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Blood, 15 February 2006, Vol. 107, No. 4, pp. 1413-1420. Prepublished online as a Blood First Edition Paper on September 15, 2005; DOI 10.1182/blood-2005-07-2648. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-07-2648v1 107/4/1413    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Cohen-Saidon, C. Articles by Razin, E. Search for Related Content PubMed PubMed Citation Articles by Cohen-Saidon, C. Articles by Razin, E. Related Collections Immunobiology Apoptosis Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Antiapoptotic function of Bcl-2 in mast cells is dependent on its association with heat shock protein 90 Cellina Cohen-Saidon, Irit Carmi, Avishai Keren, and Ehud Razin From the Department of Biochemistry, Hebrew University Hadassah Medical School, Jerusalem, Israel. In the present study, we demonstrated that the antiapoptotic function of Bcl-2 in mast cells is significantly dependent on its association with the heat shock protein 90 (Hsp90). Dissociation of these 2 proteins inhibits the antiapoptotic activity of Bcl-2 by initiating the release of cytochrome c from mitochondria into cytosol and increasing the activity of caspase 3 and caspase 7, resulting in mast-cell apoptosis. The antiapoptotic activity of Bcl-2 was greatly affected by knocking-out specifically Hsp90 using the RNA interference approach. Thus, for the first time, it has been shown that Hsp90 might modulate the antiapoptotic activity of Bcl-2 at least in mast cells. These findings could have implications for a novel strategy of regulating apoptosis in patients with mastocytosis and other mast cell–associated diseases. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. Stuehler, S. Mielke, M. Chatterjee, J. Duell, S. Lurati, F. Rueckert, H. Einsele, R. C. Bargou, and M. S. Topp Selective depletion of alloreactive T cells by targeted therapy of heat shock protein 90: a novel strategy for control of graft-versus-host disease Blood, September 24, 2009; 114(13): 2829 - 2836. [Abstract] [Full Text] [PDF] A. V. Andreeva, M. A. Kutuzov, and T. A. Voyno-Yasenetskaya G{alpha}12 is targeted to the mitochondria and affects mitochondrial morphology and motility FASEB J, August 1, 2008; 22(8): 2821 - 2831. [Abstract] [Full Text] [PDF] C.-C. Kuo, C.-M. Liang, C.-Y. Lai, and S.-M. Liang Involvement of Heat Shock Protein (Hsp)90beta but Not Hsp90{alpha} in Antiapoptotic Effect of CpG-B Oligodeoxynucleotide J. Immunol., May 15, 2007; 178(10): 6100 - 6108. [Abstract] [Full Text] [PDF] M. Chatterjee, S. Jain, T. Stuhmer, M. Andrulis, U. Ungethum, R.-J. Kuban, H. Lorentz, K. Bommert, M. Topp, D. Kramer, et al. STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90{alpha} and {beta} in multiple myeloma cells, which critically contribute to tumor-cell survival Blood, January 15, 2007; 109(2): 720 - 728. [Abstract] [Full Text] [PDF] B. Vergnes, B. Gourbal, I. Girard, S. Sundar, J. Drummelsmith, and M. Ouellette A Proteomics Screen Implicates HSP83 and a Small Kinetoplastid Calpain-related Protein in Drug Resistance in Leishmania donovani Clinical Field Isolates by Modulating Drug-induced Programmed Cell Death Mol. Cell. Proteomics, January 1, 2007; 6(1): 88 - 101. [Abstract] [Full Text] [PDF]

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