| 1 | Hyperglycemia induces protein nonenzymeatic glycosylation in brain neurons of diabetic rats at early stage显示文摘BACKGROUND: Protein nonenzymatic glycosylation is supposed to be one of mechanisms for chronic complications development in diabetes mellitus, and therefore, might play an important role in the neuronal degeneration. OBJECTIVE: To study the protein nonenzymatic glycosylation in brain neurons of diabetic rats, and to analyze the pathway of neuronal degeneration at the early stage of hyperglymecia. DESIGN: Randomized controlled animal experiment. SETTING: Department of Endocrinology, First hospital Affiliated to General Hospital of Chinese PLA and Beijing Laboratory for Brain Aging, Xuanwu Hospital Affiliated to Capital Medical University. MATERIALS: Thirty-five male Wistar rats (grade Ⅱ), aged 3 months old, and 11 male purebred Kunming mice (grade Ⅲ) without special pathogen, aged 3 months old, were provided by the Animal Room of Capital Medical University. METHODS: This experiment was carried out in the Beijing Laboratory for Brain Aging, Xuanwu Hospital Affiliated to Capital Medical University in 1998. The rats in the diabetic model group were intraperitoneally injected into 10 g/L STZ according to 60 mg/kg to establish rat models of diabetes mellitus. The blood glucose and body mass of rats in each group were determined respectively at 1, 2 and 3 months after modeling. The antibodies of advanced glycosylation end products (AGEs) of bovine serum albumin (anti-BSA) were self-prepared: ①The antigen of AGEs-BSA was prepared.②Eleven male Kuming mice (grade Ⅱ) of 3 months old without special pathogen were selected to inoculate AGEs-BSA. ③ The animals were immunized. ④Primary purification and detection of poly-antibodies of AGEs: the AGEs were performed immunohistochemical examination at 1 month after diabetic modeling by ELISA method. MAIN OUTCOME MEASURES: ① Detection results of blood glucose and body mass of rats in two groups at different time points. ② Determination of polyclonal antibody titer of AGEs-BSA. ③ Changes in immunohistochemical image of AGEs in brain tissue of rats in two groups. RESULTS: Thirteen rats in the diabetic model group and fifteen rats in the normal model group entered the stage of final analysis. ①Changes of blood glucose and body mass: At 1, 2 and 3 months after modeling, the blood glucose of rats in the diabetic model group were respectively(28.8±2.8),(23.1±5.5),(25.4± 5.1) mmol/L, which were significantly higher than those in the normal control group [(6.2±0.9),(6.1±0.8), (6.1±0.7) mmol/L,P < 0.01]; At 1, 2 and 3 months after modeling, the body mass of rats in the diabetic model group were respectively (250.1±52.2),(263.8±50.0),(261.5±42.6) g, which were significantly lower than those in the normal control group [(422.6±36.2),(462.6±39.0),(485.0±28.8) g,P < 0.01]. ②Determination of antibody titer of immune serum: The mice were treated by AGEs-BSA of different concentrations twice. After that, the titer of AGEs -BSA was determined, and the results of which indicated that a higher absorbance existed at 1∶1 000. ③Determination of antigen concentration: The final titer of antibody in the abdominal dropsy was determined, and the results of which suggested that there was a much higher absorbance in the AGEs-BSA at the concentration of 5–50 mg/L. ④Determination of antibody titer in abdominal dropsy: The antibody titer in abdominal dropsy was detected by ELISA method with antigen at 20 mg/L, which indicated that the maximum absorbance (1.265±0.039) existed at 1∶4 000, and very larger absorbance (0.982±0.067) at 1∶20 000. The polyclonal antibody of AGEs-BSA was successfully prepared. ⑤Immunohistochemical detection results: The immunohistochemical staining of AGEs showed there were positive neurons in the first month in the diabetic model group, whereas it was not significant in the normalcontrol group. The positive substances were found mainly in the cytoplasm. CONCLUSION: Hyperglycemia at the early stage of diabetes mellitus (1 month after modeling) can lead to protein nonenzymeatic glycosylation in brain neurons, and no obvious reactions mentioned above are found in the normal control group. It suggests that the degenerative changes of tissue structure of central nervous system are related with protein nonenzymeatic glycosylation caused by hyperglycemia. | Jingsheng Hu Xueyi Ma Shuli Sheng | 2007 | Neural Regeneration Research2007，2，1： | 2 |
| 2 | Reconfiguring confined magnetic colloids with tunable fluid transport behavior显示文摘Collective dynamics of confined colloids are crucial in diverse scenarios such as self-assembly and phase behavior in materials science,microrobot swarms for drug delivery and microfluidic control.Yet,fine-tuning the dynamics of colloids in microscale confined spaces is still a formidable task due to the complexity of the dynamics of colloidal suspension and to the lack of methodology to probe colloids in confinement.Here,we show that the collective dynamics of confined magnetic colloids can be finely tuned by external magnetic fields.In particular,the mechanical properties of the confined colloidal suspension can be probed in real time and this strategy can be also used to tune microscale fluid transport.Our experimental and theoretical investigations reveal that the collective configuration characterized by the colloidal entropy is controlled by the colloidal concentration,confining ratio and external field strength and direction.Indeed,our results show that mechanical properties of the colloidal suspension as well as the transport of the solvent in microfluidic devices can be controlled upon tuning the entropy of the colloidal suspension.Our approach opens new avenues for the design and application of drug delivery,microfluidic logic,dynamic fluid control,chemical reaction and beyond. | Zhizhi Sheng Mengchuang Zhang Jing Liu Paolo Malgaretti Jianyu Li Shuli Wang Wei Lv Rongrong Zhang Yi Fan Yunmao Zhang Xinyu Chen Xu Hou | 2021 | National Science Review2021，8，5： | 1 |
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