Association between the severity of angiographic coronary artery disease and paraoxonase-1 promoter gene polymorphism T[-107] C in Iranian population

The oxidation of low-density lipoproteins and cell membrane lipids is believed to play an integral role in the development of fatty streak lesions, an initial step in coronary artery disease [CAD]. Paraoxonase-1 [PON1] is an enzyme associated with the high-density lipoprotein [HDL] particle. PON1 protects LDL from oxidative modification by hydrolyzing lipid peroxides, suggestive of a role for PON1 in the development of CAD. The present study tested the hypothesis that Paraoxonase-1 promoter polymorphism T[-107]C could be a risk factor for severity of CAD in Iranian population. Paraoxonase-1 promoter genotypes were determined in 300 consecutive subjects [> 40 years old] who underwent coronary angiography [150 subjects with >50% stenosis served as cases [CAD+] and 150 subjects with < 20% stenosis served as controls [CAD-]]. PON1 promoter genotypes were determined by PCR and BSTU1 restriction enzyme digestion. CAD+ Subjects did not show any significant differences in the distribution of PON1 promoter genotypes as compared to CAD- Subjects [P = 0.075]. However the analysis of PON1 promoter genotypes distribution showed a higher percentage of [-107] TT among CAD+ compared with CAD- [P = 0.027]. After controlling for other risk factors, the T[- 107]C polymorphism had interaction with age [P = 0.012], but did not show any interaction with other risk factors such as BMI, gender, smoking, diabetes, level of HDL-C, LDL-C, triglyceride and Total cholesterol. These data suggest that the TT genotype may represent a genetic risk factor for Coronary artery disease in Iranian population

Cloning of glucose oxidase gene in PKK233-3

Glucose oxidase [GO] has found a variety of industrial applications such as food, chemical and personal care industries. However one of the most important application of GO is used as diagnostic kits. The aim of study was isolation of GO gene from a recombinant vector [PET21aGO] and sub cloning and expression in PKK233-3 vector. Recombinant PET21a GO was extracted from E.coli DH5alpha and was digested with Restriction Enzymes; BamHI, Hindlll then isolated GO gene [1.8kb] and cloned in PKK233-3. PKK233-3GO was transformed in to E.coli DH5alpha. Our data demonstrated that the GO gene has expected size in agarose gel electrophoresis and also the cloned Go has a correct size after restriction analysis. The GO gene was cloned in prokaryotic host. This is a report of cloning of GO gene in Iran that can be used for further cloning of that gene in expression vectors for production of recombinant Enzyme