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PMID: 15950321 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis.

Neurobiology of aging ·Vol. 27 ·No. 7 ·2006-07-00 ·Pages 918-25

Sultana R, Boyd-Kimball D, Poon HF, Cai J, Pierce WM, Klein JB, Markesbery WR, Zhou XZ, Lu KP, Butterfield DA

Abstract

Alzheimer disease (AD) is characterized neuropathologically by intracellular neurofibrillary tangles (NFT) and of extracellular senile plaques (SP), the central core of which is amyloid beta-peptide (Abeta) derived from amyloid precursor protein (APP), a transmembrane protein. AD brain has been reported to be under oxidative stress that may play an important role in the pathogenesis and progression of AD. The present proteomics study is focused on identification of a specific target of protein oxidation in AD hippocampus that has relevance to the role of oxidative stress in AD. Here, we report that the protein, Pin1, is significantly down-regulated and oxidized in AD hippocampus. The identity of Pin1 was confirmed immunochemically. Analysis of Pin1 activity in AD brain and separately as oxidized pure Pin1 demonstrated that oxidation of Pin1 led to loss of activity. Pin1 has been implicated in multiple aspects of cell cycle regulation and dephosphorylation of tau protein as well as in AD. The in vivo oxidative modification of Pin1 as found by proteomics in AD hippocampus in the present study suggests that oxidative modification may be related to the known loss of Pin1 isomerase activity that could be crucial in AD neurofibrillary pathology. Taken together, these results provide evidence supporting a direct link between oxidative damage to neuronal Pin1 and the pathobiology of AD.

MeSH Terms
Aged, 80 and over Alzheimer Disease/metabolism,physiopathology Down-Regulation/physiology Female Hippocampus/metabolism,physiopathology Humans Immunohistochemistry Male NIMA-Interacting Peptidylprolyl Isomerase Neurofibrillary Tangles/metabolism Oxidation-Reduction Oxidative Stress/physiology Peptidylprolyl Isomerase/metabolism Phosphorylation Protein Processing, Post-Translational/physiology Proteomics tau Proteins/metabolism
Chemicals
NIMA-Interacting Peptidylprolyl Isomerase tau Proteins PIN1 protein, human Peptidylprolyl Isomerase
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Sultana Rukhsana
Department of Chemistry, University of Kentucky, Lexington, KY 40506, USA.
Boyd-Kimball Debra
Poon H Fai
Cai Jain
Pierce William M
Klein Jon B
Markesbery William R
Zhou Xiao Zhen
Lu Kun Ping
Butterfield D Allan
Article Info
Journal
Neurobiology of aging
Abbr.
Neurobiol Aging
ISSN
0197-4580
Published
2006-07-00
Epub
2005-00-13
Pages
918-25
Language
English
Region
United States
NLM ID
8100437
Subset
IM
Grants
NIA NIH HHS · AG-05119 · United States
NIA NIH HHS · AG-10836 · United States
NIA NIH HHS · AG17870 · United States
NIA NIH HHS · AG22082 · United States
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