GSTT1 and GSTM1 null variants in Mestizo and Amerindian populations from northwestern Mexico and a literature review.

Luz Elena Palma-Cano,Mauricio González-Ponce,Angélica Martínez-Hernández,Angel Licón-Trillo,Verónica Moreno-Brito,Ruth Lechuga-Valles,Everardo González-Rodríguez,Lorena Orozco,Irene Leal-Berumen,Miguel Cid,Emilio J Córdova

doi:10.1590/1678-4685-gmb-2016-0142

Luz Elena Palma-Cano, Mauricio González-Ponce + Show 9 more

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https://doi.org/10.1590/1678-4685-gmb-2016-0142

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Abstract

The GSTT1 and GSTM1 genes are key molecules in cellular detoxification. Null variants in these genes are associated with increase susceptibility to developing different types of cancers. The aim of this study was to determine the prevalence of GSTT1 and GSTM1 null genotypes in Mestizo and Amerindian individuals from the Northwestern region of Mexico, and to compare them with those reported worldwide. GSTT1 and GSTM1 null variants were genotyped by multiplex PCR in 211 Mestizos and 211 Amerindian individuals. Studies reporting on frequency of GSTT1 and GSTM1 null variants worldwide were identified by a PubMed search and their geographic distribution were analyzed. We found no significant differences in the frequency of the null genotype for GSTT1 and GSM1 genes between Mestizo and Amerindian individuals. Worldwide frequencies of the GSTT1 and GSTM1 null genotypes ranges from 0.10 to 0.51, and from 0.11 to 0.67, respectively. Interestingly, in most countries the frequency of the GSTT1 null genotype is common or frequent (76%), whereas the frequency of the GSMT1 null genotype is very frequent or extremely frequent (86%). Thus, ethnic-dependent differences in the prevalence of GSTT1 and GSTM1 null variants may influence the effect of environmental carcinogens in cancer risk.

Highlights

The family of the glutathione S-transferases (GSTs) is composed of enzymes that play an essential role in the cellular protection against a wide range of hazardous molecules, such as reactive oxygen species (ROS), xenobiotics and electrophilic compounds
We found no significant difference in the frequencies of the wild type or of null genotype for GSTT1 and GSTM1 between Mestizo and Tarahumara individuals
The frequency of the GSTT1 null genotype observed in the Mestizo individuals included in our study was similar to those previously reported in Mexican-Mestizos from the northeastern and central regions of the country (0.11 vs. 0.10–0.13 and 0.12–0.15, respectively), as well as in one population from the Southeast (0.11 vs. 0.09)

Summary

Introduction

The family of the glutathione S-transferases (GSTs) is composed of enzymes that play an essential role in the cellular protection against a wide range of hazardous molecules, such as reactive oxygen species (ROS), xenobiotics and electrophilic compounds. GSTs catalyze the conjugation of reduced glutathione (GSH), the major antioxidant molecule in the cell, to a myriad of hazardous molecules, including carcinogens, drugs and xenobiotics. GSTs are able to detoxify noxious products of the cellular metabolism, such as reactive oxygen and nitrogen species through their glutathione peroxidase activity (Board and Menon, 2013; Galal et al, 2015). These enzymes are involved in cellular processes others than detoxification, including chaperone activities, regulation of kinase-mediated signal transduction and S-glutathionylation cycle (Pajaud et al, 2012; Klaus et al, 2013; Zhang et al, 2014a)

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