A study of lipid profile and ECG changes in chronic kidney disease patients

Introduction: Hyperlipidemia, one of the important risk factor of atherosclerosis, is an abnormality commonly encountered in patients with chronic kidney disease. There are several other important risk factors, such as smoking, proteinuria, oxidative stress, inflammation and dyslipidemia that independently or in combination with elevated blood pressure, can cause deterioration in renal function. Aim of the study: To analyze lipid alterations that can occur in chronic kidney disease patients. Materials and methods: This study was conducted among 50 patients with chronic kidney disease. All the patients with established chronic kidney disease ensured with radiological evidence and on conservative treatment were included in the study. Lipid profile parameters are estimated under standard techniques. Results: Total cholesterol (TC), Triglycerides (TGL), High-Density Lipoprotein (HDL), and LowDensity Lipoprotein (LDL) of all the patients were investigated for the lipid profile study. It was found that the majority (80%) of the study participants were found to have low HDL, 62% of the participants were found to have a high triglyceride level. Overall, seven patients (14%) showed abnormal lipid profile with respect to all the four parameters. Conclusion: HDL-C levels were lower and triglycerides, total cholesterol, and TGL levels were higher in the study group. There is a statistically significant increase in serum triglycerides level in patients with CKD stage 3, 4 and 5. Predominant lipid abnormalities were reduced HDL-C levels and elevated TGL.

Comparison of toxicity of selected mustard agents by percutaneous and subcutaneous routes.

Comparative toxicity of nitrogen mustards (HN-1, HN-2 and HN-3) and sulphur mustard was carried out in mice. Based on LD50, the toxicity pattern was HN-2 < HN-1 < HN-3 < sulphur mustard by percutaneous route whereas, by subcutaneous route the toxicity pattern was sulphur mustard < HN-3 < HN-2 < HN-1. Single dose of 1 LD50 of nitrogen mustards and sulphur mustard was administered percutaneously and various oxidative stress parameters were also evaluated. The weight loss was more in HN-2 on day 3 and in sulphur mustard on day 7. There was a drastic fall of WBC count on day 3 in all groups with a recovery in nitrogen mustard groups on day 7. The RBC count and haemoglobin content showed a significant increase on day 7 in sulphur mustard group. The plasma enzymes (ALT, AST and ALP) showed an increase in all groups on day 3 and day 7. The hepatic GSH and GSSG contents were reduced and MDA content increased in all groups, with a further change in sulphur mustard on 7 day. Extensive DNA fragmentation was observed in all the nitrogen mustard groups compared to sulphur mustard group, on day 3. However, on the day 7 the DNA fragmentation was same in all groups. This study showed that the nitrogen mustards and sulphur mustard were extremely toxic by percutaneous route and caused oxidative stress. Sulphur mustard was more toxic by the percutaneous route and the effects were delayed and progressive.

Visceral manifestations of von Hippel-Lindau disease: value of ultrasound and CT imaging.

Visceral manifestations of von Hippel-Lindau disease (VHLD) are generally asymptomatic and their early detection is of considerable help in the management. This communication documents the usefulness of imaging studies in detecting visceral manifestations in two cases of VHLD.

Rapid purification of secretory acid proteinase from Candida albicans and its characterization.

Secretory acid proteinase from C. albicans was purified from culture supernatant to apparent homogeneity by ion-exchange chromatography. Two isozymes of the proteinase were resolved using a novel chromatofocusing method. The enzyme, which appears to be a glycoprotein, consists of a single polypeptide chain with glutamine at the N-terminus. Its molecular weight is about 45,000 and isoelectric point is pH 4.6. At pH 5, the proteinase is stable at 45 degrees C for at least 15 min. It has a broad substrate specificity. With BSA as a substrate, Km was determined to be 1.6 x 10(-4) M. The enzyme is inhibited by pepstatin and thus is a carboxyl proteinase. It undergoes autocatalytic digestion at or below pH 5.0. The kinetics of induction of proteinase by various proteins are also reported.