Glutathione S-transferase hGSTM3 and ageing-associated neurodegeneration: Relationship to Alzheimer's disease

Tatyana L. Tchaikovskaya, Vadim Fraifeld, Tinatin Urphanishvili, John H. Andorfer, Peter Davies, Irving Listowsky

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Glutathione S-transferases (GSTs) are detoxification enzymes that can counter ageing-associated oxidative and chemical stresses. The transcript of a distinct subclass of human GSTs (hGSTM3) was shown by RNA blot analysis to be widely distributed in different regions of adult brain. HPLC profiles indicated that the hGSTM3 subunit was the second most abundant GST subunit in brain. Immunocytochemistry performed with hGSTM3-specific antisera, showed prominent staining of neuritic plaques, neurofibrillary tangles and microglia in sections of hippocampus obtained from patients with Alzheimer's disease. The staining pattern was distinct from that obtained with normal brains. Because hGSTM3 is rich in cysteine residues and readily undergoes S-glutathiolation reactions, deposition of this protein could originate from cross-links produced by oxidative stress.

Original languageEnglish (US)
Pages (from-to)309-315
Number of pages7
JournalMechanisms of Ageing and Development
Volume126
Issue number2
DOIs
StatePublished - Feb 2005

Fingerprint

Glutathione Transferase
Brain
Alzheimer Disease
Aging of materials
Oxidative Stress
Staining and Labeling
Detoxification
Neurofibrillary Tangles
Oxidative stress
Amyloid Plaques
Microglia
Cysteine
Immune Sera
Hippocampus
Immunohistochemistry
High Pressure Liquid Chromatography
RNA
Enzymes
Proteins

Keywords

  • Ageing
  • Alzheimer's disease
  • Brain
  • Glutathione S-transferases
  • hGSTM5 subunit
  • Microglia

ASJC Scopus subject areas

  • Aging
  • Biochemistry
  • Developmental Biology
  • Developmental Neuroscience

Cite this

Glutathione S-transferase hGSTM3 and ageing-associated neurodegeneration : Relationship to Alzheimer's disease. / Tchaikovskaya, Tatyana L.; Fraifeld, Vadim; Urphanishvili, Tinatin; Andorfer, John H.; Davies, Peter; Listowsky, Irving.

In: Mechanisms of Ageing and Development, Vol. 126, No. 2, 02.2005, p. 309-315.

Research output: Contribution to journalArticle

Tchaikovskaya, Tatyana L. ; Fraifeld, Vadim ; Urphanishvili, Tinatin ; Andorfer, John H. ; Davies, Peter ; Listowsky, Irving. / Glutathione S-transferase hGSTM3 and ageing-associated neurodegeneration : Relationship to Alzheimer's disease. In: Mechanisms of Ageing and Development. 2005 ; Vol. 126, No. 2. pp. 309-315.
@article{59cf3c9e4bbd48c78035e36745bd09e8,
title = "Glutathione S-transferase hGSTM3 and ageing-associated neurodegeneration: Relationship to Alzheimer's disease",
abstract = "Glutathione S-transferases (GSTs) are detoxification enzymes that can counter ageing-associated oxidative and chemical stresses. The transcript of a distinct subclass of human GSTs (hGSTM3) was shown by RNA blot analysis to be widely distributed in different regions of adult brain. HPLC profiles indicated that the hGSTM3 subunit was the second most abundant GST subunit in brain. Immunocytochemistry performed with hGSTM3-specific antisera, showed prominent staining of neuritic plaques, neurofibrillary tangles and microglia in sections of hippocampus obtained from patients with Alzheimer's disease. The staining pattern was distinct from that obtained with normal brains. Because hGSTM3 is rich in cysteine residues and readily undergoes S-glutathiolation reactions, deposition of this protein could originate from cross-links produced by oxidative stress.",
keywords = "Ageing, Alzheimer's disease, Brain, Glutathione S-transferases, hGSTM5 subunit, Microglia",
author = "Tchaikovskaya, {Tatyana L.} and Vadim Fraifeld and Tinatin Urphanishvili and Andorfer, {John H.} and Peter Davies and Irving Listowsky",
year = "2005",
month = "2",
doi = "10.1016/j.mad.2004.08.029",
language = "English (US)",
volume = "126",
pages = "309--315",
journal = "Mechanisms of Ageing and Development",
issn = "0047-6374",
publisher = "Elsevier Ireland Ltd",
number = "2",

}

TY - JOUR

T1 - Glutathione S-transferase hGSTM3 and ageing-associated neurodegeneration

T2 - Relationship to Alzheimer's disease

AU - Tchaikovskaya, Tatyana L.

AU - Fraifeld, Vadim

AU - Urphanishvili, Tinatin

AU - Andorfer, John H.

AU - Davies, Peter

AU - Listowsky, Irving

PY - 2005/2

Y1 - 2005/2

N2 - Glutathione S-transferases (GSTs) are detoxification enzymes that can counter ageing-associated oxidative and chemical stresses. The transcript of a distinct subclass of human GSTs (hGSTM3) was shown by RNA blot analysis to be widely distributed in different regions of adult brain. HPLC profiles indicated that the hGSTM3 subunit was the second most abundant GST subunit in brain. Immunocytochemistry performed with hGSTM3-specific antisera, showed prominent staining of neuritic plaques, neurofibrillary tangles and microglia in sections of hippocampus obtained from patients with Alzheimer's disease. The staining pattern was distinct from that obtained with normal brains. Because hGSTM3 is rich in cysteine residues and readily undergoes S-glutathiolation reactions, deposition of this protein could originate from cross-links produced by oxidative stress.

AB - Glutathione S-transferases (GSTs) are detoxification enzymes that can counter ageing-associated oxidative and chemical stresses. The transcript of a distinct subclass of human GSTs (hGSTM3) was shown by RNA blot analysis to be widely distributed in different regions of adult brain. HPLC profiles indicated that the hGSTM3 subunit was the second most abundant GST subunit in brain. Immunocytochemistry performed with hGSTM3-specific antisera, showed prominent staining of neuritic plaques, neurofibrillary tangles and microglia in sections of hippocampus obtained from patients with Alzheimer's disease. The staining pattern was distinct from that obtained with normal brains. Because hGSTM3 is rich in cysteine residues and readily undergoes S-glutathiolation reactions, deposition of this protein could originate from cross-links produced by oxidative stress.

KW - Ageing

KW - Alzheimer's disease

KW - Brain

KW - Glutathione S-transferases

KW - hGSTM5 subunit

KW - Microglia

UR - http://www.scopus.com/inward/record.url?scp=11144307948&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=11144307948&partnerID=8YFLogxK

U2 - 10.1016/j.mad.2004.08.029

DO - 10.1016/j.mad.2004.08.029

M3 - Article

C2 - 15621212

AN - SCOPUS:11144307948

VL - 126

SP - 309

EP - 315

JO - Mechanisms of Ageing and Development

JF - Mechanisms of Ageing and Development

SN - 0047-6374

IS - 2

ER -