Abstract
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.
MeSH terms
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Alzheimer Disease / physiopathology
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Cell Line
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Cloning, Molecular
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HeLa Cells
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Humans
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In Situ Nick-End Labeling
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Lymphocytes
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Membrane Proteins / chemistry*
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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Presenilin-1
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Protein Binding
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Proto-Oncogene Proteins c-bcl-2 / chemistry*
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Proto-Oncogene Proteins c-bcl-2 / isolation & purification
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Proto-Oncogene Proteins c-bcl-2 / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Reverse Transcriptase Polymerase Chain Reaction
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Staurosporine / pharmacology
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Tumor Cells, Cultured
Substances
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Membrane Proteins
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PSEN1 protein, human
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Presenilin-1
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Proto-Oncogene Proteins c-bcl-2
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Recombinant Proteins
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Staurosporine