Allsop, D and Wong, C W and Ikeda, S and Landon, M and Kidd, M and Glenner, G G (1988) Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease. Proceedings of the National Academy of Sciences, 85 (8). pp. 2790-2794. ISSN 0027-8424Full text not available from this repository.
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 gland. 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.
|Journal or Publication Title:||Proceedings of the National Academy of Sciences|
|Uncontrolled Keywords:||Adrenal Glands ; Alzheimer Disease ; Amyloid ; Amyloid beta-Peptides ; Antibodies, Monoclonal ; Humans ; Islets of Langerhans ; Ligands ; Oligopeptides ; Peptide Fragments ; Protein Precursors|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||01 Nov 2011 16:12|
|Last Modified:||13 Oct 2016 02:36|
Actions (login required)