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Molecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase

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Abstract

Here we describe the purification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from normal leukocytes of healthy subjects and leukocytes of chronic myeloid leukemia (CML) patients and from normal mouse muscle and sarcoma tissue. The data indicate that some properties of GAPDH of leukocytes of CML patients and sarcoma tissues are similar and also similar to those of EAC (Ehrlich ascites carcinoma) cellular GAPDH but distinctly different from those of the normal cellular GAPDH. Polyclonal antiserum raised against the 54 kDa subunit of EAC cell GAPDH strongly reacted with GAPDH of leukocytes of CML patients and sarcoma tissue GAPDH only and weakly reacted with GAPDH of normal leukocyte and normal muscle and a variety of other tissues of normal rats. Both the subunits of GAPDH of sarcoma tissues were partially sequenced from the N-terminus and compared with the known sequences of GAPDH. The altered properties of GAPDH of three different malignant sources might be common feature of all malignant cells, which is discussed in relation to glycolysis and malignant aberrations.

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Abbreviations

CML:

chronic myeloid leukemia

EAC:

Ehrlich ascites carcinoma

GAPDH:

glyceraldehyde-3-phosphate dehydrogenase

References

  1. Ristow, M. (2006) Cur. Opin. Clin. Nut. Metab. Care, 9, 339–345.

    Article  CAS  Google Scholar 

  2. Costello, L. C., and Franklin, R. B. (2005) Mol. Cell. Biochem., 280, 1–8.

    Article  PubMed  CAS  Google Scholar 

  3. Gatenby, R. A., and Gillies, R. J. (2004) Nat. Rev. Cancer, 4, 891–899.

    Article  PubMed  CAS  Google Scholar 

  4. Wenner, C. E. (1975) in Cancer (Becker, F. F., ed.) Vol. 3, Plenum, New York, pp. 389–403.

    Google Scholar 

  5. Mazurek, S., Grimm, H., Boschek, C. B., Vaupel, P., and Eigenbrodt, E. (2002) Br. J. Nutr., 87, S23–S29.

    Article  PubMed  CAS  Google Scholar 

  6. Zu, X. L., and Guppy, M. (2004) Biochem. Biophys. Res. Commun., 313, 459–465.

    Article  PubMed  CAS  Google Scholar 

  7. Mathupala, S. P., Rempel, A., and Pedersen, P. L. (1997) J. Bioenerg. Biomembr., 29, 339–343.

    Article  PubMed  CAS  Google Scholar 

  8. Harris, J. I., and Waters, M. (1976) in The Enzymes (Boyer, P. D., ed.) 3rd Edn., Vol. 13, Academic Press, New York, pp. 1–49.

    Google Scholar 

  9. Tokunaga, K., Nakamura, Y., Sakata, K., Fujimori, K., Ohkubo, M., Sawada, K., and Sakiyama, S. (1987) Cancer Res., 47, 5616–5619.

    PubMed  Google Scholar 

  10. Epner, D. E., Partin, A. W., Schalken, J. A., Issacs, J. T., and Coffey, D. S. (1993) Cancer Res., 53, 1995–1997.

    PubMed  CAS  Google Scholar 

  11. Vila, M. R., Nicolas, A., Morote, J., de Torres, I., and Meseguer, A. (2000) Cancer, 89, 152–164.

    Article  PubMed  CAS  Google Scholar 

  12. Appelskog, I. B., Ammerpohl, O., Svechnikova, I. G., Lui, W. O., Almqvist, P. M., and Ekstrom, T. J. (2004) Int. J. Oncol., 24, 1419–1425.

    PubMed  CAS  Google Scholar 

  13. Isidoro, A., Casado, E., Redondo, A., Acebo, P., Espinosa, E., Alonso, A. M., Cejas, P., Hardisson, D., Fresno, V. J. A., Belda-Iniesta, C., Gonzalez-Baron, M., and Cuezva, J. M. (2005) Carcinogenesis, 26, 2095–2104.

    Article  PubMed  CAS  Google Scholar 

  14. Ng, E. K., Tusi, N. B., Lam, N. Y., Chiu, R. W., Yu, S. C., Wong, S. C., Lo, E. S., Rainer, T. H., Johnson, P. J., and Lo, Y. M. (2002) Clin. Chem., 48, 1212–1217.

    PubMed  CAS  Google Scholar 

  15. Ferguson, R. E., Carroll, H. P., Harris, A., Maher, E. R., Selby, P. J., and Banks, R. E. (2005) Proteomics, 5, 566–571.

    Article  PubMed  CAS  Google Scholar 

  16. Nakano, M., Funayama, S., de Oliveira, M. B. M., Bruel, S. L., and Gomes, E. M. (1992) Comp. Biochem. Physiol., 102B, 873–877.

    CAS  Google Scholar 

  17. Bagui, S., Ray, M., and Ray, S. (1999) Eur. J. Biochem., 262, 386–395.

    Article  PubMed  CAS  Google Scholar 

  18. Halder, J., Ray, M., and Ray, S. (1993) Int. J. Cancer, 54, 443–449.

    Article  PubMed  CAS  Google Scholar 

  19. Ray, M., Basu, N., and Ray, S. (1997) Mol. Cell. Biochem., 177, 21–26.

    Article  PubMed  CAS  Google Scholar 

  20. Gomes, E. M., Funayama, S., de Oliveira, M. B. M., Bruel, S. L., and Nakano, M. (1992) Comp. Biochem. Physiol., 102B, 879–884.

    CAS  Google Scholar 

  21. Epner, D. E., and Coffey, D. S. (1996) The Prostate, 28, 372–378.

    Article  PubMed  CAS  Google Scholar 

  22. Ghosh, S., Mukherjee, K., Ray, M., and Ray, S. (2001) Eur. J. Biochem., 268, 6037–6044.

    Article  PubMed  CAS  Google Scholar 

  23. Schroder, J.-M., Mrowietz, U., and Christophers, E. (1988) J. Immunol., 140, 3534–3540.

    PubMed  CAS  Google Scholar 

  24. Davis, B. J. (1964) Ann. N. Y. Acad. Sci., 121, 404–427.

    Article  PubMed  CAS  Google Scholar 

  25. Laemmli, U. K. (1970) Nature, 227, 680–685.

    Article  PubMed  CAS  Google Scholar 

  26. Layne, F. (1957) Meth. Enzymol., 3, 447–454.

    Article  Google Scholar 

  27. Oguchi, M., Meriwether, B. P., and Park, J. H. (1973) J. Biol. Chem., 248, 5562–5570.

    PubMed  CAS  Google Scholar 

  28. Yang, S. T., and Deal, W. C., Jr. (1964) Biochemistry, 8, 2806–2813.

    Article  Google Scholar 

  29. Launay, J. F., Jellali, A., and Vanier, M. T. (1989) Biochim. Biophys. Acta, 996, 103–109.

    PubMed  CAS  Google Scholar 

  30. Durrieu, C., Bernier-Valentin, F., and Rousset, B. (1987) Mol. Cell. Biochem., 74, 55–65.

    Article  PubMed  CAS  Google Scholar 

  31. Hara, M. R., Cascio, M., and Sawa, A. (2006) Biochim. Biophys. Acta, 1762, 502–509.

    PubMed  CAS  Google Scholar 

  32. Carujo, S., Estanyol, J. M., Ejarque, A., Agell, N., Bachs, O., and Pujol, M. J. (2006) Oncogene, 25, 4033–4042.

    Article  PubMed  CAS  Google Scholar 

  33. Levashov, P. A., Muronetz, V. I., Klyachko, N. L., and Nagradova, N. K. (1998) J. Protein Chem., 17, 229–235.

    Article  PubMed  CAS  Google Scholar 

  34. Welch, J. E., Brown, P. L., O’Brien, D. A., Magyar, P. L., Bunch, D. O., Mori, C., and Eddy, E. M. (2000) J. Androl., 21, 328–338.

    PubMed  CAS  Google Scholar 

  35. Casati, D. F. G., Sesma, J. I., and Iglesias, A. A. (2000) Plant Sci., 154, 107–115.

    Article  Google Scholar 

  36. Brooks, S. P., and Storey, K. B. (1991) Biochem. Int., 25, 477–489.

    PubMed  CAS  Google Scholar 

  37. Malhotra, O. P., Prabhakar, P., Sengupta, T., and Kayastha, A. M. (1995) Eur. J. Biochem., 227, 556–562.

    Article  PubMed  Google Scholar 

  38. Mazurek, S., Hugo, F., Failing, K., and Eigenbrodt, E. (1996) J. Cell. Physiol., 167, 238–250.

    Article  PubMed  CAS  Google Scholar 

  39. Fokina, K. V., Dainyak, M. B., Nagradova, N. K., and Muronetz, V. I. (1997) Arch. Biochem. Biophys., 345, 185–192.

    Article  PubMed  CAS  Google Scholar 

  40. Nguyen, T. N., Wang, H.-J., Zalzal, S., Nanci, A., and Nabi, I. R. (2000) Exp. Cell Res., 258, 171–183.

    Article  PubMed  CAS  Google Scholar 

  41. Dan’shina, P. V., Schmalhausen, E., Arutiunov, D. Y., Pleten’, A. P., and Muronetz, V. I. (2003) Biochemistry (Moscow), 68, 593–600.

    Article  Google Scholar 

  42. Mazzola, J. L., and Sirover, M. A. (2002) Brain Res. Mol. Brain Res., 100, 95–101.

    Article  PubMed  CAS  Google Scholar 

  43. Mazzola, J. L., and Sirover, M. A. (2003) J. Neurosci. Res., 71, 279–285.

    Article  PubMed  CAS  Google Scholar 

  44. Furuhata, A., Nakamura, M., Osawa, J., and Uchida, K. (2002) J. Biol. Chem., 277, 27919–27926.

    Article  PubMed  CAS  Google Scholar 

  45. Song, S., and Finkel, T. (2007) Nat. Cell. Biol., 9, 869–870.

    Article  PubMed  CAS  Google Scholar 

  46. Sirover, M. A. (2005) J. Cell. Biochem., 95, 45–52.

    Article  PubMed  CAS  Google Scholar 

  47. Glaser, P. E., Han, X., and Gross, R. W. (2002) Proc. Natl. Acad. Sci. USA, 99, 14104–14109.

    Article  PubMed  CAS  Google Scholar 

  48. Xing, C., LaPorte, J. R., Barbay, J. K., and Myers, A. G. (2004) Proc. Natl. Acad. Sci. USA, 101, 5862–5866.

    Article  PubMed  CAS  Google Scholar 

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Correspondence to M. Ray.

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Published in Russian in Biokhimiya, 2009, Vol. 74, No. 7, pp. 886–898.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM08-347, February 8, 2009.

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Patra, S., Ghosh, S., Bera, S. et al. Molecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase. Biochemistry Moscow 74, 717–727 (2009). https://doi.org/10.1134/S0006297909070037

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  • DOI: https://doi.org/10.1134/S0006297909070037

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