IMMUNOHISTOCHEMICAL EVIDENCE FOR THE DERIVATION OF A PEPTIDE LIGAND FROM THE AMYLOID BETA-PROTEIN PRECURSOR OF ALZHEIMER-DISEASE
IMMUNOHISTOCHEMICAL EVIDENCE FOR THE DERIVATION OF A PEPTIDE LIGAND FROM THE AMYLOID BETA-PROTEIN PRECURSOR OF ALZHEIMER-DISEASE
复制标题
DOI：
10.1073/pnas.85.8.2790
复制
发表时间：
1988-04-01
影响因子：
11.1
通讯作者：
GLENNER, GG
中科院分区：
文献类型：
--
作者：
ALLSOP, D;WONG, CW;GLENNER, GG
A monoclonal antibody to a synthetic peptide consisting of residues 8-17 of the amyloid .beta. protein of Alzheimer disease was used in immunohistochemical studies to reveal binding sites for this peptide in vesicular elements in the islets of Langerhans of the pancreas and the zona reticularis of the adrenal glands. These binding sites may represent a specific membrane receptor. These results, together with similarities in structural features between the precursors for epidermal growth factor and .beta. protein, suggest that the .beta.-protein precursor may be processed to release an active peptide ligand rather than acting as a membrane receptor. In Alzheimer disease, abnormal processing of this active peptide precursor may result in the deposition of .beta.-protein amyloid fibrils in the brain.
