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PMID: 3121789 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Neuritic plaque amyloid in Alzheimer's disease is highly racemized.

Journal of neurochemistry ·Vol. 50 ·No. 1 ·1988-01-00 ·Pages 69-74

Shapira R, Austin GE, Mirra SS

Abstract

Neuritic plaque core amyloid protein in Alzheimer's disease brain tissue was investigated for the extent of amino acid racemization. Long-lived human proteins exhibit racemization of certain amino acids over the course of a human lifetime. Purified core amyloid was found to contain relatively large proportions of D-aspartate and D-serine, suggesting that neuritic plaque amyloid is derived from a long-lived precursor protein. Alternatively, racemization of protein amino acids may be abnormally accelerated in Alzheimer's disease.

MeSH Terms
Aged Alzheimer Disease/metabolism Amino Acids/analysis,metabolism Amyloid/analysis Amyloid beta-Peptides Aspartic Acid/analysis,metabolism Brain Chemistry Electrophoresis, Polyacrylamide Gel Female Humans Hydrolysis Isomerism Male Middle Aged Molecular Weight Protein Precursors/metabolism Racemases and Epimerases/metabolism Serine/analysis,metabolism
Chemicals
Amino Acids Amyloid Amyloid beta-Peptides Protein Precursors Aspartic Acid Serine Racemases and Epimerases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Shapira R
Department of Biochemistry, Veterans Administration Medical Center, Atlanta, Georgia.
Austin G E
Mirra S S
Article Info
Journal
Journal of neurochemistry
Abbr.
J Neurochem
ISSN
0022-3042
Published
1988-01-00
Pages
69-74
Language
English
Region
England
NLM ID
2985190R
Subset
IM
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