Cell surface localization of the 78 kD glucose regulated protein (GRP 78) induced by thapsigargin

References

• Burel C., Mezger V., Pinto M., Rallu M., Trigon S., Morange M. Mammalian heat shock protein families. Expression and functions. Experientia 1992; 48: 629–634
   PubMedGoogle Scholar
• Haas I. G. BIP (GRP 78), an essential hsp 70 resident protein in the endoplasmic reticulum. Experientia 1994; 50: 1012–1020
   PubMedGoogle Scholar
• Little E., Ramakrishnan M., Roy B., Gazit G., Lee A. S. The glucose-regulated proteins (GRP 78 and GRP 94): functions, gene regulation, and applications. Critical Review Eukaryotic Gene Expression 1994; 4: 1–18
   PubMedGoogle Scholar
• Wong W. L., Brostrom M. A., Kuznetsov G., Gmitter-Yellen D., Bostrom C. O. Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells. Biochemical Journal 1993; 289: 71–79
   PubMed Web of Science ®Google Scholar
• Cheng T. C., Benton H. P. The intracellular Ca2+-pump inhibitors thapsigargin and cyclopiazonic acid induce stress proteins in mammalian chondrocytes. Biochemical Journal 1994; 301: 563–568
   PubMed Web of Science ®Google Scholar
• Inesi G., Sagara Y. Thapsigargin, a high affinity and global inhibitor of intracellular Ca2+-transport ATPases. Archives of Biochemistry and Biophysics 1992; 298: 313–317
   PubMed Web of Science ®Google Scholar
• Demaurex N., Lew D. P., Krause K. H. Cyclopiazonic acid depletes intracellular Ca2+ stores and activates an influx pathway for divalent cations in HL-60 cells. Journal of Biological Chemistry 1992; 267: 2318–2324
   PubMed Web of Science ®Google Scholar
• Ghosh T. K., Bian J. H., Short A. D., Rybak S. L., Gill D. L. Persistent intracellular calcium pool depletion by thapsigargin and its influence on cell growth. Journal of Biological Chemistry 1991; 266: 24690–24697
   PubMed Web of Science ®Google Scholar
• Li W. W., Alexandre S., Cao X., Lee A. S. Transactivation of the GRP 78 promoter by Ca2+ depletion. A comparative analysis with A23187 and the endoplasmic reticulum Ca2+-ATPaase inhibitor thapsigargin. Journal of Biological Chemistry 1993; 268: 12003–12009
   PubMed Web of Science ®Google Scholar
• Delpino A., Lapenta V., Piselli P., Fucile S. Thapsigargin induces 78K GRP in human TE 671/RD cells. Journal of Experimental and Clinical Cancer Research 1994; 13: 373–379
   Web of Science ®Google Scholar
• Delpino A., Piselli P., Mangano G. Protein synthesis in TE 671/RD (human rabdomiosarcoma) cells treated with thapsigargin and hyperthermia: impairment of HSP 70 induction. Journal of Biological Regulators and Homeostatic Agents 1995; 9: 132–138
   PubMed Web of Science ®Google Scholar
• Multhoff G., Hightower L. E. Cell surface expression of heat shock proteins and the immune response. Cell Stress and Chaperones 1996; 1: 167–176
   PubMed Web of Science ®Google Scholar
• Takemoto H., Yoshimori T., Yamamoto A., Miyata Y., Yahara I., Inoue K., Tashiro Y. Heavy chain binding protein (BIP/GRP 78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Archives of Biochemistry and Biophysics 1992; 296: 129–136
   PubMed Web of Science ®Google Scholar
• Altmeyer A., Maki R. G., Feldweg A. M., Heike M., Protopopov V. P., Masur S. K., Srivastava P. K. Tumor-specific cell surface expression of the-KDEL containing, endoplasmic reticular heat shock protein gp96. International Journal of Cancer 1996; 69: 340–349
   PubMed Web of Science ®Google Scholar
• Chouchane L., Bowers F. S., Sawasdikosol S., Simpson R. M., Kindt T. J. Heat shock proteins expressed on the surface of human T cell leukemia virus Type I-infected cell lines induce autoantibodies in rabbits. Journal of Infectious Diseases 1994; 169: 253–259
   PubMed Web of Science ®Google Scholar
• Heufelder A. E., Wenzel B. E., Bahn R. S. Cell surface localization of a 72 kilodalton heat shock protein in retro-ocular fibroblasts from patients with Graves' ophthalmopathy. Journal of Clinical Endocrinology and Metabolism 1992; 74: 732–736
   PubMed Web of Science ®Google Scholar
• Ferrqrini M., Heltai S., Zocchi M. R., Rugarli C. Unusual expression and localization of heat-shock proteins in human tumor cells. International Journal of Cancer 1992; 51: 613–619
   PubMed Web of Science ®Google Scholar
• Piselli P., Vendetti S., Vismara D., Poccia F., Delpino A., Ivanyi J., Colizzi V. Intracytoplasmatic and membrane expression of 28–, 65, and 70 kDa heat shock proteins on lymphomonocytoid tumor cell lines. Fundamental and Clinical Immunology 1994; 2: 45–51
   Google Scholar
• Multhoff G., Botzer C., Wiesnet M., Muller E., Meier T., Wilmanns W., Issels R. D. A stress-inducible 72 kDa heat-shock protein (HSP 72) is expressed on the surface of human tumor cells but not on normal cells. International Journal of Cancer 1995; 61: 272–279
   PubMed Web of Science ®Google Scholar
• De Nagel D. C., Pierce S. K. A case for chaperones in antigen processing. Immunology Today 1992; 13: 86–90
   PubMedGoogle Scholar
• Wiest D. L., Burgess W. H., McKean D., Kearse K. P., Singer A. The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes. EMBO Journal 1995; 14: 3425–3433
   PubMed Web of Science ®Google Scholar
• Winfield J. B., Jarjour W. N. Stress proteins, autoimmunity, and autoimmune disease. Current Topics in Microbiology and Immunology 1991; 167: 161–187
   PubMed Web of Science ®Google Scholar
• Srivastava P. K. Heat shock proteins in immune response to cancer: the fourth paradigm. Experientia 1994; 50: 1054–1060
   PubMedGoogle Scholar
• Suto R., Srivastava P. K. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 1995; 269: 1585–1588
   PubMed Web of Science ®Google Scholar
• Kaur I., Voss S. D., Gupta R. S., Schell K., Fisch P., Sondel P. M. Human periferal gamma delta T cells recognize Hsp60 molecules on Daudi Burkitt's lymphoma cells. Journal of Immunology 1993; 150: 2046–2055
   PubMed Web of Science ®Google Scholar
• Wileman T., Kane L. P., Carson G. R., Terhorst C. Depletion of cellular calcium accelerates protein degradation in the endoplasmic reticulum. Journal of Biological Chemistry 1991; 266: 4500–4507
   PubMed Web of Science ®Google Scholar
• Jiang S., Chow S. C., Nicotera P., Orrenius S. Intracellular Ca2+ signals activate apoptosis in thymocytes: studies using the Ca2+-ATPase inhibitor thapsigargin. Experimental Cell Research 1994; 212: 84–92
   PubMed Web of Science ®Google Scholar
• Furuya Y., Lundmo P., Short A. D., Gill D. L., Isaacs J. T. The role of calcium, pH, and cell proliferation in the programmed (apoptotic) death of androgen-independent pro-static cancer cells induced by thapsigargin. Cancer Research 1994; 54: 6167–6175
   PubMed Web of Science ®Google Scholar
• Poccia F., Piselli P., Vendetti S., Bach S., Amendola A., Placido R., Colizzi V. Heat-shock protein expression on the membrane of T cells undergoing apoptosis. Immunology 1996; 88: 6–12
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T/4. Nature 1978; 274: 699–701
   PubMed Web of Science ®Google Scholar
• Chamberlain J. P. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Analytical Biochemistry 1979; 98: 132–135
   PubMed Web of Science ®Google Scholar