Bifunctionality of a biofilm matrix protein controlled by redox state

Significance The biofilm matrix is a critical target in the hunt for novel strategies to destabilize or stabilize biofilms. Knowledge of the processes controlling matrix assembly is therefore an essential prerequisite to exploitation. Here, we highlight that the complexity of the biofilm matrix is even higher than anticipated, with one matrix component making two independent functional contributions to the community. The influence the protein exerts is dependent on the local environmental properties, providing another dimension to consider during analysis. These findings add to the evidence that bacteria can evolve multifunctional uses for the extracellular matrix components.</jats:p

Why Does Exercise “Triggerâ€? Adaptive Protective Responses in the Heart?

Numerous epidemiological studies suggest that individuals who exercise have decreased cardiac morbidity and mortality. Pre-clinical studies in animal models also find clear cardioprotective phenotypes in animals that exercise, specifically characterized by lower myocardial infarction and arrhythmia. Despite the clear benefits, the underlying cellular and molecular mechanisms that are responsible for exercise preconditioning are not fully understood. In particular, the adaptive signaling events that occur during exercise to “trigger� cardioprotection represent emerging paradigms. In this review, we discuss recent studies that have identified several different factors that appear to initiate exercise preconditioning. We summarize the evidence for and against specific cellular factors in triggering exercise adaptations and identify areas for future study

Chitosan–hydroxyapatite composite biomaterials made by a one step co-precipitation method: preparation, characterization and in vivo tests

A series of biocompatible chitosan/hydroxyapatite composites has been synthesized in an aqueous medium from chitosan solution and soluble precursor salts by a one-step coprecipitation method. The composite materials were produced in dense and porous variants. XRD and IR studies have shown that the apatite crystals in the composites have structural characteristics similar to those of crystals in biogenic apatite. A study of in vivo behaviour of the materials was carried out. Cylindrical rods made of the chitosan/ hydroxyapatite composite material were implanted into the tibial bones of rats. After 5, 10, 15 and 24 days of implantation, histological and histo-morphometric analyses of decalcified specimens were undertaken to evaluate their biocompatibility and the possibility to apply them in bone tissue engineering. The calcified specimens were examined by scanning electron microscopy combined with X-ray microanalysis to compare the elemental composition and morphological characteristics of the implant and the bone during integration. Porous specimens were osteoconducting and were replaced in vivo by newly formed bone tissue

Histone 2A stimulates glucose-6-phosphatase activity by permeabilization of liver microsomes.

Histone 2A increases glucose-6-phosphatase activity in liver microsomes. The effect has been attributed either to the conformational change of the enzyme, or to the permeabilization of microsomal membrane that allows the free access of substrate to the intraluminal glucose-6-phosphatase catalytic site. The aim of the present study was the critical reinvestigation of the mechanism of action of histone 2A. It has been found that the dose-effect curve of histone 2A is different from that of detergents and resembles that of the pore-forming alamethicin. Inhibitory effects of EGTA on glucose-6-phosphatase activity previously reported in histone 2A-treated microsomes have been also found in alamethicin-permeabilized vesicles. The effect of EGTA cannot therefore simply be an antagonization of the effect of histone 2A. Histone 2A stimulates the activity of another latent microsomal enzyme, UDP-glucuronosyltransferase, which has an intraluminal catalytic site. Finally, histone 2A renders microsomal vesicles permeable to non-permeant compounds. Taken together, the results demonstrate that histone 2A stimulates glucose-6-phosphatase activity by permeabilizing the microsomal membrane