77 research outputs found

    Effect of a single Dialysis session on plasma Lp(a) levels in patients on Maintenance haemodialysis

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    Background: 
Cardiovascular disease (CVD) is a major cause of mortality in End stage renal disease (ESRD) patients on Maintenance haemodialysis (MHD). Lp (a), is a specialized form of glycoprotein-LDL-cholesterol complex and is an independent risk factor for myocardial infarction. The risk is related to its atherogenic and thrombogenic properties. The present study was taken up to evaluate changes in Lp(a) and Lipid profile in patients undergoing hemodialysis session. 

Methodology: 
Twenty seven patients with end stage renal disease who were on maintenance hemodialysis were included. Plasma samples were collected hourly during a dialysis session with polysulfone membrane using bicarbonate dialysate. Plasma cholesterol, triglycerides, and Lp(a) were estimated on Beckmann CX9 Fully Automated Analyzer using commercial kits. Statistical analysis was performed using SPSS for windows version 11.5.

Results: 
Results of analysis of variance for repeated measures after correction for hemoconcentration where necessary revealed a decrease in Lp(a) (p=0.022) and triglycerides (p=0.001) levels and no change in cholesterol (p=0.48) levels.

Conclusion: 
Maintenance dialysis program is known to produce Dyslipidemia. Study of Lp(a) in dialysis patients is important as this is an independent risk marker. However there are very few reports on changes in Lp(a) due to the dialysis session. Our findings will be discussed in comparison with other reports.
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    Atherogenic dyslipidemia in diabetic nephropathy: lipoprotein (a), lipid ratios and atherogenic index

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    Background: Atherogenic lipid profile is reported to become pronounced with onset of nephropathy. Lipid ratios also indicate atherogenic dyslipidemia. Lipoprotein (a) [(Lp(a)] considered as an independent risk factor for cardiovascular diseases (CVD), may play an important role in development and progression of nephropathy in type 2 diabetes mellitus (T2DM). The present study aimed to assess atherogenic dyslipidemia in T2DM and diabetic nephropathy patients. Methods: Total cholesterol (TC), triglycerides(Tgl), high density lipoprotein (HDL), low density lipoprotein (LDL), very low density lipoprotein (VLDL), Lp(a), lipid ratios: TC/HDL, Tgl/HDL, LDL/HDL, non-HDL cholesterol and atherogenic index (AI) was assessed in T2DM (n=35), diabetic nephropathy (n=30) and healthy individuals (n=30). Means of biochemical parameters were compared by ANOVA (analysis of variance). Pearson correlation was performed to study the association between parameters. Receiver operating characteristics (ROC) curve analysis was done to assess the predictive ability of the variables.Results: Atherogenic dyslipidemia with elevated Lp(a), TC, Tgl, VLDL, LDL, non-HDL cholesterol, lipid ratios, AI and low HDL levels were observed in both T2DM patients with and without nephropathy when compared to controls. Significantly high Tgl/HDL, TC/HDL and AI were observed in diabetic nephropathy when compared to T2DM. Conclusion: T2DM and diabetic nephropathy are associated with dyslipidemia which was more pronounced in diabetic nephropathy. Elevated Lp(a) levels may be considered as an independent CVD risk marker in T2DM and diabetic nephropathy patients along with atherogenic lipid ratio indicators

    Effect Of A Dialysis Session On Plasma Branched Chain Aminio Acids In Hemodialysis Patients

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    Protein and amino acid (AA) metabolism is abnormal in End stage renal disease (ESRD). Hemodialysis (HD) procedure is a strong catabolic stimulus. Branched chain amino acids (BCAAs) can affect other AA levels by reducing AA efflux from muscle due to inhibition of muscle protein degradation. Essential amino acids and keto acid supplements including BCAA and branched-chain keto acid (BCKA) are proposed to decrease protein intake while maintaining protein status. This study was taken up to evaluate the effect of a dialysis session on plasma BCAA’s for which fifteen patients of ESRD on Maintenance HD, thrice a week were recruited into the study. Analysis was done on samples drawn at the beginning (pre-HD) and after the end of each dialysis session (post-HD). Plasma BCAA’s were estimated by Reverse phase High performance liquid chromatography using pre column derivatization with O-pthalaldehyde-Mercaptoethanol. A significant decrease in plasma concentration of Valine and Isoleucine were observed post-HD compared to the pre-HD levels (p<0.05). After correcting the data by creatinine, the decrease in plasma concentrations of Valine and Isoleucine were still found to be statistically significant. The percentage losses after the completion of HD were –24.45, –23.19, and –6.22% respectively for valine, isoleucine, and leucine. The lower reduction in leucine could be due to its appearance from muscle catabolism during the dialysis session. In conclusion, hemodialysis itself may influence dialysate amino acid losses and may have an effect on muscle protein breakdown and this negative protein can be reversed with nutritional supplementation

    A multipurpose immobilized biocatalyst with pectinase, xylanase and cellulase activities

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    <p>Abstract</p> <p>Background</p> <p>The use of immobilized enzymes for catalyzing various biotransformations is now a widely used approach. In recent years, cross-linked enzyme aggregates (CLEAs) have emerged as a novel and versatile biocatalyst design. The present work deals with the preparation of a CLEA from a commercial preparation, Pectinex™ Ultra SP-L, which contains pectinase, xylanase and cellulase activities. The CLEA obtained could be used for any of the enzyme activities. The CLEA was characterized in terms of kinetic parameters, thermal stability and reusability in the context of all the three enzyme activities.</p> <p>Results</p> <p>Complete precipitation of the three enzyme activities was obtained with n-propanol. When resulting precipitates were subjected to cross-linking with 5 mM glutaraldehyde, the three activities initially present (pectinase, xylanase and cellulase) were completely retained after cross-linking. The V<sub>max</sub>/K<sub>m </sub>values were increased from 11, 75 and 16 to 14, 80 and 19 in case of pectinase, xylanase and cellulase activities respectively. The thermal stability was studied at 50°C, 60°C and 70°C for pectinase, xylanase and cellulase respectively. Half-lives were improved from 17, 22 and 32 minutes to 180, 82 and 91 minutes for pectinase, xylanase and cellulase respectively. All three of the enzymes in CLEA could be reused three times without any loss of activity.</p> <p>Conclusion</p> <p>A single multipurpose biocatalyst has been designed which can be used for carrying out three different and independent reactions; 1) hydrolysis of pectin, 2) hydrolysis of xylan and 3) hydrolysis of cellulose. The preparation is more stable at higher temperatures as compared to the free enzymes.</p

    Hacking into bacterial biofilms: a new therapeutic challenge

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    Microbiologists have extensively worked during the past decade on a particular phase of the bacterial cell cycle known as biofilm, in which single-celled individuals gather together to form a sedentary but dynamic community within a complex structure, displaying spatial and functional heterogeneity. In response to the perception of environmental signals by sensing systems, appropriate responses are triggered, leading to biofilm formation. This process involves various molecular systems that enable bacteria to identify appropriate surfaces on which to anchor themselves, to stick to those surfaces and to each other, to construct multicellular communities several hundreds of micrometers thick, and to detach from the community. The biofilm microbial community is a unique, highly competitive, and crowded environment facilitating microevolutionary processes and horizontal gene transfer between distantly related microorganisms. It is governed by social rules, based on the production and use of "public" goods, with actors and recipients. Biofilms constitute a unique shield against external aggressions, including drug treatment and immune reactions. Biofilm-associated infections in humans have therefore generated major problems for the diagnosis and treatment of diseases. Improvements in our understanding of biofilms have led to innovative research designed to interfere with this process

    A Novel Manganese Efflux System, YebN, Is Required for Virulence by Xanthomonas oryzae pv. oryzae

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    Manganese ions (Mn2+) play a crucial role in virulence and protection against oxidative stress in bacterial pathogens. Such pathogens appear to have evolved complex mechanisms for regulating Mn2+ uptake and efflux. Despite numerous studies on Mn2+ uptake, however, only one efflux system has been identified to date. Here, we report on a novel Mn2+ export system, YebN, in Xanthomonas oryzae pv. oryzae (Xoo), the causative agent of bacterial leaf blight. Compared with wild-type PXO99, the yebN mutant was highly sensitive to Mn2+ and accumulated high concentrations of intracellular manganese. In addition, we found that expression of yebN was positively regulated by Mn2+ and the Mn2+-dependent transcription regulator, MntR. Interestingly, the yebN mutant was more tolerant to methyl viologen and H2O2 in low Mn2+ medium than PXO99, but more sensitive in high Mn2+ medium, implying that YebN plays an important role in Mn2+ homoeostasis and detoxification of reactive oxygen species (ROS). Notably, deletion of yebN rendered Xoo sensitive to hypo-osmotic shock, suggesting that YebN may protect against such stress. That mutation of yebN substantially reduced the Xoo growth rate and lesion formation in rice implies that YebN could be involved in Xoo fitness in host. Although YebN has two DUF204 domains, it lacks homology to any known metal transporter. Hence, this is the first report of a novel metal export system that plays essential roles in hypo-osmotic and oxidative stress, and virulence. Our results lay the foundations for elucidating the complex and fascinating relationship between metal homeostasis and host-pathogen interactions
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