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Aquaporin-2 (AQP2) is a small, transmembrane protein, active in the principal cells of the renal collecting duct system. Phosphorylation and dephosphorylation of this protein regulate its redistribution in the cell, thereby influencing renal water reabsorption. The aims of the study were to identify and analyse the location of AQP2 phosphorylated at position 261, and to determine its potential role in renal water balance regulation, because data on AQP2 in cattle are scarce, and the mechanisms regulating its expression and cellular localization remain unclear. The analyses were carried out on kidneys collected from eight Polish Holstein-Friesian Black-and-White male calves, aged 5–7 months. It was found, using immunohistochemistry and commercially available phosphospecific antibodies, that in cattle AQP2 Ser-261 is located exclusively in the apical plasma membrane of the principal cells of the collecting duct. This atypical location of AQP2 Ser-261 allows to conclude that it may play a significant role in the process of renal water retention. The results of our previous studies on the regulation of renal total AQP2 excretion with urine in calves, as well as the bioinformatic analysis of available data presented in this study, seem to support this assumption. In addition, bioinformatic tools predicted mitogen activated protein kinases (MAPK) as a possible vasopressin-independent factor involved in AQP2 Ser-261 phosphorylation and accumulation in the apical plasma membrane.
Over the past ten years, proteomic tools have been extensively used in various studies aimed at a better understanding of fish biology and aquaculture. A variety of post-genomic techniques have been developed and adapted for protein profiling of complex biological samples, such as tissues. This review will discuss the applications of expression proteomics in fish health monitoring with regard to nutritional and environmental changes, as well as bacterial or viral infection, in selected tissues relevant to fish physiology, i.e. the kidney, brain, blood plasma, and liver.
The present study was undertaken to determine blood plasma protein and lipid profile changes in healthy Polish Holstein-Fresian calves of Black-and-White variety. Blood was drawn immediately after birth, before first colostrum intake and at the 3rd, 6th, 12th, 24th, 36th, 48th and 72nd hour of life. Subsequent four blood samples were collected at 24 hour intervals until the 7th day of life. Plasma proteins within the isoelectric point ranging from 3.0 to 10.0 were separated using high resolution two-dimensional electrophoresis. Among the 74 protein spots detected and analyzed, 16 were significantly altered during the first week of life. Differentially expressed spots were excised from the gels and subjected to peptide mass fingerprinting using MALDI-TOF MS. In total, 12 spots were successfully identified, which correspond to three proteins, namely: apolipoprotein A-I, apolipoprotein A-IV and fibrinogen gamma-B chain. A gradual increase in plasma triglyceride, total cholesterol, HDL and LDL cholesterol values was shown during the first seven days of calves life. The lowest concentration of these indicators were observed at birth and was followed by a rapid increase during the first week of postnatal life. These changes appear to be related to the transition in energy sources, from a maternal nutrient supply comprising mainly carbohydrates and amino acids to a diet which was rich in fat – colostrum and milk. This was reflected by the intense up-regulation of plasma proteins related with lipid transport and lipoprotein metabolism during the first week of life.
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