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PMID: 1625800 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid.

Neuroscience letters ·Vol. 135 ·No. 2 ·1992-02-03 ·Pages 235-8

Wisniewski T, Frangione B

Abstract

Many biochemically diverse proteins can give rise to amyloid fibrils; however, they are all accompanied by P component and glucosaminoglycans. With antibodies specific to apolipoprotein E (apo E) we used immunohistochemical techniques to test for the presence of this protein in both cerebral and systemic amyloid. We found apo E immunoreactivity in all tested types of cerebral and systemic amyloid. In amyloid deposits apo E P, component and glucosaminoglycans may be acting as 'pathological molecular chaperones'. The latter we define as a group of unrelated proteins that induce beta-pleated conformation in amyloidogenic polypeptides.

MeSH Terms
Amyloid/metabolism Apolipoproteins E/cerebrospinal fluid,immunology,metabolism Brain Chemistry/physiology Glycosaminoglycans/metabolism Humans Microscopy, Immunoelectron Nervous System Diseases/metabolism,pathology Paraffin Embedding Serum Amyloid P-Component/metabolism
Chemicals
Amyloid Apolipoproteins E Glycosaminoglycans Serum Amyloid P-Component
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wisniewski T
Department of Pathology, New York University Medical Center, New York 10016.
Frangione B
Article Info
Journal
Neuroscience letters
Abbr.
Neurosci Lett
ISSN
0304-3940
Published
1992-02-03
Pages
235-8
Language
English
Region
Ireland
NLM ID
7600130
Subset
IM
Grants
NIA NIH HHS · AG 08721 · United States
NIAMS NIH HHS · AR 02594 · United States
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