Alterations in the hepatic enzymes following experimental lead poisoning

An investigation on the influence of lead toxicity on some of the hepatic enzymes was studied in rats both after a shorter interval of 15 d and after longer intervals of 60 and 90 d. Three different doses of lead as 5, 10, and 50 mg/kg body wt were administered orally on every alternate day. Whereas significant inhibition of succinic dehydrogenase was seen following lead poisoning, the activity acid and alkaline phosphatase increased with lead intoxication. The histoarchitecture of the liver was grossly intact. Liver accumulated less lead compared to kidney at 60 and 90 d.     

Metformin promotes Mycobacterium tuberculosis killing and increases the production of human β-defensins in lung epithelial cells and macrophages

Diabetes has been associated with an increased risk of developing tuberculosis. The reasons related to the increased susceptibility to develop TB in type 2 diabetes mellitus (T2DM) individuals, has not been completely elucidated. However, this susceptibility has been attributed to several factors including failures and misfunctioning of the immune system. In the present study, we aimed to determine the role of anti-hyperglycemic drugs such as glyburide, insulin, and metformin to promote the killing of mycobacteria through the regulation of innate immune molecules such as host defense peptides (HDP) in lung epithelial cells and macrophages. Our results showed that metformin reduces bacillary loads in macrophages and lung epithelial cells which correlates with higher production of β-defensin-2, -3 and -4. Since β-defensins are crucial molecules for controlling Mycobacterium tuberculosis growth, the present results suggest that the use of metformin would be the first choice in the treatment for T2DM2, in patients within tuberculosis-endemic areas.     

Molecular and immunological characterization of the major outer membrane proteins of Brucella

Abstract Saccharomyces cerevisiae exponentially growing in basic or 0.7 M NaCl medium were isotopically labelled with ³⁵S-methionine, followed by protein separation and quantification by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) combined with computerised image analysis. The electrophoretic separation resolved about 650 proteins of which 13 displayed significant and at least 2-fold changes in rate of synthesis during saline growth. By sequencing of 2D-PAGE resolved proteins, one of the 8 induced spot, p42.9/5.5, was shown to correspond to the full length (containing the N-terminal extension) product of the GPD 1 gene encoding the cytoplasmic glycerol 3-phosphate dehydrogenase. The expression of the TDH 3 gene, glyceraldehyde 3-phosphate dehydrogenase, and the ENO 2 gene, enolase, decreased during growth in NaCl medium, declines hypothesised to have an impact on the flux to glycerol.     

Reaction profile of the last step in cytochrome P-450 catalysis revealed by studies of model complexes

 A series of oxoiron(IV) porphyrin cation radical complexes was investigated as compound I analogs of cytochrome P-450. Both the spectroscopic features and the reactivities of the complexes in oxygen atom transfer to olefins were examined as a function of only one variable, the axial ligand trans to the oxoiron(IV) bond. The results disclosed two important kinetic steps – electron transfer from olefin to oxoiron(IV) and intramolecular electron transfer from metal to porphyrin radical – which are affected differently by the axial ligands. The large kinetic barrier of the latter step in the reaction of olefins with the perchlorato-bound oxoiron(IV) porphyrin cation radical complex enabled the trapping of a reaction intermediate in which the metal, but not the porphyrin radical, is reduced. The first electron transfer step is probably followed by σ-bond formation, which readily accounts for formation of isomerized organic products at low temperatures. It is finally postulated that part of the enhanced oxygenation activities of cytochrome P-450 monooxygenases and chloroperoxidases is due to a lowering of the energy barrier for the second electron transfer step via participation of their redox-active cysteinate ligand. Received: 16 January 1997 / Accepted: 24 May 1997     

The Importance of Amine-degrading Enzymes on the Biogenic Amine Degradation in Fermented Foods: A review

Biogenic amines (BAs) are a class of harmful compounds often be found in high protein foods, especially naturally fermented foods. BAs derive from free amino acid decarboxylation through microbial activities and can cause toxic effects (headache, heart palpitations, vomiting) on humans, depending on individual sensitivity. Indigenous amine-degrading strains or strains producing amine-degrading enzymes (ADEs) have drawn great attention since they play an important role in affecting BA accumulation, and enzymes/genes involved in the biosynthetic mechanisms. They also help maintain the sensory quality of the final products. Besides, due to ADEs’ harmless catalytic products, they can be further utilized in fermented foods and beverages to reduce BAs. This review describes in detail the mechanisms of BAs formation, as well as the diversity of ADEs able to degrade BAs in a model or real food systems. A deeper knowledge of this issue is crucial because ADEs’ activities are often associated with strains rather than species or genera. Moreover, this information can help to improve the selection and characterization of strains for further applications as starters or bioprotective cultures, to obtain high-quality foods with reduced BAs contents.     

Membrane—vanadium interaction: A toxicokinetic evaluation

Vanadium is an important trace metal widely distributed in environment. Interaction of vanadate with skeletal muscle sarcolemma and basement membrane has been focussed. Scatchard analysis indicated the presence of more than one binding site for vanadate. Vanadate inhibits sarcolemmal and intestinal brush border membrane enzymes in a non-competitive manner. Membrane-vanadium interaction may lead to several structural and functional changes. The binding of vanadium to basement membrane may have some protective role.     

The influence of seed apparency,nutrient content and chemical defenses on dietary preference in Dipodomys ordii

Summary Physical, nutritional and defensive qualities of seeds differ in the extent to which they influence granivore preference. In a study aimed to quantifying those differences, Ord's kangaroo rats (Dipodomys ordii) were found to prefer the seeds of just three of twenty-nine species: Cryptantha crassisepala, Oryzopsis hymenoides and Salsola kali. Oryzopsis hymenoides was most preferred during the early plant growth season (April–July); preference for S. kali peaked during late (August–November) and dormant (December–March) seasons; and greatest preference for C. crassisepala occurred during dormant and early seasons. Regression of forage ratios, averaged across seasons, against seed length, mass, abundance, patchiness, percent nitrogen, energy content, and chemical defenses showed seed length to be the most important predictor of seed preference. Seed length combined with nitrogen (protein) content and levels of two defensive compounds, saponins and non-protein amino acids, to account for 68% of the variation in seed preference. The importance of seed length rather than biomass indicated that there are limits to the ability of D. ordii to detect small seeds and that small size facilitated escape of dispersed seeds. Seasonality in preference suggested, however, that seed escape was encountered by predispersal harvesting of newly maturing seeds still on plants. Maximization of protein intake contradicted previously published observations, but presumably reflected low nitrogen availability. In addition to small size, the presence of saponins or non-protein amino acids in seeds was sufficient to negate the positive influence of higher protein content.     

Cyclic CMP and cyclic UMP mediate bacterial immunity against phages

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A temperature‐dependent conformational change of NADH oxidase from Thermus thermophilus HB8

Using molecular dynamics simulations and steady‐state fluorescence spectroscopy, we have identified a conformational change in the active site of a thermophilic flavoenzyme, NADH oxidase from Thermus thermophilus HB8 (NOX). The enzyme's far‐UV circular dichroism spectrum, intrinsic tryptophan fluorescence, and apparent molecular weight measured by dynamic light scattering varied little between 25 and 75°C. However, the fluorescence of the tightly bound FAD cofactor increased approximately fourfold over this temperature range. This effect appears not to be due to aggregation, unfolding, cofactor dissociation, or changes in quaternary structure. We therefore attribute the change in flavin fluorescence to a temperature‐dependent conformational change involving the NOX active site. Molecular dynamics simulations and the effects of mutating aromatic residues near the flavin suggest that the change in fluorescence results from a decrease in quenching by electron transfer from tyrosine 137 to the flavin. Proteins 2012. © 2011 Wiley Periodicals, Inc.