Abstract
Lactogen-dependent Nb2 lymphoma cells, widely employed for studying prolactin (PRL) mitogenic mechanisms, are also useful for investigations of apoptosis in T-lineage lymphocytes. Utilizing PRL-dependent Nb2-11 cultures, apoptosis-regulatory genes were evaluated for participation in dexamethasone-(DEX) provoked cell death or its inhibition by PRL. Treatment of lactogen-starved, G1-arrested Nb2-11 cells with DEX (100 nM) activated apoptosis within 12 h evaluated by flow cytometric analysis of fragmented DNA. This effect was not associated with altered expression of bcl-2, bax, or pim-1. PRL (10 ng/mL), coincubated with DEX-treated cells, completely blocked DEX-induced apoptosis. This inhibition was associated with increased expression of bcl-2 and pim-1 mRNAs, genes reported to suppress apoptosis, within 2–6 h after addition of the hormone. Moreover, the increased transcription of bcl-2 and pim-1 was coupled to increases in their protein levels. The results suggest that bcl-2, bax, and pim-1 do not play a critical role in DEX-induced apoptosis in Nb2 cells. However, expression of bcl-2, together with pim-1, may have a role in mediating the antiapoptotic actions of PRL.
Similar content being viewed by others
References
Gout P. W., Beer, C. T., and Noble R. L. (1980). Cancer Res. 40, 2433–2436.
Fleming, W. H., Pettigrew, N. M., Matusik, R. J., and Friesen, H. G. (1982). Cancer Res. 42, 3138–3141.
Gout P. W., Horsman, D. E., Fox, K., de Jong, G., Ma, S., and Bruchovsky, N. (1994). Anticancer Res. 14, 2485–2492.
Richards J. F., Beer C. T., Bourgeault C., Chen K., and Gout P. W. (1982). Mol. Cell. Endocrinol. 26, 41–49.
Horseman N. D. (1995). Endocrinology 136, 5249–5251.
Lebron, J. J., Ali, S., Sofer, L., Ullrich, A., and Kelly, P. A. (1994). J. Biol. Chem. 269, 14,021–14,026.
Clevenger, C. V. and Medaglia, M. V. (1994). Mol. Endocrinol. 8, 674–681.
Rao, Y-P., Buckley, D. J., and Buckley, A. R. (1995). Cell Growth Differ. 6, 1235–1244.
Stevens, A. M., Wang, Y-F., Sieger, K. A., Lu, H-F., and Yu-Lee, L-Y. (1995). Mol. Endocrinol. 9, 513–525.
Erwin, R. A., Kirken, R. A., Malabarba, M. G., Farrar, W. L., and Rui, H. (1995). Endocrinology 136, 3512–3518.
Buckley, A. R., Buckley, D. J., Leff, M. A., Hoover, D. S., and Magnuson, N. S. (1995). Endocrinology 136, 5252–5259.
Fletcher-Chiappini, S. E., Compton, M. M., La Voie, H. A., Day, E. B., and Witorsch, R. J. (1993). Proc. Soc. Exp. Biol. Med. 202, 345–352.
Witorsch, R. J., Day, E. B., LaVoie, H. A., Hashemi, N., and Taylor, J. K. (1993). Proc. Soc. Exp. Biol. Med. 203, 454–460.
LaVoie, H. A. and Witorsch, R. J. (1995). Proc. Soc. Exp. Biol. Med. 209, 257–269.
Kerr, J. F., Wyllie, A. H., and Currie, A. R. (1972). Br. J. Cancer 26, 239–257.
Raff, M. C. (1992). Nature 356, 397–400.
Peitsch, M. C., Muller, C., and Tschopp, J. (1993). Nucleic Acids Res. 21, 4206–4209.
Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S. (1998) Nature 391, 43–50.
Bakhshi, A., Jensen, J. P., Goldman, P., Wright, J. J., McBride, O. W., Epstein, A. L., et al. (1985). Cell 41, 899–906.
Cleary, M. L. and Sklar, J. (1985). Proc. Natl. Acad. Sci. USA 82, 7439–7443.
Tsujimoto, Y. and Croce, C. M. (1986). Proc. Natl. Acad. Sci. USA 83, 5214–5218.
Oltvai, Z. N., Milliman, C. L., and Korsmeyer, S. J. (1993). Cell 74, 609–619.
Ohta, K., Iwai, K., Kasahara, Y., Taniguchi, N., Krajewski, S., Reed, J. C., et al. (1995). Int. Immunol. 7, 1817–1825.
McDonnell, T. J., Deane, N., Platt, F. M., Nunez, G., Jaeger, U., McKearn, J. P., et al. (1989). Cell 57, 79–88.
McDonnell, T. J., Nunez, G., Platt, F. M., Hockenberry, D., London, L., McKearn, J. P., et al. (1990). Mol. Cell Biol. 10, 1901–1907.
McDonnell, T. J. and Korsmeyer, S. J. (1991). Nature 349, 254–256.
Leff, M. A., Buckley, D. J., Krumenacker, J. S., Reed, J. C., Miyashita, T., and Buckley, A. R. (1996). Endocrinology 137, 5456–5462.
Yin, X. M., Oltval, Z. N., and Korsmeyer, S. J. (1994). Nature 369, 321–323.
Zha, H., Aime-Sempe, C., Sato, T., and Reed, J. C. (1996). J. Biol. Chem. 271, 7440–7444.
Amson, R., Sigaux, F., Przedborski, S., Flandrin, G., Givol, D., and Telerman, A. (1989). Proc. Natl. Acad. Sci. USA 86, 8857–8861.
Meeker, T. C., Nagarajan, L., ar-Rushdi, A., and Croce, C. M. (1987). J. Cell. Biochem. 35, 105–112.
Dautry, F., Weil, D., Yu J., and Dautry-Varsat, A. (1988). J. Biol. Chem. 263, 17,615–17,620.
Liang, H., Hittelman, W., and Nagarajan, L. (1996). Arch. Biochem. Biophys. 330, 259–265.
Moroy, T., Grzeschiczek, A., Petzold, S., and Hartmann, K. U. (1993). Proc. Natl. Acad. Sci. USA 90, 10,734–10,738.
Takahashi, C., Harada, Y., Ariga, H., and Iguchi-Ariga, S. M. (1995). Biochem. Biophys. Res. Commun. 215, 538–546.
Nicoletti, I., Migliorati, G., Pagliacci, M. C., Grignani, F., and Riccardi, C. (1991). J. Immunol. Methods 139, 271–279.
Feinberg, A. P. and Vogelstein, B. (1983). Anal. Biochem. 132, 6–13.
Church, G. M. and Gilbert, W. (1984). Proc. Natl. Acad. Sci. USA 81, 1991–1995.
Broome, H. E., Dargan, C. M., Krajewski, S., and Reed, J. C. (1995). J. Immunol. 155, 2311–2317.
Buckley, A. R., Buckley, D. J., Gout, P. W., Liang, H-Q., Rao, Y-P., and Blake, M. J. (1993). Mol. Cell. Endocrinol. 98, 17–25.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Krumenacker, J.S., Buckley, D.J., Leff, M.A. et al. Prolactin-regulated apoptosis of Nb2 lymphoma cells. Endocr 9, 163–170 (1998). https://doi.org/10.1385/ENDO:9:2:163
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1385/ENDO:9:2:163