ABSTRACT
BACKGROUND AND AIMS: The C677T polymorphism of 5,10 methylenetetrahydrofolate reductase (MTHFR) gene has been associated with hypertension and coronary artery disease in several populations worldwide, but results are still controversial. The aim of this study was to examine the possible association of C677T polymorphism with ST-elevation myocardial infarction (STEMI) in young Mexican subjects. METHODS: In a case-control study, 167 unrelated patients < or = 45 years of age with diagnosis of STEMI who were admitted to a cardiovascular intense care unit and 167 unrelated controls subjects matched by age and gender were recruited from January 2006 and June 2009. The C677T polymorphism was determined in all participants by a polymerase chain reaction-restriction fragment length polymorphism assay (PCR-RFLP). RESULTS: There was no significant difference in the genotype distribution between groups (p = 0.69) or allele frequency (p = 0.40). There were independent factors for STEMI: smoking (OR 4.9, 95% CI 3.0-8.1, p = 0.001), hypertension (OR 1.8, 95% CI 1.0-3.3, p = 0.03), family history of atherothrombotic disease (OR 2.3, 95% CI 2.0-4.6, p = 0.02), and dyslipidemia (OR 3.2, 95% CI 1.8-5.6, p <0.001). Diabetes mellitus did not represent an independent risk factor for STEMI (OR 1.2, 95% CI 0.2-2.2, p = 0.82). CONCLUSIONS: The TT genotype from the C677T of 5,10 MTHFR gene is not an independent risk factor for STEMI in the Mexican population. However, more studies are needed to determine the possible "protective effect" of the C677T polymorphism in our population.
Subject(s)
Methylenetetrahydrofolate Reductase (NADPH2)/genetics , Myocardial Infarction/genetics , Polymorphism, Genetic , Adult , Base Sequence , Case-Control Studies , DNA Primers , Female , Gene Frequency , Humans , Male , Mexico , Myocardial Infarction/enzymology , Polymerase Chain Reaction , Polymorphism, Restriction Fragment LengthABSTRACT
The intracellular proteinase pumAi in Ustilago maydis has been associated with yeast-mycelium dimorphic transition. The proteinase was purified from a cell-free extract by ammonium sulfate fractionation and chromatographic steps including hydrophobic interactions on a Phenyl Superose column, ion exchange on a Mono Q column, and gel filtration on Superose 12 columns. The enzyme has a mass of 35.3-36.6 kDa, a pH and temperature optimum of 4.0 and 40 degrees C, respectively, and a pI of 5.5. The enzyme degraded hemoglobin, gelatin, albumin, and casein, but not collagen, and the enzymatic activity was strongly inhibited by pepstatin A, an aspartyl proteinase-specific inhibitor. The biochemical characteristics of pumAi are similar to other fungal intracellular aspartyl proteinases, however, this is the first biochemical characterization of a basidiomycete proteinase probably associated with dimorphic yeast-mycelium transition.
