Summary
Rabbit hexokinase (EC 2.7.1.1) has been shown to exist in reticulocytes as two distinct molecular forms, designated hexokinase Ia and Ib, but only one of these was consistently present in mature red cells. In vivo, hexokinase la and Ib show a decay rate of 3 and 8% a day, respectively, while in vitro they show a similar stability.
The possibility that the proteolytic activities of the reticulocyte could be responsible for the fast decay of hexokinase was investigated. No differences were found in the decay rates of hexokinase la and Ib during in vitro reticulocyte maturation in presence or absence of proteolytic inhibitors. Contrariwise, many findings indicate the ATP-dependent proteolytic system of the reticulocyte as a possible mechanism. In fact, the decay of hexokinase and the degradation of 3H-globins are both stimulated by ATP and ubiquitin; they show similar kinetic properties and both disappear during reticulocyte maturation.
The cellular localization of hexokinase la and Ib was shown to be responsible for the differences found between their decay rates.
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Abbreviations
- PMSF:
-
phenylmethylsulfonyl fluoride
- TPCK:
-
1-1-tosylamide-2-phenylethyl-chloromethyl ketone
- TLCK:
-
N α-p-tosyl-L-lysine chloromethyl ketone
References
Brewer, G. J., 1974. The Red Blood Cell, Vol. 1, pp. 387–433, Academic Press, New York.
Rapoport, T. A., Heinrich, R., Jacobasch, G. and Rapoport, S., 1974. Eur. J. Biochem. 42: 107–120.
Minakami, S. and Yoshikawa, H., 1966. J. Biochem. 59: 139–144.
Rogers, P. A., Fischer, R. A-. and Harris, H., 1975. Clin. Chim. Acta. 65: 291–298.
Turner, B. M., Fischer, R. A. and Harris, H., 1975. Isozymes, Vol. 1, pp. 781–795, Academic Press, New York.
Chapman, R. G., and Shaumberg, L., 1967. Br. J. Haematol. 13: 665–678.
Fornaini, G., Magnani, M., Dacha, M., Bossu, M., and Stocchi, V., 1978. Mech. Ageing Dev. 8: 249–256.
Magnani, M., Stocchi, V., Bossu, M., Dacha, M., and Fornaini, G., 1979. Mech. Ageing Dev. 11: 209–217.
Stocchi, V., Magnani, M., Canestrari, F., Dachà, M., and Fornaini, G., 1981. J. Biol. Chem. 256: 7856–7862.
Magnani, M., Stocchi, V., Dachà, M., Canestrari, F., and Fornaini, G., 1980. FEBS Lett. 120: 264–266.
Magnani, M., Dachà, M., Stocchi, V., Ninfali, P., and Fornaini, G., 1980. J. Biol. Chem. 255: 1752–1756.
Stocchi, V., Magnani, M., Canestrari, F., Dachà, M., and Fornaini, G., 1982. J. Biol. Chem. 257: 2357–2364.
Magnani, M., Stocchi, V., Canestrari, F., Dachà, M., and Fornaini, G., 1982. Biochem. Int. 4: 673–677.
Fornaini, G., Dachà, M., Magnani, M., and Stocchi, V., 1982. Mol. Cell. Bioehem. 49: 129–142.
Etlinger, J. D. and Goldber, L. A., 1977. Proc. Natl. Acad. Sci. U.S.A. 74: 54–58.
Beutler, E., 1975. Red Cell Metabolism, 2nd ed., Gruner & Stratton, New York.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., 1951. J. Biol. Chem. 193: 265–275.
Magnani, M., Stocchi, V., Ninfali, P., Dachà, M., Bossu, M. and Fornaini, G., 1979. Bull. Mol. Biol. Med. 4: 90–99.
Dacie, J. V. and Lewis, S. M., 1975. Practical Haematology, 5th ed., p. 79, Churchill & Livingstone, London.
Magnani, M., Serafini, G., Stocchi, V., Bossu, M. and Dachà, M., 1982. Arch. Biochem. Biophys. 150: 96–104.
Wilson, J. E., 1972. Arch. Biochem. Biophys. 150: 96–104.
Schapira, G., Rosa, J., Maleknia, N. and Padieu, 1968. In: Methods in Enzymology (Grossman, L. and Moldave, K., eds.), Vol. XIIB, pp. 747–769, Academic Press, New York.
Ciechanover, A., Hod, Y. and Hershko, A., 1978. Biochem. Biophys. Res. Commun. 81: 1100–1105.
Ciechanover, A., Elias, S., Heller, H., Ferber, S. and Hershko, A., 1980. J. Biol. Chem. 255: 7525–7528.
Magnani, M., Piatti, E., Serafini, N., Palma, F., Dachà, M. and Fornaini, G., 1983. Mech. Ageing Dev. 22: 295–308.
Hershko, A., Ciechanover, A. and Rose, I., 1979. Proc. Natl. Acad. Sci. U.S.A. 76: 3107–3110.
Hershko, A., Ciechanover, A., Heller, H., Hass, A. L. and Rose, L., 1980. Proc. Natl. Acad. Sci. U.S.A. 77: 1783–1786.
Ciechanover, A., Haller, H., Elias, S., Hass, A. L. and Hershko, A., 1980. Proc. Natl. Acad. Sci. U.S.A. 77: 1365–1368.
Rapoport, S., Schewe, T., Wiesner, R., Halangk. W., Ludwig, P., Janicke-Höhne, M., Tannert, Chr., Heibsch, Ch. and Klatt, D., 1979. Eur. J. Biochem. 96: 545–561.
Dubiel, W., Müller, M. and Rapoport, S., 1981. Biochem. Int. 3: 165–171.
Glowacki, E. and Millette, R., 1965. J. Mol. Biol. 11: 116–127.
Seaman, C., Wyss, S. and Piomelli, S., 1980. Am. J. Hematol. 8: 31–42.
Pontremoli, S., Salamino, F., Sparatore, B., Melloni, E., Morelli, A., Benatti, U. and De Flora, A., 1979. Biochem. J. 181: 559–568.
Pontremoli, S., Melloni, E., Salamino, F., Sparatore, B., Michetti, M., Benatti, U., Morelli, A. and De Flora, A., 1980. Eur. J. Biochem. 110: 421–430.
Chandler, C. F. and Ballard, F. J., 1978. Biochem. J. 176: 151–158.
Wilkinson, K. D., Urban, M. K. and Haas, A. L., 1980. J. Biol. Chem. 255: 7529–7532.
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Magnani, M., Stocchi, V., Dachà, M. et al. Rabbit red blood cell hexokinase. Mol Cell Biochem 61, 83–92 (1984). https://doi.org/10.1007/BF00239607
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DOI: https://doi.org/10.1007/BF00239607