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

Biomedical and Life Sciences

Keywords

Alzheimer Disease, Amyloid, Amyloid beta-Protein Precursor, Binding Sites, Humans, Ligands, Protein Precursors

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

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Evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer's disease. / Allsop, D; Ikeda, S; Glenner, G G.
In: Progress in Clinical and Biological Research, Vol. 317, 1989, p. 893-902.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{66ff51ed7e234b79991d36227082583b,

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

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).",

keywords = "Alzheimer Disease, Amyloid, Amyloid beta-Protein Precursor, Binding Sites, Humans, Ligands, Protein Precursors",

author = "D Allsop and S Ikeda and Glenner, {G G}",

year = "1989",

language = "English",

volume = "317",

pages = "893--902",

journal = "Progress in Clinical and Biological Research",

issn = "0361-7742",

publisher = "John Wiley and Sons Inc.",

}

RIS

TY - JOUR

T1 - Evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer's disease

AU - Allsop, D

AU - Ikeda, S

AU - Glenner, G G

PY - 1989

Y1 - 1989

N2 - 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).

AB - 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).

KW - Alzheimer Disease

KW - Amyloid

KW - Amyloid beta-Protein Precursor

KW - Binding Sites

KW - Humans

KW - Ligands

KW - Protein Precursors

M3 - Journal article

C2 - 2513585

VL - 317

SP - 893

EP - 902

JO - Progress in Clinical and Biological Research

JF - Progress in Clinical and Biological Research

SN - 0361-7742

ER -

Research

Keywords