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The Journal of Immunology, 1998, 161: 1169-1175.
Copyright © 1998 by The American Association of Immunologists

Characterization of a Novel Bax-Associated Protein Expressed in Hemopoietic Tissues and Regulated During Thymocyte Apoptosis1

Huiling He2,*, Pamela A. Hershberger3,* and Susan A. McCarthy4,*,{dagger}

Departments of * Surgery and {dagger} Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213

Members of the Bcl-2 protein family have been implicated as critical intracellular regulators of apoptosis. Most studies of this protein family have utilized transformed and/or transfected cell lines expressing high levels of these proteins. In the current study, we have analyzed normal murine lymphoid cells and tissues and have detected a previously unreported protein of approximately 16 kDa recognized by an anti-Bax Ab. This 16-kDa protein is abundant in hemopoietic tissues of both wild-type and Bax knock-out mice, it can heterodimerize with Bax in normal lymphocytes, and it is dramatically down-modulated in thymocytes in response to apoptotic stimuli. These results suggest that this protein may have antiapoptotic activity and may participate in the regulation of apoptosis in normal lymphocytes.




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Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory factor during the G0 to S phase transition
PNAS, September 15, 1998; 95(19): 11095 - 11100.
[Abstract] [Full Text] [PDF]




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