Nano Zinc Supplementation Affects Immunity, Hormonal Profile, Hepatic Superoxide Dismutase 1 (SOD1) Gene Expression and Vital Organ Histology in Wister Albino Rats.

The study was conducted to assess nano zinc (ZnN) as a feed supplement with an aim to compare the supplemental dose of inorganic zinc (ZnI). ZnN was synthesized from 0.45 molar (M) zinc nitrate [Zn(NO3)2.6H2O] and 0.9 M sodium hydroxide (NaOH) and was confirmed to be of ZnN by TEM-EDAX measurements. Wister albino rats (rats; 84, 53.6 ± 0.65 g) were divided into seven groups (4 replicate with 3 rats each) and given feed supplemented with zinc for 60 days with either of the following diets: (1) normal control (NC): basal diet (BD) + no supplemental Zn; (2) ZnI-25: BD + 25 mg/kg Zn from inorganic ZnO; (3) ZnN-25: BD + 25 mg/kg of ZnN; (4) ZnN-12.5: BD + 12.5 mg/kg of ZnN; (5) ZnN-6.25: BD + 6.25 mg/kg of ZnN; (6) ZnN-3.125: BD + 3.125 mg/kg of ZnN; (7) ZnN-50: BD + 50 mg/kg of ZnN. T3 and insulin-like growth factor-1 (IGF-1) hormone levels were similar among groups (P > 0.05), whereas T4 and testosterone were significantly affected, based on supplemented dose. Zn supplementation improved both cell-mediated and humoral immunity. However, both cell-mediated immunity at 24 h and humoral immunity were statistically similar in ZnI-25 and ZnN-6.25 groups. Superoxide dismutase 1 gene expression was found to be similar in all experimental groups. The vascular degeneration were found in liver tissues moderately in NC, mildly in ZnN-6.25 and ZnN-3.125 groups, and no observable changes were noticed in kidney and spleen tissues. However, there was a mild damage in intestinal epithelium of ZnN-25 group rats, hyperplasia of goblet cells, and moderate damage in intestinal villi were observed in ZnN-50 group rats. From the study, it can be concluded that ZnN at half the dose of ZnI showed similar or better responses in terms of immunity, SOD-1 expression, hormonal profiles, and the tissue architecture of vital organs in rats, i.e., 25 mg/kg of Zn from ZnI and 12.5 mg/kg of ZnN impacted similar biological responses like immunity, SOD-1 expression, hormonal profiles, and the tissue architecture of vital organs in rats.

A new method for post-translationally labeling proteins in live cells for fluorescence imaging and tracking.

We present a novel method to fluorescently label proteins, post-translationally, within live Saccharomycescerevisiae. The premise underlying this work is that fluorescent protein (FP) tags are less disruptive to normal processing and function when they are attached post-translationally, because target proteins are allowed to fold properly and reach their final subcellular location before being labeled. We accomplish this post-translational labeling by expressing the target protein fused to a short peptide tag (SpyTag), which is then covalently labeled in situ by controlled expression of an open isopeptide domain (SpyoIPD, a more stable derivative of the SpyCatcher protein) fused to an FP. The formation of a covalent bond between SpyTag and SpyoIPD attaches the FP to the target protein. We demonstrate the general applicability of this strategy by labeling several yeast proteins. Importantly, we show that labeling the membrane protein Pma1 in this manner avoids the mislocalization and growth impairment that occur when Pma1 is genetically fused to an FP. We also demonstrate that this strategy enables a novel approach to spatiotemporal tracking in single cells and we develop a Bayesian analysis to determine the protein's turnover time from such data.

Effect of substituting increasing levels of organic Zn for inorganic Zn on performance, hematological and serum biochemical constituents, antioxidant status and immune response in rat.

The effect of replacing dietary Zn supplemented from inorganic (ZnCO3) source with organic Zn (Zn methionine; Zn-met) was investigated in 72 rats (98.42 ± 1.483 g) by randomly allotting to 4 diets (6 replicates/diet, 3 rats/replicate). Basal diet was prepared with purified ingredients without Zn. The control diet (AIN-76A) contained 12 ppm of Zn from ZnCO3 (100-I). In the other diets ZnCO3 was replaced with Zn-met at the rates of 50 (50I:50O), 75 (25I:75O) or 100% (100-O). Weekly body weight and daily feed intake were recorded for 14 weeks. Blood was collected by retro-orbital puncture on the 70th and 80th day to determine haematological and various serum biochemical constituents, and antioxidant enzyme activities in haemolysate, respectively. Rats were antigenically challenged with sheep RBC on day 73 to assess humoral immune response (HIR), and on day 95 for cell mediated immune response (CMIR) and rats were sacrificed at the end of rearing period to collect liver, muscle, pancreas and kidneys for Zn estimation and oxidative stress markers in liver. The data were analysed using completely randomized design. Weight gain and feed intake, hematological and serum biochemical constituents, Zn content in organs (except liver) were not influenced by replacing ZnCO3 with Zn-met. Zinc concentrations in the serum and liver were higher (P<0.05) with 50% replacement of ZnCO3 with Zn-met compared to 0 or 100% replacement. Lower (P<0.05) lipid peroxidation and higher (P<0.05) glutathione peroxidase and glutathione reductase activities were observed with 50 and 75% replacement of ZnCO3 with Zn-met compared to 0 or 100% replacement. Protein carbonyls and reduced glutathione in liver were not affected, while TBARS decreased (P<0.05) with substituting Zn-met (50-100%) for ZnCO3. The HIR and CMIR increased with increasing Zn-met supplementation and the highest response was observed with 75-100% replacement of ZnCO3 with Zn-met. It is concluded that replacement of 50 or 75% of ZnCO3 with Zn-met increased antioxidant and immune response in rats with no effect on growth.

Supported membranes on chemically structured and rough surfaces.

We present a general linear response description of membrane adhesion at rough or chemically structured surfaces. Our method accounts for nonlocal Van der Waals effects and contains the more approximate (and local) Deryagin approach in a simple limit. Specializing to supported membranes we consider the effects of substrate structure on the membrane adhesion energy and configuration. Adhesion is usually less favorable for rough substrates and the membrane shape tends to follow that of the surface contours. Chemical patterning (described by a spatially varying Van der Waals force), however, favors adhesion with the membrane configuration being out of phase with the surface structure. Finally, considering a surface indented with "V"-shaped trenches, we show that our approach is in good agreement with an exact numerical solution.