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Objective To find a better composition substitution fluid for continuous venovenous hemofiltration (CWH) comparing with the Port's composition substitution fluid,and to evaluate its efficiency and prognosis on patients with dysfunction of glycometabolism and multiple organ dysfunction syndrome (MODS) caused by trauma. Method Totol of 134 patients in the Firist Affiliated Hospotal of the Fourth Miliatary Medicial University,with glycometabolism dysfunction and MODS caused by trauma between Janurary 2001 and December 2006 were treated with CVVH.They were divided into two groups:the Port's composition substitution fluid which glucose concentration was 59.1 mmoL/L (group A,59 cases) and the new substitution fluid which glucose concentration is 11.8 mmol/L (group B,75 cases).The changes of electrolytes,arterial blood gas analysis,blood glucose and osmolarity during CVVH were observed.Results The mortality in group A was significantly higher than that in group B (64.4 % vs 40.0 %,P = 0.005).Before treated with CVVH,there was no significant differences of APACHEⅡscores between group A and group B.Either in the survival patients or in non-survivors,the APACHEⅡscores in group B were significantly higher than that in group A (P
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1 ml/kg)and the ICU stay.Results The hospital mortality of AKI phaseⅢwas significantly higher than that of AKI phaseⅠorⅡ(P
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<p><b>BACKGROUND</b>Human urate anion exchanger (hURAT1) as a major urate transporter expressed on renal tubular epithelial cells regulates blood urate level by reabsorbing uric acid. Antibody is an important tool to study hURAT1. This study aimed, by genetic immunization, to produce mouse anti-hURAT1 polyclonal antibody with high throughput and high specificity and to detect the location of hURAT1 in human kidney.</p><p><b>METHODS</b>Human renal total RNA was isolated and the entire cDNA of hURAT1 was amplified by RT-PCR. The sequence of intracellular high antigenicity fragment (A280 to R349) was chosen by prediction software of protein antigenicity, and its cDNA was amplified from cDNA of hURAT1, and then cloned into pBQAP-TT vector to construct recombinant plasmid pBQAP-TT-hURAT1-210 for genetic immunization. Mice were inoculated with this recombinant plasmid and two other adjuvant plasmids, pCMVi-GMCSF and pCMVi-Flt3L, which helped to enhance the antibody's generation. After four weeks, the mice were sacrificed to obtain the anti-hURAT1 antibody from serum. The antibody was identified by western blot analysis and immunohistochemistry. At the same time, rabbit anti-hURAT1 antibody was produced by protein immunization. The specificity and efficiency between the rabbit and mouse anti-hURAT1 antibody were compared by western blot analysis and immunohistochemistry.</p><p><b>RESULTS</b>The entire cDNA of hURAT1 and cDNA of its intracellular high immunogenic fragment were amplified successfully. Recombinant plasmid pBQAP-TT-hURAT1-210 for genetic immunization was confirmed by restriction digestion and sequencing. Both the mouse anti-hURAT1 antibody and rabbit anti-hURAT1 antibody recognized 58 kD hURAT1 and 64 kD glycosylated hURAT1 protein bands in western blot. Immunohistochemically, hURAT1 was located at the brush border membrane of renal proximal tubular cells. In addition, the throughput and specificity of the mouse anti-hURAT1 antibody were higher than those of the rabbit anti-hURAT1 antibody.</p><p><b>CONCLUSION</b>Genetic immunization can generate anti-hURAT1 polyclonal antibody of high throughput and specificity.</p>