Deuterium brain imaging at 7T during D2 O dosing.

PURPOSE: To characterize the (2 H) deuterium MR signal measured from human brain at 7T in participants loading with D2 O to ˜1.5% enrichment over a six-week period. METHODS: 2 H spectroscopy and imaging measurements were used to track the time-course of 2 H enrichment within the brain during the initial eight-hour loading period in two participants. Multi-echo gradient echo (MEGE) images were acquired at a range of TR values from four participants during the steady-state loading period and used for mapping 2 H T1 and T2 * relaxation times. Co-registration to higher resolution 1 H images allowed T1 and T2 * relaxation times of deuterium in HDO in cerebrospinal fluid (CSF), gray matter (GM), and white matter (WM) to be estimated. RESULTS: 2 H concentrations measured during the eight-hour loading were consistent with values estimated from cumulative D2 O dose and body mass. Signal changes measured from three different regions of the brain during loading showed similar time-courses. After summing over echoes, gradient echo brain images acquired in 7.5 minutes with a voxel volume of 0.36 ml showed an SNR of ˜16 in subjects loaded to 1.5%. T1 -values for deuterium in HDO were significantly shorter than corresponding values for 1 H in H2 O, while T2 * values were similar. 2 H relaxation times in CSF were significantly longer than in GM or WM. CONCLUSION: Deuterium MR Measurements at 7T were used to track the increase in concentration of 2 H in brain during heavy water loading. 2 H T1 and T2 * relaxation times from water in GM, WM, and CSF are reported.

Rapid protein disappearance rates along the small intestine advantage poultry performance and influence the post-enteral availability of amino acids.

A foundation diet, an intermediate blend and a summit diet were formulated with different levels of soyabean meal, casein and crystalline amino acids to compare 'slow' and 'rapid' protein diets. The diets were offered to male Ross 308 chicks from 7 to 28 d post-hatch and assessed parameters included growth performance, nutrient utilisation, apparent digestibility coefficients and disappearance rates of starch and protein (N) in four small intestinal segments. Digestibility coefficients and disappearance rates of sixteen amino acids in three small intestinal segments and amino acid concentrations in plasma from portal and systemic circulations from the foundation and summit diets were determined. The dietary transition significantly accelerated protein (N) disappearance rates in the distal jejunum and ileum. The transition from foundation to summit diets significantly increased starch digestibility coefficients in the ileum and disappearance rates in all four small intestinal segments. These starch responses were associated with significant enhancements in nutrient utilisation. The dietary transition linearly increased digestibility coefficients and disappearance rates of amino acids in the majority of cases. The summit diet increased plasma concentrations of five amino acids but decreased those of four amino acids relative to the foundation diet to significant extents. Plasma concentrations of free amino acids were higher in the portal than systemic circulations. Rapid protein disappearance rates advantaged poultry performance and influenced post-enteral availability of amino acids. If the underlying mechanisms are to be identified, further research into the impact of protein digestive dynamics on broiler performance is required but appears justified.

The Fc Domain of Immunoglobulin Is Sufficient to Bridge NK Cells with Virally Infected Cells.

Clearance of pathogens or tumor cells by antibodies traditionally requires both Fab and Fc domains of IgG. Here, we show the Fc domain of IgG alone mediates recognition and clearance of herpes simplex virus (HSV1)-infected cells. The human natural killer (NK) cell surface is naturally coated with IgG bound by its Fc domain to the Fcγ receptor CD16a. NK cells utilize the Fc domain of bound IgG to recognize gE, an HSV1-encoded glycoprotein that also binds the Fc domain of IgG but at a site distinct from CD16a. The bridge formed by the Fc domain between the HSV1-infected cell and the NK cell results in NK cell activation and lysis of the HSV1-infected cell in the absence of HSV1-specific antibody in vitro and prevents fatal HSV1 infection in vivo. This mechanism also explains how bacterial IgG-binding proteins regulate NK cell function and may be broadly applicable to Fcγ-receptor-bearing cells.