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 Blood, 1 May 2007, Vol. 109, No. 9, pp. 3849-3855.
Prepublished online as a Blood First Edition Paper on February 13, 2007; DOI 10.1182/blood-2006-11-056879.

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IMMUNOBIOLOGY

Nur77 converts phenotype of Bcl-B, an antiapoptotic protein expressed in plasma cells and myeloma

Frederic Luciano1, Maryla Krajewska1, Paulina Ortiz-Rubio1, Stan Krajewski1, Dayong Zhai1, Benjamin Faustin1, Jean-Marie Bruey1, Beatrice Bailly-Maitre1, Alan Lichtenstein2, Siva Kumar Kolluri1, Arnold C. Satterthwait1, Xiao-Kun Zhang1, and John C. Reed1

1 Burnham Institute for Medical Research, La Jolla, CA; 2 Veterans Administration Greater Los Angeles Healthcare System, CA

Defects in apoptosis mechanisms play important roles in malignancy and autoimmunity. Orphan nuclear receptor Nur77/TR3 has been demonstrated to bind antiapoptotic protein Bcl-2 and convert it from a cytoprotective to a cytodestructive protein, representing a phenotypic conversion mechanism. Of the 6 antiapoptotic human Bcl-2 family members, we found that Nur77/TR3 binds strongest to Bcl-B, showing selective reactivity with Bcl-B, Bcl-2, and Bfl-1 but not Bcl-XL, Mcl-1, or Bcl-W. Nur77 converts the phenotype of Bcl-B from antiapoptotic to proapoptotic. Bcl-B is prominently expressed in plasma cells and multiple myeloma. Endogenous Bcl-B associates with endogenous Nur77 in RPMI 8226 myeloma cells, where RNA interference experiments demonstrated dependence on Bcl-B for Nur77-induced apoptosis. Furthermore, a Nur77-mimicking peptide killed RPMI 8226 myeloma cells through a Bcl-B–dependent mechanism. Because Bcl-B is abundantly expressed in plasma cells and some myelomas, these findings raise the possibility of exploiting the Nur77/Bcl-B mechanism for apoptosis for eradication of autoimmune plasma cells or myeloma.


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Bcl-B and Nur77/TR3: a deadly combination
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Blood 2007 109: 3622. [Full Text] [PDF]



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