Mn-SOD 47 CC genotype in combination with high tea consumption may prevent complications in Tunisian type-2 diabetes.

Reactive oxygen species metabolizing enzymes may play an important role in the prevention of type-2 diabetes (T2D) complications. We analyzed the association between Cu/Zn-SOD +35 A/C, Mn-SOD T47C, and CAT -21 A/T gene polymorphisms and complications, in combination with tea consumption in Tunisian T2D. A sample of 366 T2D subjects was enrolled in this study. All participants were asked about tea consumption and frequency. Anthropometric, clinical, and routine biochemical characteristics were obtained from subjects' updated medical records. Malondialdehyde, as an early marker of lipid peroxidation, was measured in plasma samples. Urinary polyphenol derivatives (UPDs), as a marker of polyphenols intake, were assessed by the Folin-Ciocalteu assay. SODs and CAT genotypes were determined by conventional restriction fragment length polymorphism-polymerase chain reaction (RFLP-PCR) methods. From all subjects, the results showed that in high tea consumers (>3 cups/day), the frequency of the Mn-SOD 47 CC genotype was significantly higher in T2D without complications compared with T2D with complications (P = 0.03; OR = 0.284; 95%CI = 0.086-0.939). However, no significant associations were observed with Cu/Zn-SOD +35 A/C or CAT -21 A/T genes polymorphisms. Additionally, the evaluation of UPDs showed that individuals carrying the Mn-SOD 47 CC genotype and consuming more than three cups of tea per day present significantly higher UPDs (P = 0.038). In conclusion, the Mn-SOD 47 C variant in combination with high tea consumption may provide protection against complications in T2D.

Influence of the site of measurement on the ability of plethysmographic variability index to predict fluid responsiveness.

BACKGROUND: Plethysmographic variability index (PVI) is an accurate predictor of fluid responsiveness in mechanically ventilated patients. However, the site of measurement of the plethysmographic waveform impacts its morphology and its respiratory variation. The goal of this study was to investigate the ability of PVI to predict fluid responsiveness at three sites of measurement (the forehead, ear, and finger) in mechanically ventilated patients under general anaesthesia. METHODS: We studied 28 subjects after induction of general anaesthesia. Subjects were monitored with a pulmonary artery catheter and three pulse oximeter sensors (the finger, ear, and forehead). Pulse pressure variation, central venous pressure, cardiac index (CI), and PVI measured at the forehead, ear, and finger (PVI(forehead), PVI(ear), and PVI(finger)) were recorded before and after fluid loading (FL). Subjects were responders to volume expansion if CI increased >15% after FL. RESULTS: Areas under the receiver-operating curves to predict fluid responsiveness were 0.906, 0.880, and 0.836 for PVI(forehead), PVI(ear), and PVI(finger), respectively (P<0.05). PVI(forehead), PVI(ear), and PVI(finger) had a threshold value to predict fluid responsiveness of 15%, 16%, and 12% with sensitivities of 89%, 74%, and 74% and specificities of 78%, 74%, and 67%, respectively. CONCLUSIONS: PVI can predict fluid responsiveness in anaesthetized and ventilated subjects at all three sites of measurement. However, the threshold values for predicting fluid responsiveness differ with the site of measurement. These results support the use of this plethysmographic dynamic index in the cephalic region when the finger is inaccessible or during states of low peripheral perfusion.

Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding.

In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H(2)O(2). The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn(2+) ion. In addition, X-ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta-coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N-terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper-like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.