate-independent protein kinase that phosphorylates pyruvate kinase type M2. Cancer Res. 40, 1733-1741.
- 22. Presek, P., Reinacher, M. & Eigenbrodt, E. (1988) Pyruvate kinase type M is phosphory- lated at tyrosine residues in cell transformed by Rous sarcoma virus. FEBS Lett. 242, 194-198.
- 23. Fister, P., Eigenbrodt, E., Presek, P., Reinacher, M. & Schoner, W. (1983) Pyruvate kinase type Ma is phosphorylated in the intact chicken liver cell. Biochem. Biophys. Res. Commun. 115, 409-414.
- 24. Giugni, T.D., Chen, K. & Cohen, S. (1988) Activation of a cytosolic serine protein kinase by epidermal growth factor. J. Biol. Chem. 263, 18988-18995.
- 25. Weernink, P.A.O., Rijksen, G., Van der Hei- jden, M.C.M. & Staal, G.E.J. (1990) Phosphorylation of pyruvate kinase type K in human gliomas by a cyclic adenosine 5'-monophos- phate-independent protein kinase. Cancer Res. 50, 4604-4610.
- 26. Moule, S.K. & McGivan, J.D. (1991) Epidermal growth factor stimulates the phosphorylation of pyruvate kinase in freshly isolated rat hepatocytes. FEBS Lett. 280, 37-40.
- 27. Titanji, V.P., Zetterqvist, O. & Engstrom, L. (1976) Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphory- lation reactions, catalysed by cyclic-AMP-dependent protein kinases and histone phosphatase. Biochim. Biophys. Acta 422, 98-108.
- 28. Ljungstrom, O., Hjelmquist, G. & Engstrom, L. (1974) Phosphorylation of purified rat liver pyruvate kinase by cyclic 3',5'-AMP-stimu- lated protein kinase. Biochim. Biophys. Acta 358, 289-298.
- 29. Kędryna, T., Guminska, M. & Marchut, E. (1983) The inhibitory effect of ^cysteine and its derivatives on glycolysis in Ehrlich ascites tumour cells. Biochim. Biophys. Acta 763, 64-71.
- 30. Anderson, M.W., Reynolds, S.H., You, M. & Marenpost, R.M. (1992) Role of protooncogene activation in carcinogenesis. Environ. Health Perspect. 98, 13-24.
- 31. Weber, G. (1968) Carbohydrate metabolism in cancer cells and the molecular correlation concept. Naturwissenschafien 55, 418-429.
- 32. Weber, G. (1977) Enzymology of cancer cells. New Engl. J. Med. 296, 486-493.
- 33. Gosalvez, M., Lopez-Alarcon, L., Garcia- Suarez, S., Montalvo, A. & Weinhouse, S. (1975) Stimulation of tumor-cell respiration by inhibitors of pyruvate kinase. Eur. J. Biochem. 55, 315-321.
- 34. Guminska, M., Stachurska, M.B., Christen- sen, B., Tromholt, V., Kieler, J., Radzikowski, Cz. & Dus, D. (1989) Pyruvate kinase inhibited by L-cysteine as a marker of tumorigenic human urothelial cell lines. Experientia 45, 571-574.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-d729b7f3-bf90-46b8-911a-c6774109ab14