Wireless handheld ultrasound for internal jugular vein assessment in pediatric patients.

BACKGROUND: Rapid evolution of ultrasound technology has allowed widespread use of handheld ultrasound devices (HHUDs) for many possible applications. Along with the adult population, the use of HHUDs for Point of Care Ultrasound (POCUS) in pediatric medicine has been increasing over the last few years. However, pediatric-specific literature is still scarce on mobile vascular ultrasound. OBJECTIVE: To evaluate diagnostic capabilities of Vscan Air™ in comparison with high-end ultrasound for the assessment of the internal jugular vein in children and adolescents. METHODS: 42 Internal Jugular Veins (IJVs) of 21 pediatric patients were scanned by an experienced examiner using a WLAN-supported handheld ultrasound device (Vscan Air™) and high-end cart-based ultrasound (LOGIQ E9) as reference. B-Mode and Color-coded Doppler (CCDS) were performed and compared. Image quality was assessed using a score of 0 to 5 and statistically analyzed. Results were interpreted independently by two readers in consensus. RESULTS: 21 patients (2-17 years; mean 11,00±4,5 years; female n = 11, male n = 10) were examined. The rating score never dropped below 3 for both devices. The median score evaluation of B-Mode and CCDS for the high-end device was 5.00, of Vscan Air™ 5.00 for B-Mode and 4.00 for CCDS. A significant difference was shown between the two devices in the evaluation of CCDS. CONCLUSIONS: Vscan Air™ ultrasound device allows sufficient assessability of the IJV in pediatric patients, opening up new possibilities for fast and mobile POCUS of cervical veins and potential guidance of central venous catheter placement.

Human Cytomegalovirus Induces Vitamin-D Resistance In Vitro by Dysregulating the Transcriptional Repressor Snail.

Vitamin-D supplementation is considered to play a beneficial role against multiple viruses due to its immune-regulating and direct antimicrobial effects. In contrast, the human cytomegalovirus (HCMV) has shown to be resistant to treatment with vitamin D in vitro by downregulation of the vitamin-D receptor. In this study, we aimed to elucidate the mechanism and possible biological consequences of vitamin-D resistance during HCMV infection. Mechanistically, HCMV induced vitamin-D resistance by downregulating the vitamin-D receptor (VDR) within hours of lytic infection. We found that the VDR was inhibited at the promoter level, and treatment with histone deacetylase inhibitors could restore VDR expression. VDR downregulation highly correlated with the upregulation of the transcriptional repressor Snail1, a mechanism likely contributing to the epigenetic inactivation of the VDR promoter, since siRNA-mediated knockdown of Snail partly restored levels of VDR expression. Finally, we found that direct addition of the vitamin-D-inducible antimicrobial peptide LL-37 strongly and significantly reduced viral titers in infected fibroblasts, highlighting VDR biological relevance and the potential of vitamin-D-inducible peptides for the antiviral treatment of vitamin-D deficient patients.

Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I.

The NADH:ubiquinone oxidoreductase, respiratory complex I, couples electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. The complex consists of a peripheral arm catalyzing the redox reaction and a membrane arm catalyzing proton translocation. The membrane arm is almost completely aligned by a 110 Å unique horizontal helix that is discussed to transmit conformational changes induced by the redox reaction in a piston-like movement to the membrane arm driving proton translocation. Here, we analyzed such a proposed movement by cysteine-scanning of the helix of the Escherichia coli complex I. The accessibility of engineered cysteine residues and the flexibility of individual positions were determined by labeling the preparations with a fluorescent marker and a spin-probe, respectively, in the oxidized and reduced states. The differences in fluorescence labeling and the rotational flexibility of the spin probe between both redox states indicate only slight conformational changes at distinct positions of the helix but not a large movement.