Lancaster EPrints

Evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer's disease

Allsop, D and Ikeda, S and Glenner, G G (1989) Evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer's disease. Progress in clinical and biological research, 317. pp. 893-902. ISSN 0361-7742

Full text not available from this repository.

Abstract

A monoclonal antibody to a synthetic peptide consisting of residues 8-17 of amyloid beta-protein was used in immunohistochemical studies to reveal binding sites for this peptide in cytoplasmic vesicles in cells of the adrenal zona reticularis and the islets of Langerhans of the pancreas. These binding sites showed some specificity for this peptide and so may represent a membrane receptor. These results suggest that the membrane bound beta-protein precursor may be processed by limited extracellular proteolysis to release a peptide ligand containing the 8-17 sequence. It has been reported recently that the core protein of a heparin sulphate proteoglycan (HSPG) secreted by PC12 cells shows some homology with the beta-protein precursor. This suggests that the binding sites might be due to the presence of a HSPG core protein receptor. Further studies should be carried out to find out if receptors to beta-protein peptides are present in brain tissue, since these might play a role in the catabolism of the beta-protein precursor, and in the formation of cerebral amyloid in Alzheimer's disease (AD).

Item Type: Article
Journal or Publication Title: Progress in clinical and biological research
Uncontrolled Keywords: Alzheimer Disease ; Amyloid ; Amyloid beta-Protein Precursor ; Binding Sites ; Humans ; Ligands ; Protein Precursors
Subjects:
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 50866
Deposited By: ep_importer_pure
Deposited On: 08 Nov 2011 11:37
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 19:44
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/50866

Actions (login required)

View Item