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• W2009587796 abstract "Several observations support the hypothesis that pathogenetic mechanisms of β amyloid formation in Alzheimer's disease may involve alterations in amyloid precursor protein (APP) gene expression. In this regard, molecular dissection of the APP gene transcriptional regulation is of primary importance. We report evidence that members of the family of transcription factors NFκB/Rel can specifically recognize two identical sequences located in the 5′-regulatory region of APP. These sequences, which we refer to as APPκB sites, interact preferentially with p50-containing members of the family. In particular, p50 homodimers and p50/p65 and p50/c-Rel heterodimers act as transcriptional activators at the APPκB site. Finally, the nuclear complex specifically binding to the APPκB sites proves to be an integral part of neurons and lymphocytes. Several observations support the hypothesis that pathogenetic mechanisms of β amyloid formation in Alzheimer's disease may involve alterations in amyloid precursor protein (APP) gene expression. In this regard, molecular dissection of the APP gene transcriptional regulation is of primary importance. We report evidence that members of the family of transcription factors NFκB/Rel can specifically recognize two identical sequences located in the 5′-regulatory region of APP. These sequences, which we refer to as APPκB sites, interact preferentially with p50-containing members of the family. In particular, p50 homodimers and p50/p65 and p50/c-Rel heterodimers act as transcriptional activators at the APPκB site. Finally, the nuclear complex specifically binding to the APPκB sites proves to be an integral part of neurons and lymphocytes." @default.
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• W2009587796 date "1995-11-01" @default.
• W2009587796 modified "2023-10-13" @default.
• W2009587796 title "Identification and Characterization of a κB/Rel Binding Site in the Regulatory Region of the Amyloid Precursor Protein Gene" @default.
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• W2009587796 doi "https://doi.org/10.1074/jbc.270.45.26774" @default.
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