Perceptions of an Electronic Medical Record (EMR): Lessons from a French Longitudinal Survey

AbstractThe goal of this longitudinal study is to examine the evolution of the perceptions, namely anxiety, ease of use, usefulness, misfit (not customization), trust and usefulness, related to an Electronic Medical Record (EMR) for the clinical staff in a French Teaching hospital. Two surveys were conducted first in September 2013 and second in December 2015, based on a questionnaire consisting of items on the Likert scale. As results, the correlation of all the variables between the two surveys is very significant (except for usefulness, for which the relationship is significant). This is not surprising, given previous studied focused on habits and learning related to technology adoption. Nevertheless, the increase is not spectacular and it makes necessary to evaluate EMR satisfaction and perceptions in order to elaborate a measure standard enabling comparisons and benchmarking among hospitals

Immunohistochemical aspects of Ito and Kupffer cells in the liver of domesticated and wild ruminants

The mammalian liver is a morphologically and functionally complex organ, made up of not only of the largely pre- dominant parenchymal cells (hepatocytes) but also non-parenchymal cells. Although there are less non-parenchymal cells than hepatocytes, they nevertheless play an important role in regulating many hepatocyte functions, as well as in the immunology of the liver. We investigated the structural aspects of the liver and the morpho-functional characteris- tics of Ito and Kupffer cells in two domesticated ruminant species (cattle and goat) in comparison with four wild rumi- nant species living in captivity in a zoo in northern Italy. The liver specimens were studied using histological, histo- chemical and immunohistochemical methods. The liver parenchyma was structurally normal. Immunohistochemistry was performed for desmin, glial fibrillary acidic protein (GFAP), vimentin, \u3b1-smooth muscle actin (\u3b1-SMA), collagen I, lysozyme, CD 68 and tumor necrosis factor \u3b1 (TNF-\u3b1). In all the studied ruminants, Ito cells reacted with desmin and vimentin antibodies, Kupffer cells were evidenced only with lysozyme-immunopositivity, and both displayed a charac- teristic distribution in the hepatic lobular/acinar structure. The results obtained, not only contribute to the knowledge of ruminant wild species, but also help to define a normal structure reference for the diagnosis and treatment of liver diseases

Regulation of activity and localization of the WNK1 protein kinase by hyperosmotic stress

Mutations within the WNK1 (with-no-K[Lys] kinase-1) gene cause Gordon's hypertension syndrome. Little is known about how WNK1 is regulated. We demonstrate that WNK1 is rapidly activated and phosphorylated at multiple residues after exposure of cells to hyperosmotic conditions and that activation is mediated by the phosphorylation of its T-loop Ser382 residue, possibly triggered by a transautophosphorylation reaction. Activation of WNK1 coincides with the phosphorylation and activation of two WNK1 substrates, namely, the protein kinases STE20/SPS1-related proline alanine–rich kinase (SPAK) and oxidative stress response kinase-1 (OSR1). Small interfering RNA depletion of WNK1 impairs SPAK/OSR1 activity and phosphorylation of residues targeted by WNK1. Hyperosmotic stress induces rapid redistribution of WNK1 from the cytosol to vesicular structures that may comprise trans-Golgi network (TGN)/recycling endosomes, as they display rapid movement, colocalize with clathrin, adaptor protein complex 1 (AP-1), and TGN46, but not the AP-2 plasma membrane–coated pit marker nor the endosomal markers EEA1, Hrs, and LAMP1. Mutational analysis suggests that the WNK1 C-terminal noncatalytic domain mediates vesicle localization. Our observations shed light on the mechanism by which WNK1 is regulated by hyperosmotic stress

Administration of a novel plant extract product via drinking water to post-weaning piglets : effects on performance and gut health

The present study evaluated the effects of a novel plant extract (PE) product (GrazixTM) on the performance and gut health of weaned piglets challenged with Escherichia coli. The PE was a standardised mixture of green tea leaves (Camellia sinensis) and pomegranate fruit (Punica granatum) obtained by using the LiveXtractTM process. A total of 144 piglets were weaned at 24 days and allocated to 8 for a 35-day experiment with a 2 7 2 7 2 factorial design comparing different treatments (water without product (CT) or 8 \u3bcl/kg per day PE in drinking water (PE)), feeding regimens (ad libitum (AD) or restricted (RE)) and oral E. coli challenges on day 9 (sham ( 12 ) or infected ( +)). There were six pens per group with three piglets per pen. On day 35, 24 of the RE feeding piglets were slaughtered. It was found that PE supplementation increased the average daily gain (ADG) from day 28 to day 35 ( P =0.03) and increased the gain to feed ratio (G : F) from day 7 to day 14 ( P = 0.02). RE feeding led to lower feed intake in piglets during the 1st week ( P<0.01), 2nd week ( P = 0.06), 3rd week ( P = 0.05), and throughout the course of the overall study period ( P = 0.05). E. coli challenge decreased the ADG and G : F ratio from day 7 to day 14 ( P = 0.08 and <0.01, respectively) and increased the faecal score (higher values indicate more severe diarrhoea) on days 14, 21, 28 and 35 ( P<0.01). PE supplementation decreased the faecal score in the challenged piglets during the 1st week post-challenge ( P<0.01). E. coli challenge increased the faecal E. coli level on day 14 ( P = 0.03) and increased the Enterobacteriaceae level on day 35 ( P<0.01). Reduced faecal E. coli was observed on days 14 and 35 ( P = 0.05 and 0.02, respectively), and reduced Enterobacteriaceae ( P<0.01) was found on day 35 in the PE animals. RE feeding increased the faecal Lactobacillus, Enterobacteriaceae and E. coli levels on day 35 ( P = 0.02, <0.01 and <0.01, respectively). These results suggest that PE supplementation may improve the gut health status of post-weaning piglets and counteract some of the negative effects that occur when piglets are challenged with E. coli

Glyburide inhibits the Cryopyrin/Nalp3 inflammasome

Glyburide, a sulfonylurea drug commonly used to treat type 2 diabetes, shuts down IL-1β secretion by preventing Cyropyrin activation

Phosphorylation and Transport in the Na-K-2Cl Cotransporters, NKCC1 and NKCC2A, Compared in HEK-293 Cells

Na-K-2Cl cotransporters help determine cell composition and volume. NKCC1 is widely distributed whilst NKCC2 is only found in the kidney where it plays a vital role reabsorbing 20% of filtered NaCl. NKCC2 regulation is poorly understood because of its restricted distribution and difficulties with its expression in mammalian cell cultures. Here we compare phosphorylation of the N-termini of the cotransporters, measured with phospho-specific antibodies, with bumetanide-sensitive transport of K+ (86Rb+) (activity) in HEK-293 cells stably expressing fNKCC1 or fNKCC2A which were cloned from ferret kidney. Activities of transfected transporters were distinguished from those of endogenous ones by working at 37°C. fNKCC1 and fNKCC2A activities were highest after pre-incubation of cells in hypotonic low-[Cl−] media to reduce cell [Cl−] and volume during flux measurement. Phosphorylation of both transporters more than doubled. Pre-incubation with ouabain also strongly stimulated fNKCC1 and fNKCC2A and substantially increased phosphorylation, whereas pre-incubation in Na+-free media maximally stimulated fNKCC1 and doubled its phosphorylation, but inhibited fNKCC2A, with a small increase in its phosphorylation. Kinase inhibitors halved phosphorylation and activity of both transporters whereas inhibition of phosphatases with calyculin A strongly increased phosphorylation of both transporters but only slightly stimulated fNKCC1 and inhibited fNCCC2A. Thus kinase inhibition reduced phosphorylation and transport, and transport stimulation was only seen when phosphorylation increased, but transport did not always increase with phosphorylation. This suggests phosphorylation of the N-termini determines the transporters' potential capacity to move ions, but final activity also depends on other factors. Transport cannot be reliably inferred solely using phospho-specific antibodies on whole-cell lysates

Acute Insulin Stimulation Induces Phosphorylation of the Na-Cl Cotransporter in Cultured Distal mpkDCT Cells and Mouse Kidney

The NaCl cotransporter (NCC) is essential for sodium reabsorption at the distal convoluted tubules (DCT), and its phosphorylation increases its transport activity and apical membrane localization. Although insulin has been reported to increase sodium reabsorption in the kidney, the linkage between insulin and NCC phosphorylation has not yet been investigated. This study examined whether insulin regulates NCC phosphorylation. In cultured mpkDCT cells, insulin increased phosphorylation of STE20/SPS1-related proline-alanine-rich kinase (SPAK) and NCC in a dose-dependent manner. This insulin-induced phosphorylation of NCC was suppressed in WNK4 and SPAK knockdown cells. In addition, Ly294002, a PI3K inhibitor, decreased the insulin effect on SPAK and NCC phosphorylation, indicating that insulin induces phosphorylation of SPAK and NCC through PI3K and WNK4 in mpkDCT cells. Moreover, acute insulin administration to mice increased phosphorylation of oxidative stress-responsive kinase-1 (OSR1), SPAK and NCC in the kidney. Time-course experiments in mpkDCT cells and mice suggested that SPAK is upstream of NCC in this insulin-induced NCC phosphorylation mechanism, which was confirmed by the lack of insulin-induced NCC phosphorylation in SPAK knockout mice. Moreover, insulin administration to WNK4 hypomorphic mice did not increase phosphorylation of OSR1, SPAK and NCC in the kidney, suggesting that WNK4 is also involved in the insulin-induced OSR1, SPAK and NCC phosphorylation mechanism in vivo. The present results demonstrated that insulin is a potent regulator of NCC phosphorylation in the kidney, and that WNK4 and SPAK are involved in this mechanism of NCC phosphorylation by insulin