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Papers In Press, published online ahead of print October 10, 2002
J. Biol. Chem, 10.1074/jbc.M209613200
Submitted on September 19, 2002
Revised on October 8, 2002
Accepted on October 10, 2002

The novel presenilin-1-associated protein (PSAP) is a pro-apoptotic mitochondrial protein

Xuemin Xu, Yong-chang Shi, Wei Gao, Guozhang Mao, Guojun Zhao, Sudesh Agrawal, Guy M. Chisolm, Dexin Sui, and Mei-Zhen Cui

Department of Pathology, University of Tennessee, Knoxville, TN 37996

Corresponding Author: xmx{at}utk.edu

Recent studies have suggested a possible role for presenilin proteins in apoptotic cell death observed in Alzheimer’s disease. The mechanism by which presenilin proteins regulate apoptotic cell death is not well understood. Using the yeast two-hybrid system, we previously isolated a novel protein, PSAP (presenilin-associated protein) that specifically interacts with the C-terminus of presenilin 1(PS1), but not presenilin 2 (PS2). Here we report that PSAP is a mitochondrial resident protein sharing homology with mitochondrial carrier protein. PSAP was detected in a mitochondria-enriched fraction and PSAP immunofluorescence was present in a punctate pattern that colocalized with a mitochondrial marker. More interestingly, overexpression of PSAP caused apoptotic death. PSAP-induced apoptosis was documented using multiple independent approaches, including membrane blebbing, chromosome condensation and fragmentation, DNA laddering, cleavage of the death substrate poly(ADP-ribose) polymerase, and flow cytometry. PSAP-induced cell death was accompanied by cytochrome c release from mitochondria and caspase-3 activation. Moreover, the general caspase inhibitor z-VAD-fmk, which blocked cell death, did not block the release of cytochrome c from mitochondria caused by overexpression of PSAP, indicating that PSAP-induced cytochrome c release was independent of caspase activity. The mitochondrial localization and proapoptotic activity of PSAP suggest that it is an important regulator of apoptosis.


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