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[Cancer Research 59, 533-537, February 1, 1999]
© 1999 American Association for Cancer Research
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[Cancer Research 59, 533-537, February 1, 1999]
© 1999 American Association for Cancer Research

Advances in Brief

BNIP3{alpha}

A Human Homolog of Mitochondrial Proapoptotic Protein BNIP31

Motoaki Yasuda2, Jia-wen Han2, Cheryl A. Dionne, Janice M. Boyd and G. Chinnadurai3

Institute for Molecular Virology, St. Louis University Medical Center, St. Louis, Missouri 63110 [M. Y., J. M. B., G. C.] and Apoptosis Technology, Inc., Cambridge, Massachusetts 02139 [J-w. H., C. A. D.]

Apoptosis is regulated by interaction of viral and cellular BCL-2 family antiapoptotic proteins with various pro-apoptotic proteins, several of which are also members of the BCL-2 family. Cellular protein BNIP3 is a BCL-2 family proapoptotic protein that interacts with viral antiapoptosis proteins such as adenoviruses E1B-19K and EBV-BHRF1 and cellular antiapoptosis proteins such as BCL-2 and BCL-xL. Database searches indicate that the human genome encodes an open reading frame for a protein, BNIP3{alpha}, that shares substantial homology with BNIP3. The BNIP3{alpha} open reading frame encodes a protein of 219 amino acids that contains a conserved BH3 domain and a COOH-terminal trans-membrane domain, characteristic of several BCL-2 family proapoptotic proteins. BNIP3{alpha} interacts with viral antiapoptosis protein E1B-19K and cellular antiapoptosis proteins BCL-2 and BCL-xL. Overexpression of BNIP3{alpha} in transfected cells results in apoptosis and suppresses the antiapoptosis activity of E1B-19K and BCL-xL. Like BNIP3, BNIP3{alpha} seems to be predominantly localized in mitochondria. These results suggest that BNIP3{alpha} is a structural and functional homologue of BNIP3. BNIP3 and BNIP3{alpha} seem to be the first examples of homologues among the various human proapoptotic proteins. Northern blot analysis reveals that BNIP3{alpha} is expressed ubiquitously in most human tissues. In contrast, BNIP3 is expressed well in several human tissues and less abundantly in certain tissues such as placenta and lung. These results suggest that although BNIP3 and BNIP3{alpha} may promote apoptosis simultaneously in most human tissues, BNIP3{alpha} may play a more universal role.




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Copyright © 1999 by the American Association for Cancer Research.