PMID: 9546365Apr 18, 1998Paper

Accelerated methylmercury elimination in gamma-glutamyl transpeptidase-deficient mice

The American Journal of Pathology
N BallatoriM W Lieberman

Abstract

The disposition and toxicity of methylmercury, a ubiquitous environmental pollutant, is modulated by binding to the endogenous tripeptide glutathione (GSH) and metabolism of the resulting methylmercury-glutathione complex by the ectoproteins gamma-glutamyl transpeptidase (GGT) and dipeptidase. To evaluate the role of GGT in the whole-body disposition of methylmercury, we compared the elimination of [203Hg]methylmercury in GGT-deficient mice with that in wild-type mice and mice heterozygous for this deficiency. The effects of N-acetylcysteine (NAC), a drug used to maintain the cysteine and GSH levels of GGT-deficient mice, were also examined. Female mice were treated with either 0.5 or 25 micromol of CH3 203HgCl/kg body weight, in the presence and absence of 10 mg/ml NAC in the drinking water. There were no differences in methylmercury excretion between the wild-type and heterozygous mice; however, the GGT-deficient mice excreted methylmercury more rapidly at both dose levels. Wild-type and heterozygous mice excreted from 11 to 24% of the dose in the first 48 hours, whereas the GGT-deficient mice excreted 55 to 66% of the dose, with most of the methylmercury being excreted in urine. Urinary methylmercury excretion was further ac...Continue Reading

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