期刊
WIENER MEDIZINISCHE WOCHENSCHRIFT
卷 161, 期 9-10, 页码 274-276出版社
SPRINGER WIEN
DOI: 10.1007/s10354-011-0887-5
关键词
Apoptosis; amyloid A beta; peptides; interactions; eucaryotic porins
Human type-1 porin/VDAC (voltage-dependent anion channel) carries a GxxxG motif in its N-terminal part, traversing the beta-barrel, while the Alzheimer. s disease (AD) rele-corresponding motifs close to their C-terminus. GxxxG motifs are established as aggregation/membrane perturbation motifs. These peptide primary structure data support a proposal I recently made on the basis of a synopsis of recent literature. Accordingly, amyloid Ab, cut from APP by beta-secretase BACE1 and gamma-secretase, has been insinuated to induce Alzheimer. s disease via apoptosis by opening type-1 porin/VDAC in cell membranes of hypometabolic neuronal cells. Considering the ubiquitous expression modus of APP, beta-and gamma-secretases and type-1 VDAC/eukaryotic porin a basic model of apoptosis might be given.
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