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Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease

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

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Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease. / Allsop, D; Wong, C W; Ikeda, S et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 8, 1988, p. 2790-2794.

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

Harvard

Allsop, D, Wong, CW, Ikeda, S, Landon, M, Kidd, M & Glenner, GG 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 of the United States of America, vol. 85, no. 8, pp. 2790-2794.

APA

Allsop, D., Wong, C. W., Ikeda, S., Landon, M., Kidd, M., & 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 of the United States of America, 85(8), 2790-2794.

Vancouver

Allsop D, Wong CW, Ikeda S, Landon M, Kidd M, Glenner GG. 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 of the United States of America. 1988;85(8):2790-2794.

Author

Allsop, D ; Wong, C W ; Ikeda, S et al. / Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease. In: Proceedings of the National Academy of Sciences of the United States of America. 1988 ; Vol. 85, No. 8. pp. 2790-2794.

Bibtex

@article{1e7d124310c44c9a8d1ddbac5c420faf,
title = "Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease",
abstract = "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.",
keywords = "Adrenal Glands, Alzheimer Disease, Amyloid, Amyloid beta-Peptides, Antibodies, Monoclonal, Humans, Islets of Langerhans, Ligands, Oligopeptides, Peptide Fragments, Protein Precursors",
author = "D Allsop and Wong, {C W} and S Ikeda and M Landon and M Kidd and Glenner, {G G}",
year = "1988",
language = "English",
volume = "85",
pages = "2790--2794",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "8",

}

RIS

TY - JOUR

T1 - Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid β-protein precursor of Alzheimer disease

AU - Allsop, D

AU - Wong, C W

AU - Ikeda, S

AU - Landon, M

AU - Kidd, M

AU - Glenner, G G

PY - 1988

Y1 - 1988

N2 - 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.

AB - 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.

KW - Adrenal Glands

KW - Alzheimer Disease

KW - Amyloid

KW - Amyloid beta-Peptides

KW - Antibodies, Monoclonal

KW - Humans

KW - Islets of Langerhans

KW - Ligands

KW - Oligopeptides

KW - Peptide Fragments

KW - Protein Precursors

M3 - Journal article

C2 - 3282239

VL - 85

SP - 2790

EP - 2794

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 8

ER -