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《Bioscience, biotechnology, and biochemistry》2013,77(12):2470-2474
β2 integrins (CD11s/CD18) promote the attachment of leukocytes to vascular endothelial cells. We performed in this study sucrose loading to rats with moderate postprandial hyperglycemia with/without once-daily dosing of the α-glucosidase inhibitor, miglitol, for 4 days under 4-h fasting conditions. The streptozotocin (STZ)-treated rats showed moderate postprandial hyperglycemia on days 1 and 4. The gene expression was higher for CD11a with fasting and 3-h postprandial on day 1, and with fasting on day 4, for CD11b with fasting on day 1 and 3-h postprandial on day 4, and for CD18 with fasting on days 1 and 4 in peripheral leukocytes from the STZ-treated rats than in peripheral leukocytes from the saline-treated rats. Miglitol reduced postprandial hyperglycemia and the gene expression of CD11a with fasting and of CD11b 3-h postprandial on day 4. These results indicate that inhibiting postprandial hyperglycemia reduced the mRNA expression of β2 integrins in peripheral leukocytes of moderately postprandial hyperglycemic rats. 相似文献
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氧化葡糖杆菌(Gluconobacter oxydans)来源的山梨醇脱氢酶可催化N-羟乙基葡萄糖胺合成6-脱氧-6-氨基(N-羟乙基)-α-L-呋喃山梨糖,即合成降血糖药物米格列醇的关键中间体。本文采用适应性驯化策略,以甘油为唯一碳源,通过40 g/L、60 g/L、80 g/L和100 g/L甘油梯度连续传代培养,筛选获得了一株以甘油为碳源的高活力菌株G.oxydans A-3-D,扫描电镜结果表明该细胞表面褶皱较原始菌株有显著增加。在80 g/L甘油培养基摇瓶培养24 h后,菌体浓度为4.58 g DCW/L,山梨醇脱氢酶的发酵体积酶活与比酶活分别为原始菌株G.oxydans ZJB-605的1.3倍及1.5倍。此外,在摇瓶培养条件下对影响催化反应进程的关键因素进行了考查,结果表明在摇瓶体系中,G.oxydans A-3-D的最适催化反应条件为80.0 g/L底物、2.0 g DCW/L菌体细胞、20 mmol/L Mg~(2+)浓度,15℃反应48 h后底物转化率达到90.8%,6NSL累积浓度为72.6 g/L,较G.oxydans ZJB-605有显著提升。 相似文献
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《Protein science : a publication of the Protein Society》2018,27(8):1498-1508
Carbohydrate hydrolyzing α‐glucosidases are commonly found in microorganisms present in the human intestine microbiome. We have previously reported crystal structures of an α‐glucosidase from the human gut bacterium Blaubia (Ruminococcus) obeum (Ro‐αG1) and its substrate preference/specificity switch. This novel member of the GH31 family is a structural homolog of human intestinal maltase‐glucoamylase (MGAM) and sucrase–isomaltase (SI) with a highly conserved active site that is predicted to be common in Ro‐αG1 homologs among other species that colonize the human gut. In this report, we present structures of Ro‐αG1 in complex with the antidiabetic α‐glucosidase inhibitors voglibose, miglitol, and acarbose and supporting binding data. The in vitro binding of these antidiabetic drugs to Ro‐αG1 suggests the potential for unintended in vivo crossreaction of the α‐glucosidase inhibitors to bacterial α‐glucosidases that are present in gut microorganism communities. Moreover, analysis of these drug‐bound enzyme structures could benefit further antidiabetic drug development. 相似文献
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