Caenorhabditis elegans gcs-1 confers resistance to arsenic-induced oxidative stress

Liao, V; Yu, CW

HERO ID

627325

Reference Type

Journal Article

Year

2005

Language

English

PMID

16333752

HERO ID 627325
In Press No
Year 2005
Title Caenorhabditis elegans gcs-1 confers resistance to arsenic-induced oxidative stress
Authors Liao, V; Yu, CW
Journal BioMetals
Volume 18
Issue 5
Page Numbers 519-528
Abstract Gamma-glutamylcysteine synthetase (gamma-GCS) catalyzes the first, rate-limiting step in the biosynthesis of glutathione (GSH). To evaluate the protective role of cellular GSH against arsenic-induced oxidative stress in Caenorhabditis elegans (C. elegans), we examined the effect of the C. elegans ortholog of GCS(h), gcs-1, in response to inorganic arsenic exposure. We have evaluated the responses of wild-type and gcs-1 mutant nematodes to both inorganic arsenite (As(III)) and arsenate (As(V)) ions and found that gcs-1 mutant nematodes are more sensitive to arsenic toxicity than that of wild-type animals. The amount of metal ion required to kill half of the population of worms falls in the order of wild-type/As(V)>gcs-1/As(V)> wild-type/As(III)>gcs-1/As(III). gcs-1 mutant nematodes also showed an earlier response to the exposure of As(III) and As(V) than that of wild-type animals. Pretreatment with GSH significantly raised the survival rate of gcs-1 mutant worms compared to As(III)- or As(V)-treated worms alone. These results indicate that GCS-1 is essential for the synthesis of intracellular GSH in C. elegans and consequently that the intracellular GSH status plays a critical role in protection of C. elegans from arsenic-induced oxidative stress.
Doi 10.1007/s10534-005-2996-3
Pmid 16333752
Wosid WOS:000233823500007
Is Certified Translation No
Dupe Override No
Comments |WOS:000233823500007
Is Public Yes
Language Text English
Keyword gamma-glutamylcysteine synthetase; glutathione; Caenorhabditis elegans; arsenic
Is Qa No