Lipid peroxidation and changes in major antioxidant markers in copper quinolate fungicide-exposed rats.

The present study investigated the toxic effects of sub-chronic exposure to copper quinolate (CuQ) fungicide on liver and kidney function. Twenty-four adult male Wistar rats were equally divided into a control group, and three treated groups received, respectively, by oral gavage, three increasing doses of CuQ: 47; 67.1; and 94 mg/kg b.w corresponding, respectively, LD50/100, LD50/70, and LD50/50 daily for 8 weeks. CuQ resulted in a significant increase in the serum enzymatic activity of aspartate aminotransferase (AST), alkaline phosphatase (ALP), lactate dehydrogenase (LDH), and the serum levels of urea, creatinine, uric acid, and malondialdehyde, along with a marked decrease in alanine aminotransferase (ALT) activity, and the contents of total protein and albumin compared to those of the control group. Furthermore, glutathione content and the enzymatic activity of superoxide dismutase (SOD), catalase (CAT), glutathione S-transferase (GST), and glutathione peroxidase (GPx) decreased significantly in a dose-dependent manner with respect to CuQ. The adverse effects of CuO were supported by the histopathological evaluations of liver and kidney tissues. Conclusively, sub-chronic CuQ exposure was shown to induce kidney and liver oxidative damage and dysfunction.

[Adolescent binge drinking: neurocognitive consequences and gender differences]. / Piekdrinken op jonge leeftijd: gevolgen voor neurocognitieve functies en genderverschillen.

BACKGROUND: Binge drinking by adolescents and young adults is on the increase and is having serious medical and social consequences. Over the last ten years more and more research has been done into the neurocognitive effects of binge drinking and into the possibility that these effects are gender-specific. However, so far, findings have been inconsistent. AIM: To collect evidence for the negative impact of binge drinking on the neurocognitive functioning of adolescents and young adults and to find out whether binge drinking has a more serious effect on neurocognition in females than in males. METHOD: We searched the literature using PubMed and Web of Science. RESULTS: Nineteen studies satisfied our selection criteria. Eleven studies examined the binge/gender interaction. CONCLUSION: There is considerable evidence that binge drinking does have a negative effect on neurocognition in adolescents and young adults, particularly with regard to executive functioning and memory. Females seem to be more susceptible than males to deficits in spatial working memory and impulse control.

The hxB gene, necessary for the post-translational activation of purine hydroxylases in Aspergillus nidulans, is independently controlled by the purine utilization and the nicotinate utilization transcriptional activating systems.

Molybdenum-containing enzymes of the hydroxylase class (such as xanthine dehydrogenase, aldehyde oxidase and nicotinate dehydrogenase) require a terminal sulphur atom attached to the molybdenum to hydroxylate their specific substrates. The transulphurylation reaction is carried out in Drosophila melanogaster by the product of the ma-I gene. In Aspergillus nidulans, the activity of the isofunctional and homologous HxB protein is needed in at least two different metabolic contexts, when the organism grows on purines and when it grows on nicotinate as nitrogen sources. We show here that the expression of the hxB gene is not constitutive. It is induced independently and additively by the inducers of the purine and of the nicotinate utilization pathways. Each of these induction pathways is affected independently by mutations in their cognate genes, uric acid induction by mutations in the UaY protein and nicotinate and 6-nicotinate induction by those in the hxnR/aplA complex. It is, in both metabolic contexts, exquisitely sensitive to nitrogen metabolite repression and highly dependent on the AreA GATA factor.

Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a mechanism for the insertion of the terminal sulphur atom in the molybdopterin cofactor.

The molybdopterin cofactor (MoCF) is required for the activity of a variety of oxidoreductases. The xanthine oxidase class of molybdoenzymes requires the MoCF to have a terminal, cyanolysable sulphur ligand. In the sulphite oxidase/nitrate reductase class, an oxygen is present in the same position. Mutations in both the ma-l gene of Drosophila melanogaster and the hxB gene of Aspergillus nidulans result in loss of activities of all molybdoenzymes that necessitate a cyanolysable sulphur in the active centre. The ma-l and hxB genes encode highly similar proteins containing domains common to pyridoxal phosphate-dependent cysteine transulphurases, including the cofactor binding site and a conserved cysteine, which is the putative sulphur donor. Key similarities were found with NifS, the enzyme involved in the generation of the iron-sulphur centres in nitrogenase. These similarities suggest an analogous mechanism for the generation of the terminal molybdenum-bound sulphur ligand. We have identified putative homologues of these genes in a variety of organisms, including humans. The human homologue is located in chromosome 18.q12.