Polymorphisms in the GSTT1 and GSTM1 genes are associated with increased risk of preeclampsia in the Mexican mestizo population.

Preeclampsia is a pregnancy-specific disorder in humans and a major cause of maternal and neonatal morbidity and mortality. Increasing evidence suggests that oxidative stress plays an important role in the pathogenesis of preeclampsia. The aim of this study was to investigate the relationship between null alleles of the glutathione S-transferases (GST) M1 and T1 genes and the risk of preeclampsia. This case-control study involved 112 preeclamptic and 233 normoevolutive pregnant women. The null polymorphisms were genotyped by multiplex polymerase chain reaction (PCR). Our results showed an increased risk of preeclampsia in patients with the GSTT1 null genotype [odds ratio (OR) = 2.21; 95% confidence interval (CI) = 1.14-4.27; P = 0.018]. Our data further showed that a combination of deletion genotypes of the GSTM1 and GSTT1 genes conferred an even higher risk of preeclampsia (OR = 4.56, 95%CI = 1.59-13.09; P = 0.005). Our results provide the first evidence suggesting that a GSTT1 null polymorphism might be associated with preeclampsia in the Mexican mestizo population, and that this risk increases with the combination of both GSTT1 and GSTM1 null polymorphisms.

Temporal secretion of a multicellulolytic system in Myxobacter sp. AL-1. Molecular cloning and heterologous expression of cel9 encoding a modular endocellulase clustered in an operon with cel48, an exocellobiohydrolase gene.

The Gram-negative soil micro-organism Myxobacter sp. AL-1 possesses at least five extracellular cellulases, the production of which is regulated by the growth cycle. We cloned the complete gene for one of these cellulases, termed cel9, which encoded a 67-kDa modular family 9 endoglycohydrolase, which was produced during the stationary phase of growth and was strongly enhanced by avicel. The predicted product of cel9 matches the structural architecture of family 9 cellulases such as Thermonospora fusca endo/exocellulase E4. Cel9 protein was synthesized in Escherichia coli from a multicopy plasmid and in Bacillus subtilis from the isopropyl thiogalactoside-inducible Pspac promoter and was purified from the culture medium. Thermal stability, optimum pH and temperature dependence of Cel9 were similar when expressed from either source, and were indistinguishable from related cellulases produced by thermophilic bacteria. Downstream from cel9 was found a partial ORF, designated cel48, the deduced product of which was highly similar to bacterial exocellobiohydrolases and processive endoglucanases belonging to family 48 of the glycosyl hydrolases. The cel9 and cel48 genes appear to be arranged as part of an operon.