Effects of aldo-keto reductase family 1 member A on osteoblast differentiation associated with lactate production in MC3T3-E1 preosteoblastic cells.

Aldo-keto reductase family 1 member A (AKR1A) is an NADPH-dependent aldehyde reductase widely expressed in mammalian tissues. In this study, induced differentiation of MC3T3-E1 preosteoblasts was found to increase AKR1A gene expression concomitantly increased NOx- (nitrite + nitrate), increased glucose uptake, increased [NAD(P)+]/[NAD(P)H] and lactate production but decreased reactive oxygen species (ROS) without changes in endothelial nitric oxide synthase (eNOS) expression in differentiated osteoblasts (OBs). A study using gain- and loss-of-function MC3T3-E1 cells indicated that AKR1A is essential for modulating OB differentiation and gene expression of collagen 1 A1, receptor activator of nuclear factor kappa-B ligand, and osteoprotegerin in OBs. Immunofluorescence microscopy also revealed that changes in AKR1A expression altered extracellular collagen formation in differentiated OBs. Consistently, analyses of alkaline phosphatase activity and calcium deposits of matrix mineralization by Alizarin Red S staining verified that AKR1A is involved in the regulation of OB differentiation and bone matrix formation. In addition, AKR1A gene alterations affected the levels of NOx-, eNOS expression, glucose uptake, [NAD(P)+]/[NAD(P)H] dinucleotide redox couples, lactate production, and ROS in differentiated OBs. Herein, we report that AKR1A-mediated denitrosylation may play a role in the regulation of lactate metabolism as well as redox homeostasis in cells, providing an efficient way to quickly gain energy and to significantly reduce oxidative stress for OB differentiation.

GeSn resonant-cavity-enhanced photodetectors for efficient photodetection at the 2 µm wavelength band.

The 2 µm wavelength band has recently gained increased attention for potential applications in next-generation optical communication. However, it is still challenging to achieve effective photodetection in the 2 µm wavelength band using group-IV-based semiconductors. Here we present an investigation of GeSn resonant-cavity-enhanced photodetectors (RCEPDs) on silicon-on-insulator substrates for efficient photodetection in the 2 µm wavelength band. Narrow-bandgap GeSn alloys are used as the active layer to extend the photodetection range to cover the 2 µm wavelength band, and the optical responsivity is significantly enhanced by the resonant cavity effect as compared to a reference GeSn photodetector. Temperature-dependent experiments demonstrate that the GeSn RCEPDs can have a wider photodetection range and higher responsivity in the 2 µm wavelength band at higher temperatures because of the bandgap shrinkage. These results suggest that our GeSn RCEPDs are promising for complementary metal-oxide-semiconductor-compatible, efficient, uncooled optical receivers in the 2 µm wavelength band for a wide range of applications.

GeSn resonant-cavity-enhanced photodetectors on silicon-on-insulator platforms.

We report GeSn p-i-n resonant-cavity-enhanced photodetectors (RCEPDs) grown on silicon-on-insulator substrates. A vertical cavity, composed of a buried oxide as the bottom reflector and a deposited SiO2 layer on the top surface as the top reflector, is created for the GeSn p-i-n structure to enhance the light-matter interaction. The responsivity experiments demonstrate that the photodetection range is extended to 1820 nm, completely covering all the telecommunication bands, because of the introduction of 2.5% Sn in the photon-absorbing layer. In addition, the responsivity is significantly enhanced by the resonant cavity effects, and a responsivity of 0.376 A/W in the telecommunication C-band is achieved that is significantly higher than that of conventional GeSn-based PDs. These results demonstrate the feasibility of CMOS-compatible, high-responsivity GeSn-based PDs for shortwave infrared applications.

AdeR protein regulates adeABC expression by binding to a direct-repeat motif in the intercistronic spacer.

Overexpression of the efflux pump AdeABC is associated with tigecycline resistance of multi-drug resistant Acinetobacter baumannii (MDRAB). A two-component regulatory system, sensor AdeS and regulator AdeR proteins regulate the pump. However, the detailed mechanism of the AdeR protein to enhance the expression of adeABC operon is not well defined. We illustrated the biological characteristics of AdeR proteins by comparing a mutant AdeR protein of a tigecycline resistant MDRAB to the wild AdeR protein. By analyzing a series of deletion constructs, a minimal gene cassette of the intercistronic spacer DNA fragment specifically bound with the adeR protein and resulted in band shifting in electrophoresis mobility shifting assays (EMSA). A conserve direct repeat motif was observed in the intercistronic spacer DNA. We demonstrated the AdeR protein was a direct-repeat-binding protein. Two common residue mutations on the AdeR proteins of tigecycline resistant MDRAB isolates could reduce their binding affinity with the intercistronic spacer. The free intercistronic spacer may then more efficiently support the read-through of the adeABC operon during the co-transcriptional translation in tigecycline resistant MDRAB isolates.