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

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

doi:10.1016/j.mad.2004.08.029

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

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

Radiation Oncology

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

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 language	English (US)
Pages (from-to)	309-315
Number of pages	7
Journal	Mechanisms of Ageing and Development
Volume	126
Issue number	2
DOIs	https://doi.org/10.1016/j.mad.2004.08.029
State	Published - Feb 2005

Keywords

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

ASJC Scopus subject areas

Aging
Developmental Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.mad.2004.08.029

Cite this

@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, Microglia, hGSTM5 subunit",

author = "Tatyana Tchaikovskaya and Vadim Fraifeld and Tinatin Urphanishvili and Andorfer, {John H.} and Peter Davies and Irving Listowsky",

note = "Funding Information: This work was supported by Grant Ca 42448 from the National Cancer Institute of NIH and the Atran foundation.",

year = "2005",

month = feb,

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

AU - Fraifeld, Vadim

AU - Urphanishvili, Tinatin

AU - Andorfer, John H.

AU - Davies, Peter

AU - Listowsky, Irving

N1 - Funding Information: This work was supported by Grant Ca 42448 from the National Cancer Institute of NIH and the Atran foundation.

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 - Microglia

KW - hGSTM5 subunit

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

SN - 0047-6374

VL - 126

SP - 309

EP - 315

JO - Mechanisms of Ageing and Development

JF - Mechanisms of Ageing and Development

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this