ALZHEIMERS BETA-AMYLOID PEPTIDE SPECIFICALLY INTERACTS WITH AND IS DEGRADED BY INSULIN DEGRADING ENZYME
ALZHEIMERS BETA-AMYLOID PEPTIDE SPECIFICALLY INTERACTS WITH AND IS DEGRADED BY INSULIN DEGRADING ENZYME
复制标题
DOI：
10.1016/0014-5793(94)00387-4
复制
发表时间：
1994-05-23
期刊：
影响因子：
3.5
通讯作者：
GOTO, S
中科院分区：
文献类型：
--
作者：
KUROCHKIN, IV;GOTO, S
β-淀粉样肽（β A）的脑沉积是阿尔茨海默病的标志。β A的浓度在淀粉样蛋白沉积的速率中起着关键作用。因此，鉴定参与β A加工的蛋白酶是相当重要的。I-125标记的合成β A与大鼠脑和肝脏胞质溶胶组分中M（r）= 110，000的单一蛋白质特异性交联。该蛋白被鉴定为胰岛素降解酶（IDE），因为110 kDa蛋白的标记被过量的胰岛素完全阻断，并且抗IDE单克隆抗体沉淀标记的蛋白。纯化的大鼠IDE有效地降解β A。
Cerebral deposition of beta-amyloid peptide (beta A) is a hallmark of Alzheimer's disease. Concentration of beta A could play a critical role in the rate of amyloid deposition. It is therefore of considerable importance to identify proteases involved in processing of beta A. I-125-labeled synthetic beta A specifically cross-linked to a single protein with M(r) = 110,000 in cytosol fractions from rat brain and liver. This protein was identified as insulin degrading enzyme (IDE) since the labeling of the 110 kDa protein was completely blocked by an excess of insulin, and anti-IDE monoclonal antibodies precipitated the labeled protein. Purified rat IDE effectively degraded beta A.