[Relevance of urinary specific protein assay in the diagnosis of kidney diseases].

The analysis of urinary protein composition is an important step in the evaluation and monitoring of kidney diseases. Among the various approaches, the determination of urinary-specific proteins makes it possible to non-invasively detect a preferentially tubular or glomerular injury, to orientate towards a pathological process, to guide the indication of a kidney biopsy, and to follow the evolution of the disease and the effectiveness of a therapy. No study systematically evaluated the performance of urinary-specific proteins for the diagnosis of a renal disease.

Low Serum Creatine Kinase Level Predicts Mortality in Patients with a Chronic Kidney Disease.

Background: Serum creatine kinase (sCK) reflects CK activity from striated skeletal muscle. Muscle wasting is a risk factor for mortality in patients with chronic kidney disease (CKD). The aim of this study is to evaluate whether sCK is a predictor of mortality and end-stage renal disease (ESRD) in a CKD population.

Urinary retinol binding protein is a marker of the extent of interstitial kidney fibrosis.

Currently, a non-invasive method to estimate the degree of interstitial fibrosis (IF) in chronic kidney disease is not available in routine. The aim of our study was to evaluate the diagnostic performance of the measurement of urinary low molecular weight (LMW) protein concentrations as a method to determine the extent of IF. The urines specimen from 162 consecutive patients who underwent renal biopsy were used in the analysis.

Identification of a new stilbene-derived inducer of paraoxonase 1 and ligand of the Aryl hydrocarbon Receptor.

Paraoxonase 1 (PON1) is a high-density lipoprotein-associated enzyme, synthesized in the liver and secreted into the blood. PON1 displays antioxidant properties and is involved in organophosphorous compounds and oxidized lipids degradation. Because of these beneficial effects, pharmacological regulation of PON1 appears to be highly relevant in toxicology and cardiology.

Characterisation of a human liver cystathionine beta synthase mRNA sequence corresponding to the c.[833T>C;844_845ins68] mutation in CBS gene.

Cystathionine beta synthase (CBS) is the only reaction that removes homocysteine from methionine cycle and redirects it to the transsulfuration pathway. The c.[833T>C;844_845ins68] mutation in the CBS gene has been reported initially as corresponding to classic homocystinuria.

The neuronal SAPK/JNK pathway is altered in a murine model of hyperhomocysteinemia.

Deficiency in cystathionine beta synthase (CBS) leads to high plasma homocysteine concentrations and causes hyperhomocysteinemia, a common risk factor for vascular disease, stroke and possibly neurodegenerative diseases. Various neuronal diseases have been associated with hyperhomocysteinemia, but the molecular mechanisms of homocysteine toxicity are unknown. We investigated the pathways involved in the pathological process, by analyzing differential gene expression in neuronal tissues.

Altered gene expression in liver from a murine model of hyperhomocysteinemia.

Cystathionine beta-synthase (CBS) deficiency causes severe hyperhomocysteinemia and other signs of homocystinuria syndrome, in particular a premature atherosclerosis with multiple thrombosis. However, the molecular mechanisms by which homocysteine could interfere with normal cell function are poorly understood in a whole organ like the liver, which is central to the catabolism of homocysteine. We used a combination of differential display and cDNA arrays to analyze differential gene expression in association with elevated hepatic homocysteine levels in CBS-deficient mice, a murine model of hyperhomocysteinemia.