Effects of geldanamycin, a heat-shock protein 90-binding agent, on T cell function and T cell nonreceptor protein tyrosine kinases

Journal of Immunology

Volumn 164, Issue 6, 2000, Pages 2915-2923

  Yorgin, Peter D ^a,c   Hartson, Steven D ^b   Fellah, Abdul M ^a   Scroggins, Bradley T ^b   Huang, Wenjun ^b   Katsanis, Emmanuel ^a   Couchman, Jeff M ^a   Matts, Robert L ^b   Whitesell, Luke ^a  

^a UNIVERSITY OF ARIZONA COLLEGE OF MEDICINE   (United States)

^b OKLAHOMA STATE UNIVERSITY   (United States)

^c STANFORD UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONCANAVALIN A; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HERBIMYCIN; INTERLEUKIN 2; LACTACYSTIN; PROTEASOME INHIBITOR;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL SURVIVAL; CONTROLLED STUDY; DOSE RESPONSE; DOSE TIME EFFECT RELATION; DRUG PROTEIN BINDING; ENZYME INHIBITOR COMPLEX; ENZYME SPECIFICITY; IMMUNOMODULATION; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; T LYMPHOCYTE ACTIVATION;

EID: 0034654091     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.6.2915     Document Type: Article

References (46)

1. Whitesell, L., E. G. Mimnaugh, B. De Costa, C. E. Myers, and L. M. Neckers. 1994. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinoid ansamycins: essential role for stress proteins in oncogene transformation. Proc. Natl. Acad. Sci. USA 91:8324.
2. Stebbins, C. E., A. A. Russo, C. Schneider, N. Rosen, F. U. Hart, and N. P. Pavletich. 1997. Crystal structure of an hsp-90-geldanamycin complex: targeting of a protein chaperone by an anti-tumor agent. Cell 89:239.
3. Pratt, W. B., and D. O. Toft. 1997. Steroid receptor interactions with heat shock protein and immunophillin chaperones. Endocr. Rev. 18:306.
4. Csermely, P., T. Schnaider, C. Soti, Z. Prohaszka, and G. Nardai. 1998. The 90 kDa molecular chaperone family: structure, function, and clinical applications: a comprehensive review. Phamacol. Ther. 79:129.
5. Whitesell, L., and P. Cook. 1996. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10:705.
6. Bramberger, C. M., M. Wald, A. Bramberger, and H. M. Schultz. 1997. Inhibition of mineralocorticoid and glucocorticoid function by the heat shock protein 90-binding agent geldanamycin. Mol. Cell. Endocrinol. 131:233.
7. Segnitz, B., and U. Gehring. 1997. The function of steroid homone receptors is inhibited by the hsp90-specific compound geldanamycin. J. Biol. Chem. 272:18694.
8. Schulte, T. W., M. V. Blagosklonny, C. Ingui, and L. Neckers. 1995. Disruption of Raf-1-hsp90 molecular complex results in destabilization of Raf-1 and loss if Raf-1-Ras association. J. Biol. Chem. 270:24585.
9. Schulte, T. W., M. V. Blagosklonny, L. Romanova, J. F. Mushinski, B. P. Monia, J. F. Johnston, P. Nguyen, J. Trepel, and L. M. Neckers. 1996. Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway. Mol. Cell. Biol. 16:5839.
10. Stancato, L. F., A. M. Silverstein, J. K. Ownes-Grillo, Y. Chow, R. Jove, and W. B. Pratt. 1997. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J. Biol. Chem. 272:4013.
11. Schulte, T. W., W. G. An, and L. M. Neckers. 1997. Geldanamycin-induced destabilization of Raf-1 involves the proteosome. Biochem. Biophys. Res. Commun. 239:655.
12. Blagosklonny, M. V., J. Toretsky, and L. M. Neckers. 1995. Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene 11:933.
13. Dasgupta, G., and J. Momand. 1997. Geldanamycin prevents nuclear translocation of mutant p53. Exp. Cell Res. 737:29.
14. Whitesell, L., P. Suthphin, W. G. An, M. Blagosklonny, T. Schulte, and L. Neckers. 1997. Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteosome in vivo. Oncogene 14:2809.
15. Hartson, S. D., and R. L. Matts. 1994. Association of hsp90 with cellular Src-family kinases in a cell-free system correlates with an altered kinase structure and function. Biochemistry 33:8912.
16. lck. Biochemistry 35:13451.
17. Hartson, S. D., E. A. Ottinger, W. Huang, G. Barany, P. Burn, and R. L. Matts. 1998. Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase. J. Biol. Chem. 273:8475.
18. June, C. H., M. C. Fletcher, J. A. Ledbetter, J. A. Schieven, G. L. Scieven, J. N. Siegel, A. F. Phillips, and L. E. Samelson. 1990. Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction. Proc. Natl. Acad Sci. USA 87:7722.
19. Schnaider, T., J. Somogyi, P. Csermely, and M. Szamel. 1998. The hsp90-specific inhibitor, geldanamycin, blocks CD28-mediated activation of human T lymphocytes. Life Sci. 63:949.
20. lck. J. Exp. Med. 173:1421.
21. Persson, U., P. H. Bick, L. Hammerstrome, E. Moller, and C. I. Smith. 1978. Different requirements for T-cells responding to various doses of concanavalin A. Scand. J. Immunol. 8:291.
22. Gillis, S., M. M. Ferm, W. Ou, and K. A. Smith. 1978. T cell growth factor: parameters of production and a quantitative microassay for activity. J. Immunol. 120:2027.
23. lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T-cell receptor or CD2. Eur. J. Immunol. 19:2183.
24. Shaw, A. S., K. E. Amrein, C. Hammond, D. F. Stern, B. M. Sefton, and J. K. Rose. 1989. The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 59:627.
25. Rudd, C. E., J. M. Trevillyan, J. D. Dasgupta, L. L. Wong, and S. F. Schlossman. 1988. The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human T lymphocytes. Proc. Natl. Acad. Sci. USA 85:5190.
26. Straus, D. B., and A. Weiss. 1992. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T-cell antigen receptor. Cell 70:585.
27. Sepp-Lorenzino, L., Z. Ma, D. E. Lebwohl, A. Vinitsky, and N. Rosen. 1995. Herbimycin A induces the 20 S proteosome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J. Biol. Chem. 270:16580.
28. c-erbB2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271:22796.
29. Loo, M. A., T. J. Jensen, L. Cui, Y. Hou, X. Chang, and J. R. Riordan. 1998. Pertubation of hsp90 interaction with nascent CFTR prevents its matuation and accelerates its decreation by the proteosome. EMBO J. 17:6879.
30. Dick, L. R., A. A. Cruikshank, L. Grenier, F. D. Melandri, S. L. Nunes, and R. L. Stein. 1996. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin β-lactone. J. Biol. Chem. 271:7273.
31. Scheffner, M., B. A. Werness, J. M. Huibregtse, A. J. Levine, and P. M. Howley. 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promote the degradation of p53. Cell 63:1129.
32. Kim, N., T. Yamaguchi, S. Sekine, M. Saeki, S. Iwamuro, and S. Kato. 1998. Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product. J. Biochem. 124:35.
33. Hatoum, O. A., S. Gross-Mesilaty, K. Breitschopf, A. Hoffman, H. Gonen, A. Ciechanover, and E. Bengal. 1998. Degradation of myogenic transcription factor MyoD by the ubiquitin pathway in vivo and in vitro: regulation by specific DNA binding. Mol. Cell. Biol. 18:5670.
34. Iwamuro, S., M. Saeki, and S. Kato. 1999. Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate. J. Biochem. 126:48.
35. Supko, J. G., R. L. Hickman, M. R. Grever, and L. Malspeis. 1995. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother. Pharmacol. 36:305.
36. Whitesell, L., S. D. Shifrin, G. Schwab, and L. M. Neckers. 1992. Benzoquinoid ansamycins possess selective tumoricidal activity unrelated to src kinase inhibition. Cancer Res. 52:1721.
37. Lele, Z., S. D. Hartson, C. C. Martin, L. Whitesell, R. L. Matts, and P. H. Krone. 1999. Disruption of Zebrafish somite development by pharmacologic inhibition of hsp90. Dev. Biol. 21:56.
38. Hartson, S. D., V. Thulasirman, W. Huang, L. Whitesell, and R. L. Matts. 1999. Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates. Biochemistry 38:3837.
39. v-src1. Cancer Res. 49:780.
40. Chen, H., S. S. Singh, and G. H. Perdew. 1997. The Ah receptor is a sensitive target of geldanamycin-induced protein turnover. Arch. Biochem. Biophys. 348:190.
41. Udvardy, A. 1996. The role of controlled proteolysis in cell-cycle regulation. Eur. J. Biochem. 240:307.
42. Meriin, A. B., V. L. Gabai, J. Yaglom, V. I. Shifrin, and M. Y. Sherman. 1998. Proteosome inhibitors activate stress kinases and induce hsp72. J. Biol. Chem. 273:6373.
43. Fenteany, G., and S. L. Schreiber. 1998. Lactacystin, proteosome function and cell fate. J. Biol. Chem. 273:8545.
44. Oda, H., S. Kumar, and P. M. Howley. 1999. Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination. Proc. Natl. Acad. Sci. USA 96:9557.
45. Laing, J., P. Tadros, E. Westphale. and E. C. Beyer. 1997. Degradation of connexin43 gap junction involves both the proteosome and lysosome. Exp. Cell Res. 236:482.
46. Matsuda, S., T. Suzuki-Fujimoto, A. Minowa, H. Ueno, K. Katamura, and S. Koyasu. 1999. Temperature-sensitive ZAP70 mutants degrading through a proteosome-independent pathway. J. Biol. Chem. 274:34515.