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J Biol Chem, Vol. 274, Issue 43, 30764-30769, October 22, 1999

Presenilin 1 Protein Directly Interacts with Bcl-2

Antonella AlbericiDagger , Daniele MorattoDagger , Luisa BenussiDagger , Laura GaspariniDagger , Roberta GhidoniDagger , Luisa Benerini Gatta, Dario Finazzi, Giovanni Battista FrisoniDagger , Marco Trabucchiparallel , John H. Growdon**, Roger M. NitschDagger Dagger , and Giuliano BinettiDagger

From the Dagger  Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) Centro S. Giovanni di Dio, Neurobiology Laboratory, Alzheimer's Disease Unit, Via Pilastroni 4, 25123 Brescia, Italy, the  Institute of Chemistry, Medical School, University of Brescia, 25124 Brescia, Italy, the parallel  Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, 00154 Rome, Italy, the Dagger Dagger  Department of Psychiatry Research, University of Zurich, CH-8091 Zurich, Switzerland, and the ** Department of Neurology, Harvard Medical School, Boston, Massachusetts 02114-3139

Presenilin proteins are involved in familial Alzheimer's disease, a neurodegenerative disorder characterized by massive death of neurons. We describe a direct interaction between presenilin 1 (PS1) and Bcl-2, a key factor in the regulation of apoptosis, by yeast two-hybrid interaction system, by co-immunoprecipitation, and by cross-linking experiments. Our data show that PS1 and Bcl-2 assemble into a macromolecular complex, and that they are released from this complex in response to an apoptotic stimulus induced by staurosporine. The results support the idea of cross-talk between these two proteins during apoptosis.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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