1997年3月
Deletion of an endosomal/lysosomal targeting signal promotes the secretion of Alzheimer's disease amyloid precursor protein (APP)
JOURNAL OF BIOCHEMISTRY
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- 巻
- 121
- 号
- 3
- 開始ページ
- 585
- 終了ページ
- 590
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- JAPANESE BIOCHEMICAL SOC
Alzheimer's disease amyloid precursor protein (APP) generates a beta-amyloid protein (A beta) that is a main component of the senile plaques found in the brains of Alzheimer's disease patients, APP is thought to undergo proteolysis via two different pathways, the amyloidogenic pathway which produces Ap, and the non-amyloidogenic pathway which releases a large N-terminal fragment into the medium, The proteases that mediate these processes remain unidentified, The physiological function of APP is not clear yet, Therefore, the cytoplasmic region of APP has attracted much interest, because this region is highly conserved among species, and members of the amyloid precursor-like protein (APLP) family, Several potentially functional sequences exist in the region, including signal sequences for protein sorting and a G(0)-protein binding sequence, We constructed two mutants, 695 Delta NPTY and 695 Delta GYEN. They lack potential endosome/lysosome targeting signals, NPTY and GY, in the cytoplasmic domain of APP695, respectively, The mutant APPs had longer half-lives and were secreted more easily into the medium than the wild type, suggesting that these sequences are important for the secretion and metabolism of APP.
- リンク情報
- ID情報
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- ISSN : 0021-924X
- CiNii Articles ID : 10005456378
- Web of Science ID : WOS:A1997WN87800024