Clinical significance of the glutathione-conjugating system. [1983](IR91)

Clinical significance of the glutathione-conjugating system. [1983](IR91)

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Clinical significance of the glutathione-conjugating system.

http://www.ncbi.nlm.nih.gov/pubmed/6338534
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Pharmacol Res Commun. 1983 Jan;15(1):1-13.
Clinical significance of the glutathione-conjugating system.
Siegers CP, Younes M.

Abstract
Glutathione displays important functions in living cells of many species, human included. Apart from its direct antioxidative activity, which supports the maintenance of the reduced state of proteinthiols, and its possible role in amino acid transport across membranes, it appears to exert several detoxification functions. These include the conjugation of electrophilic compounds and the reduction of H2O2 and lipid hydroperoxides. Disorders in GSH synthesis and metabolism are known and produce hemolysis (溶血; 紅血球溶解) in the first place. Little data exist concerning GSH and the GSH-dependent enzymes involved in its various functions in normal and diseased human tissues. The aim of this review is to stimulate research in this area.

PMID: 6338534 [PubMed - indexed for MEDLINE]
Publication Types, MeSH Terms, Substances
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(Memo Item created on June 11, 2011 03:43 PM)
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electrophilic
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electrophilic
親電子的; 吸電子的

In chemistry, an electrophile (literally electron-lover) is a reagent attracted to electrons that participates in a chemical reaction by accepting an electron pair in order to bond to a nucleophile. Because electrophiles accept electrons, they are Lewis acids (see acid-base reaction theories).
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Glutathione and GSH-dependent enzymes in the human gastric mucosa [1984](IR92)

Glutathione and GSH-dependent enzymes in the human gastric mucosa [1984](IR92)

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Glutathione and GSH-dependent enzymes in the human gastric mucosa [1984](IR92)

http://www.springerlink.com/content/u521475854l70rqk/
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BIOMEDICAL AND LIFE SCIENCES
JOURNAL OF MOLECULAR MEDICINE
Volume 62, Number 4, 183-186, DOI: 10.1007/BF01731642
ORIGINALIEN
Glutathione and GSH-dependent enzymes in the human gastric mucosa
R. Hoppenkamps, E. Thies, M. Younes and C. -P. Siegers

Abstract
The -glutamyl-transferase activity, the total glutathione content, the GSH-peroxidase activity, and the GSH S-transferase activity using an aryl substrate were estimated in the S9 fraction of gastric biopsy specimens taken from patients with normal stomach morphology (n=24), acute gastritis (n=15), chronic-atrophic gastritis (n=10), gastric ulcer (n=9), and carcinoma of the stomach (n=12). The total glutathione content of normal gastric mucosal specimens was significantly higher than that of human liver biopsy specimens, whereas the GSH-peroxidase and the GSH S-aryltransferase activities were much lower than those found in the liver. Specimens of gastric ulcer had significantly lower enzyme activities of GSH-peroxidase and GSH-aryltransferase, whereas gastric cancer tissue had significantly lower concentrations of total glutathione. The intraindividual comparison of tumorous and non-tumorous tissue showed a consistent decrease of total glutathione as well as of GSH-aryltransferase activity in carcinomatous tissue.

Key words  Glutathione - GSH-peroxidase - GSH S-aryltransferase - Human gastric mucosa - Gastric carcinoma

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Regulation of neuronal glutathione synthesis. [2008](IR91)

Regulation of neuronal glutathione synthesis. [2008](IR91)

Regulation of neuronal glutathione synthesis.
http://www.ncbi.nlm.nih.gov/pubmed/19008644

J Pharmacol Sci. 2008 Nov;108(3):227-38. Epub 2008 Nov 13.

Regulation of neuronal glutathione synthesis.
Aoyama K, Watabe M, Nakaki T.

Department of Pharmacology, Teikyo University School of Medicine, Itabashi, Tokyo, Japan.

Abstract
The brain is among the major organs generating large amounts of reactive oxygen species and is especially susceptible to oxidative stress. Glutathione (GSH) plays critical roles as an antioxidant, enzyme cofactor, cysteine storage form, the major redox buffer, and a neuromodulator in the central nervous system. GSH deficiency has been implicated in neurodegenerative diseases. GSH is a tripeptide comprised of glutamate, cysteine, and glycine. Cysteine is the rate-limiting substrate for GSH synthesis within neurons. Most neuronal cysteine uptake is mediated by sodium-dependent excitatory amino acid transporter (EAAT) systems, known as excitatory amino acid carrier 1 (EAAC1). Previous studies demonstrated EAAT is vulnerable to oxidative stress, leading to impaired function. A recent study found EAAC1-deficient mice to have decreased brain GSH levels and increased susceptibility to oxidative stress. The function of EAAC1 is also regulated by glutamate transporter associated protein 3-18. This review focuses on the mechanisms underlying GSH synthesis, especially those related to neuronal cysteine transport via EAAC1, as well as on the importance of GSH functions against oxidative stress.

PMID: 19008644 [PubMed - indexed for MEDLINE] Free full text