Expression of p56lck in B-Cell Neoplasias

Leukemia and Lymphoma

Volumn 26, Issue 42130, 1997, Pages 551-562

  Von Knethen, Andreas ^b   Abts, Harry ^a   Kube, Dieter ^a   Diehl, Volker ^a   Tesch, Hans ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

B cell neoplasias; p56lck

Indexed keywords

4' AMINO 6 HYDROXYFLAVONE; 4'-AMINO-6-HYDROXYFLAVONE; ANTI-IGM; ANTIIDIOTYPIC ANTIBODY; ENZYME INHIBITOR; FLAVONOID; IMMUNOGLOBULIN M ANTIBODY; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE;

ARTICLE; B CELL LEUKEMIA; B CELL LYMPHOMA; B LYMPHOCYTE; BIOSYNTHESIS; BURKITT LYMPHOMA; CELL CULTURE; DRUG ANTAGONISM; ENZYME ACTIVATION; HELA CELL; HODGKIN DISEASE; HUMAN; METABOLISM; PHOSPHORYLATION; STAPHYLOCOCCUS AUREUS; STIMULATION; CHRONIC LYMPHATIC LEUKEMIA; CONTROLLED STUDY; ENZYME ACTIVITY; EPSTEIN BARR VIRUS; HUMAN CELL; IMMUNOBLOTTING; LEUKEMIA CELL; LEUKEMIA CELL LINE; LYMPHOCYTE ACTIVATION; LYMPHOCYTE TRANSFORMATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTO ONCOGENE;

ANTIBODIES, ANTI-IDIOTYPIC; B-LYMPHOCYTES; BURKITT LYMPHOMA; ENZYME ACTIVATION; ENZYME INHIBITORS; FLAVONOIDS; HELA CELLS; HODGKIN DISEASE; HUMANS; LEUKEMIA, B-CELL, CHRONIC; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); LYMPHOMA, B-CELL; PHOSPHORYLATION; PROTEIN KINASE C; STAPHYLOCOCCUS AUREUS; STIMULATION, CHEMICAL; TETRADECANOYLPHORBOL ACETATE; TUMOR CELLS, CULTURED;

EID: 0030609158     PISSN: 10428194     EISSN: 10292403     Source Type: Journal    
DOI: 10.3109/10428199709050891     Document Type: Article

References (34)

1. Chow L. M. L., Veillette A. The src and csk families of tyrosine protein kinases in hematopoietic cells. Sem. Immunol. 1995; 7: 207 – 226
2. Gacon G., Gisselbrecht S., Piau J. P., Boissel J. P., Tolle J., Fischer S. High level of tyrosine protein kinase in a murine lymphoma cell line induced by Moloney leukemia virus. EMBO J. 1982; 1: 1579 – 1583
3. Veillette A., Horak I. D., Bookman M. A., Bolen J. B. Alterations of the lymphocyte-specific protein tyrosine kinase (p56lck) during T-cell activation. Mol. Cell. Biol. 1988; 8: 4353 – 4361
4. Hatakeyama M., Kono T., Kohayashi N., Kawahara A., Levin S. D., Perlmutter R. M., Taniguchi T. Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association. Science 1991; 252: 1523 – 1528
5. Cassatela M. A., Anegón I., Cuturi M. C., Griskey P., Trinchieri G., Perussia B. Fcy(CD16) interaction with ligand induces Ca2+ mobilization and phosphoinositide turnover in human natural killer cells. J. Exp. Med. 1989; 169: 549 – 567
6. Taieb J., Vitte-Mony I., Auffredou M. T., Dorseuil O., Gacon G., Bertoglio J., Vazquez A. Regulation of p56lck kinase expression and control of DNA synthesis in activated human B lymphocytes. J. Biol. Chem. 1993; 268: 9169 – 9171
7. Veillette A., Foss F. M., Sausville E. A., Bolen J. B., Rosen N. Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines. Oncogene Res. 1987; 1: 357 – 374
8. Sartor O., Gregory F. S., Templeton N. S., Pawar S., Perlmutter R. M., Rosen N. Selective expression of alternative lck mRNAs in human malignant cell lines. Mol. Cell. Biol. 1989; 99: 2983 – 2988
9. Brouns G. S., Devries E., Van Noesel C. J. M., Mason D. Y., Van Lier R. A. W., Borst J. The structure of the μ/pseudo light chain complex on the human pre-B cells is consistent with a function in signal transduction. Eur. J. Immunol. 1993; 23: 1088 – 1097
10. Adler H. T., Reynolds P. J., Kelley C. M., Sefton B. M. Transcriptional activation of lck by retrovirus promoter insertion between two lymphoid-specific promoters. J. Virol. 1988; 62: 4113 – 4122
11. Casnellie J. E., Harrison M. L., Hellstrom K. E., Krebs E. G. A lymphoma cell line expressing elevated levels of tyrosine protein kinase activity. J. Biol. Chem. 1983; 258: 10738 – 10741
12. Abraham K. M., Levin S. D., Marth J. D., Forbush K. A., Perlmutter R. M. Thymic tumorigenesis induced by overexpression of p56lck. Proc. Natl. Acad. Sci. USA 1991; 88: 3977 – 3981
13. Marth J. D., Overell R. W., Meier K. E., Krebs E. G., Perlmutter R. M. Translational activation of the lck proto-oncogene. Nature 1988; 332: 171 – 173
14. Adler H. T., Sefton B. M. Generation and characterization of transforming variants of the lck tyrosine protein kinase. Oncogene 1992; 7: 1191 – 1199
15. Mayer K. M., Ansotegui I., Ballhausen W. G. The human lck cDNA clone YT16 is a transforming oncogene. Anticancer Res. 1992; 12: 485 – 488
16. Jücker M., Abts H., Eick D., Lenoir G. M., Tesch H. Over-expression of lck in Burkitt's lymphoma cell lines. Leukemia 1991; 5: 528 – 30
17. Abts H., Jücker M., Diehl V., Tesch H. Human chronic lymphocytic leukemia cells regularly express mRNAs of the protooncogenes lck and c-fgr. Leukemia Res. 1991; 15: 987 – 997
18. Lenoir G. M., Vuillaume M., Bonnardel C. The use of lymphomatous and lymphohlastoid cell lines in the study of Burkitt's lymphoma. IARC Scientific Publication 1985; 59: 309 – 318
19. Tchou-Wong K. M., Weinstein I. B. Altered expression of protein kinase C, lck, and CD45 in a 12-O-tetradecanoylphorbol-13-acetate-dependent leukemic T-cell variant that expresses a high level of interleukin-2 receptor. Mol. Cell. Biol. 1992; 12: 394 – 401
20. Degiannis D., Hornung N., Luke-Gustites D., Raskova J., Raska K. IL-4 receptor expression by SAC-acti-vated B-lymphoctes: its role in B-cell proliferation and the effect of cyclospoiine (CsA), prednisolone and verapmil. Int. J. Immunopharmacol. 1993; 15: 829 – 32
21. Aoki Y., Isselbacher K. J., Cherayil B. J., Pillai S. Tyrosine phosphorylation of Blk and Fyn Src homol-ogy 2 domain-binding protein occurs in response to antigen-receptor ligation in B cells and constitutively, in pre-B cells. Proc. Natl. Acad. Sci. USA 1994; 91: 4204 – 8
22. Danielian S., Alcover A., Polissard L., Stefanescu M., Acuto O., Fischer S., Fagard R. Both T cell receptor (TcR)-CD3 complex and CD2 increase the tyrosine kinase activity of p56lck. CD2 can mediate TcR-CD3-indepen-dent and CD45-dependent activation of p56lck. Eur. J. Immunol. 1992; 22: 2915 – 2921
23. Danielian S., Fagard R., Boulet I., Fischer S. The retarded electrophoretic migration of p56lck induced by vanadate in lymphoma cells correlates with modified kinase activity. Biochimie 1990; 72: 315 – 322
24. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680 – 685
25. Danielian S., Fagard R., Alcover A., Acuto O., Fischer S. The lymphocyte-specific protein tyrosine kinase p56lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T cell receptor or CD2. Eur. J. Immunol. 1989; 19: 2183 – 2189
26. Angel P., Imagawa M., Chiu R., Stein B., Imbra R. J., Rahmsdorf H. J., Jonat C., Herrlich P., Karin M. Phorbol ester-inducible genes contain a comman cis element recognized by a TPA-modulated fransacting factor. Cell 1987; 49: 729 – 739
27. Makover D., Cuddy M., Yum S., Bradley K., Alpers J., Sukhatme V., Reed J. C. Phorhol ester-mediated inhibition of growth and regulation of proto-oncogene expression in the human T cell leukemia line Jurkat. Oncogene 1991; 6: 455 – 460
28. Burckhardt A. L., Brunswick M., Bolen J. B., Mond J. J. Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 1991; 88: 7410 – 7414
29. Campbell M.-A., Sefton B. M. Association between B-lymphocyte membrane immunoglobulin and multiple members of the src family of protein tyrosine kinases. Mol. Cell. 1992; 12: 2315 – 2321, Biol.
30. Cheah M. S., Ley T. J., Tronick S. R., Robbins K. C. fgr proto-oncogene mRNA induced in B lymphocytes by Epstein-Ban virus infection. Nature 1986; 319: 238 – 240
31. Wang F., Gregory C. D., Rowe M., Rickinson A. B., Wang D., Birkenbach M., Kikutani H., Kishimoto T., Kieff E. Epstein-Barr virus nuclear antigen 2 specifically induces expression of the B-cell activation antigen CD23. Proc. Natl. Acad. Sci. USA 1987; 84, 3452–3457.
32. Wang F., Gregory C., Sample C., Rowe M., Liebowitz D., Murray R., Rickinson A., Kieff E. Epstein-Barr virus latent membrane protein (LMPl) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA2 and LMPl cooperatively induce CD23. J. Virol. 1990; 64: 2309 – 2318
33. Miyazaki T., Liu Z. J., Kawahara A., Minami Y., Yamada K., Tsujimoto Y., Barsoumian E. L., Perlmutter R. M., Taniguchi T. Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and Ick cooperate in hematopoietic cell proliferation. Cell 1995; 81: 223 – 231
34. Van Oers N. S., Lilleen N., Weiss A. Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 1996; 183: 1053 – 62