EVIDENCE THAT BETA-AMYLOID PROTEIN IN ALZHEIMERS-DISEASE IS NOT DERIVED BY NORMAL PROCESSING

被引：848
作者：
SISODIA, SS
KOO, EH
BEYREUTHER, K
UNTERBECK, A
PRICE, DL
机构：
[1] JOHNS HOPKINS UNIV, SCH MED, NEUROPATHOL LAB, BALTIMORE, MD 21205 USA
[2] JOHNS HOPKINS UNIV, SCH MED, DEPT NEUROL, BALTIMORE, MD 21205 USA
[3] JOHNS HOPKINS UNIV, SCH MED, DEPT NEUROSCI, BALTIMORE, MD 21205 USA
[4] UNIV HEIDELBERG, CTR MOLEC BIOL, W-6900 HEIDELBERG, GERMANY
来源：
SCIENCE | 1990年 / 248卷 / 4954期
关键词：
D O I：
10.1126/science.1691865
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The β-amyloid protein (β/A4), derived from a larger amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer's disease. APP is an integral membrane glycoprotein and is secreted as a carboxyl-terminal truncated molecule. APP cleavage, which is a membrane-associated event, occurred at a site located within the β/A4 region. This suggests that an intact amyloidogenic β/A4 fragment is not generated during normal APP catabolism. Therefore, an early event in amyloid formation may involve altered APP processing that results in the release and subsequent deposition of intact β/A4.
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收藏
页码：492 / 495
页数：4
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