Intestinal and pancreas enzyme activity of broilers exposed to thermal stress

Thirty-two Hubbard broilers were raised under commercial husbandry to evaluate the effect of temperature exposure (26 and 35ºC) on the activity of digestive enzymes at different ages (23 and 46 days) and different diet energy levels (2,900 and 3,200 kcal ME/kg). Data were analyzed in a 2x2x2 factorial arrangement (energy/temperature/age) in a completely randomized design. Animals were slaughtered after four hours of heat exposure for sampling of an intestinal segment, to extract alkaline phosphatase, and pancreas, to extract amylase, lipase and trypsin. The activity of intestinal alkaline phosphatase was influenced by energy level and animal age. Energy level of diet and environmental temperature interfered on the activity of pancreatic amylase. Lipase activity was affected only by broiler age. There was no effect of treatments on pancreatic trypsin activity. It was concluded that the activity of the pancreatic enzymes can be regulated by different mechanisms under stress conditions induced by heat

Analysis of aquaporin expression in liver with a focus on hepatocytes

A deeper understanding of aquaporins (AQPs) expression and transcriptional regulation will provide useful information for liver pathophysiology. We established a complete AQPs mRNA expression profile in human and mouse liver, as well as protein localization of expressed AQPs. Additionally, the modulation of AQPs mRNA levels in response to various agents was determined in human HuH7 cells and in primary culture of mouse hepatocytes. AQP1, AQP3, AQP7, AQP8, and AQP9 mRNA and protein expressions were detected in human liver, while only AQP6 and AQP11 mRNAs were detected. We reported for the first time the localization of AQP3 in Kupffer cells, AQP7 in hepatocytes and endothelial cells, and AQP9 in cholangiocytes. In addition, we confirmed the localization of AQP1 in endothelial cells, and of AQP8 and AQP9 in hepatocytes. On HuH7 cells, we reported the presence of AQP4 mRNA, confirmed the presence of AQP3, AQP7, and AQP11 mRNAs, but not of AQP8 mRNA. On primary culture of murine hepatocytes, AQP1 and AQP7 mRNAs were identified, while the presence of AQP3, AQP8, AQP9, and AQP11 mRNAs was confirmed. At the protein level, murine endothelial liver cells expressed AQP1 and AQP9, while hepatocytes expressed AQP3, AQP7, AQP8, and AQP9, and macrophages expressed AQP3. Dexamethasone, forskolin, AICAR, rosiglitazone, octanoylated, and non-octanoylated ghrelin regulated some AQP expression in primary culture of murine hepatocytes and human HuH7 cells. Additional studies will be required to further assess the role of AQPs expression in human and murine liver and understand the transcriptional regulation of AQPs in hepatocytes under pathophysiological conditions.SCOPUS: ar.jinfo:eu-repo/semantics/publishe