3 research outputs found

    Comparison of Stapler, Single Layer and Double Layer Techniques for Colon Closure in Dogs

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    The present study was performed on 18 healthy dogs (aged 16.80±1.22 months) and body weight (17.07± 2.21 kg) to determine the best suturing technique among single layer, double layer and stapler technique for the closure of colon in dogs. All dog were divided into three groups, placing 6 animals in each group, i.e. group A was closed with single layer suture technique, group B was closed with double layer suture technique and group C was closed with stapler technique. The number of stitches required for colon closure were 8.83, 16.33 and 9.16 in groups –A, B and C respectively. The mean number of stitches and time taken for the completion of double layer technique was significantly higher (P</jats:p

    Heritability Estimates for Some Growth Traits of Dhatti Camel Breed in Tharparkar

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    Purposed study was conducted using 12 sire”s 232 offspring. The parameters were studied birth weight, body weight, weight at 6 month, average daily gain to 6 month, yearling weight, total weight gain from 6 month and average daily gain from 6 month till one year. The results for heritability estimates were analyzed using the variance with unequal subclass numbers by using the data of 12 parental half sib groups. The average numbers of offspring were ranged per sire 3 to 84 with mean of 16.4. The effect of sire was observed significantly higher (P≤.0) in said traits. While the results of heritability estimates were observed low to moderate for birth weight, birth weight at 6 month, average daily gain to 6month, yearling weight, total weight, weight gain to 6 month and average daily gain from six month to 1 year respectively. The results for correlation estimates between these traits were positive and high for bwt with TG6 month and bwt at 6 month with and 6 month to 1 year. It is concluded that values for heritability and correlation were observed in range of other farm animal, while for the better production and higher values selection process is advisable for these traits.</jats:p

    Effect of protein glycation by methylglyoxal on pancreatic beta cell function

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    Methylglyoxal is a physiological dicarbonyl metabolite and potent argininedirected glycating agent. It often modifies proteins at functional sites producing loss of positive charge, structural distortion and inactivation. Plasma methylglyoxal is increased in hyperglycaemia associated with diabetes and is linked to the development of vascular complications of diabetes – particularly nephropathy, retinopathy and neuropathy. The effects of dicarbonyl glycation on beta cells and involvement in early stage dysfunction and development of type 2 diabetes mellitus are not known. The aim of this project was to investigate the effect of dicarbonyl protein glycation on beta cell function and related involvement in the development of diabetes. Studies were performed in an in vitro model of beta cell dysfunction - MIN6 insulinoma cells incubated under low and high glucose concentrations, and in a pre-clinical in vivo model of decline of glucose tolerance preceding development of type 2 diabetes - high fat diet-induced insulin resistant mice. Dicarbonyl metabolism and protein damage by glycation and oxidation were studied by stable isotopic dilution analysis liquid chromatography-tandem mass spectrometry. Localisation of methylglyoxal glycation adducts within the pancreas were visualised by immunostaining. Interactions between the extracellular matrix protein, collagen IV, and MIN6 cells in vitro were investigated and impairments in adhesion were assessed following glycation with methylglyoxal. Impairments in adhesion of MIN6 cells to methylglyoxal-glycated collagen IV were assessed using atomic force microscopy force spectroscopy. The results show that MIN6 cells were resistant to accumulation of methylglyoxal when incubated in high glucose concentration although the flux of methylglyoxal was increased 41%. Glycation of collagen IV by methylglyoxal impairs binding to MIN6 cells in vitro resulting in a 91% decrease in the energy necessary to detach cells from the extracellular matrix protein. In high fat diet fed mice the concentration of methylglyoxal in the pancreas was increased. Visualisation of MG-H1 adduct residues in the pancreas showed they were predominantly on the extracellular matrix. In conclusion, protein glycation by methylglyoxal occurs in MIN6 cells in vitro and in the mouse pancreas in vivo. Although the methylglyoxal concentration in the pancreas of high fat diet fed, insulin resistant mice was increased, the lack of a concurrent increase in methylglyoxal protein glycation adducts suggests there may be increased turnover of methylglyoxal-modified proteins. Impairment of beta cell attachment to the extracellular matrix protein, collagen IV, by methylglyoxal and increased protein turnover stimulated by an increased rate of methylglyoxal glycation may impair beta cell function in pre-diabetes in vivo. Glycation by methylglyoxal may contribute to beta cell glucotoxicity and dysfunction with progression to type 2 diabetes mellitus
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