178
Views
28
CrossRef citations to date
0
Altmetric
Original Article

Heat shock protein 72 (HSP72), hyperthermia-inducible immunogenic determinant on leukemic K562 and Ewing's Sarcoma cells

Pages 39-48 | Accepted 22 Aug 1996, Published online: 09 Jul 2009

References

  • Bienz M., Pelham H. R. Mechanisms of heat-shock gene activation in higher eukaryotes. Advances in Genetics 1987; 24: 31–72
  • Booth C., Koch G. L. E. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 1989; 59: 729–737
  • Botzler C., Kolb H-J., Issels R. D., Multhoff G. Noncytotoxic alkyl-lyso-phospholipid treatment increases sensitivity of leukemic K562 cells to lysis by natural killer cells. International Journal of Cancer 1996; 65: 633–638
  • Chirico W. J., Waters M. G., Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 1988; 332: 805–810
  • Denagel D. C., Pierce S. K. Heat shock proteins in immune responses. Critical Review in Immunology 1993; 13: 71–81
  • DiCesare S., Poccia F., Mastino A., Colizzi V. Surface expressed heat-shock proteins by tressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity. Immunology 1992; 76: 341–343
  • Ferrarini M., Heltai S., Zocchi M. R., Rugarli C. Unusual expression and localization of heat-shock proteins in human cells. International Journal of Cancer 1992; 51: 613–619
  • Heufelder A. E., Wenzel B. E., Bahn R. S. Cell surface localization of a 72kDa heat shock protein in retroocular fibroblasts from patients with Graves' opthalmopathy. Journal of Clinical Endocrinology and Metabolisms 1992; 74: 732–736
  • Hightower L. E., Guidon P. T. Selective release form cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. Journal of Cell Physiology 1989; 138: 257–266
  • Issels R. D., Prenninger S. W., Nagele A., Boehm E., Sauer H., Jauch K. W., Denecke H., Berger H., Peter K., Wilmanns W. Ifosfamide plus etoposide combined with regional hyperthermia in patients with locally advanced sarcomas: a phase II study. Journal of Clinical Oncology 1990; 8: 1818–1829
  • Konno A., Sato N., Yagihashi A., Torigoe T., Cho J. M., Torimoto K., Hara I., Wada Y., Okubo M., Takahashi N. Heat- or stress-inducible transformation-associated cell surface antigen on the activated H-ras oncogene-transfected rat fibroblast. Cancer Research 1989; 49: 6578–6582
  • Li Z., Srivastava P. K. Tumor rejection antigen gp96/grp97 is an ATPase: implications for folding and antigen presentation. EMBO Journal 1993; 12: 1343–3151
  • Lindquist S. The heat-shock response. Annu. Rev. Biochem. 1986; 55: 1151–1191
  • McCoy J. L., Jerome L. J., Cannon G. B., Pomeroy T. C., Connor R. J., Oldham R. K., Weese J. L., Herbermann R. B. Leukocyte migration inhibition in patients with Ewing's sarcoma by 3-M potassium chloride extracts of fresh and tissue-cultured Ewing's sarcoma. Journal of the National Cancer Institute 1977; 59: 1119–1125
  • Morimoto R. I. Cells in stress: transcriptional activation of heat shock genes. Science 1993; 259: 1409–1410
  • Multhoff G., Botzler C., Wiesnet M., Müller E., Meier T., Issels R. D. A stress-inducible 72 kDa heat shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. International Journal of Cancer 1995a; 61: 272–279
  • Multhoff G., Botzler C., Wiesnet M., Eibner G., Issels R. CD3-large granular lymphocytes recognize a heat-inducible immunogenic determinant associated with the 72-kDa heat shock protein on human sarcoma cells. Blood 1995b; 86: 1374–1382
  • Multhoff G., Hightower L. Cell surface expression of HSP and the immune response. Cell Stress and Chaperones 1996; 1: 3
  • Pelham H. R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 1986; 46: 959–961
  • Sato N., Cho J. M., Takashima T., Tsuboi N., Nihei T., Wada Y., Kikuchi K. Immunogenicity and involvement in the host's effector mechanisms of the oncogene-induced transformation-associated cell surface antigens. In Vivo 1991; 5: 663–668
  • Heat shock: from bacteria to man. Cold Spring Harbor 1982, M. J. Schlesinger, M. Ashburner, A. Tissieres. Cold Spring Harbor Laboratory Press, New York 1982; 1–297
  • Srivastava P. K., Deleo A. B., Old L. J. Tumor rejection antigens of chemically induced sarcomas of inbred mice. Proceedings of the National Academy of Science USA 1986; 83: 3407–3411
  • Tamura Y., Tsuboi N., Sato N., Kikuchi K. 70kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity. Journal of Immunology 1993; 151: 5516–5524
  • Ullrich S. J., Robinson E. A., Law L. W., Willingham M., Appella E. A. Mouse tumor-specific transplantation antigen is a heat shock-related protein. Proceedings of the National Academy of Science, USA 1986; 83: 3121–3125
  • Vanbuskirk A., Crump B. L., Margoliash E., Pierce S. K. A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family. Journal of Experimental Medicine 1989; 170: 1799–1809
  • Welch W. J. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiological Review 1992; 72: 1063–1081
  • Welch W. J., Feramisco J. R. Nuclear and nucleolar localization of the 72.000 Dalton heat shock protein in heat shocked mammalian cells. Journal of Biological Chemistry 1984; 259: 4501–4513

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.