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RISS 인기검색어
- 검색키워드
- 저자 : Lihua Shao (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
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Effect of Micronutrient Supplementation on the Growth of Preschool Children in China
Han, Junhua,Yang, Yuexin,Shao, Xiaoping,He, Mei,Bian, Lihua,Wang, Zhu The Korean Nutrition Society 2002 Nutritional Sciences Vol.5 No.3
The purpose of this study was to investigate the effects of micronutrient supplementation on the growth of preschool children in China. A double-blind, placebo-controlled trial was conducted on 156 growth retarded preschool children who were randomly assigned to the following five groups : supplemental control (S-control; n=28); zinc supplementation (+Zn; 3.5mg Zn/day, n=34); zinc and calcium supplementation (+ZnCa; 3.5mg Zn + 250mg Ca/day, n=37); zinc, calcium and vitamin A supplementation (+ZnCaVA; 3.5mgZn + 250mgCa + 200gVA/day, n=28); and calcium and vitamin A supplementation (+CaVA; 250mgCa + 200gVA/day, n=29). Another 34 children of normal height were selected as a normal control (N-control). Supplementation continued for twelve months. After supplementation, the height gains in the +Zn group (7.84cm per year) and the +ZnCa group (7.70 cm per year) were significantly higher than that in the S-control group (6.74 cm per year, P<0.05). The weight gain in the +ZnCaVA group (2.55kg per year) and the +CaVA group (2.57 kg per year) was also significantly higher than that in the S-control group (2.19 kg per year, P<0.05). The average number of days of illness in each group taking supplements was lower than that in the S-control group (13 days per year compared with 23 days per year). No significant differences in bone maturity were observed between the groups. In conclusion, in this study Zinc and Zinc + Calcium supplementation improved the height gain, and vitamin A improved the weight gain, in growth retarded preschool children, but these supplements did not affect the maturity of bone. Micronutrient supplementation also lowered the morbidity of these children.
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Zheng, Feng,Ma, Lixian,Shao, Lihua,Wang, Gang,Chen, Fengzhe,Zhang, Ying,Yang, Song The Microbiological Society of Korea 2007 The journal of microbiology Vol.45 No.1
The Hantaan virus (HTNV) is an enveloped virus that is capable of inducing low pH-dependent cell fusion. We molecularly cloned the viral glycoprotein (GP) and nucleocapsid (NP) cDNA of HTNV and expressed them in Vero E6 cells under the control of a CMV promoter. The viral gene expression was assessed using an indirect immunofluorescence assay and immunoprecipitation. The transfected Vero E6 cells expressing GPs, but not those expressing NP, fused and formed a syncytium following exposure to a low pH. Monoclonal antibodies (MAbs) against envelope GPs inhibited cell fusion, whereas MAbs against NP did not. We also investigated the N-linked glycosylation of HTNV GPs and its role in cell fusion. The envelope GPs of HTNV are modified by N-linked glycosylation at five sites: four sites on G1 (N134, N235, N347, and N399) and one site on G2 (N928). Site-directed mutagenesis was used to construct eight GP gene mutants, including five single N-glycosylation site mutants and three double-site mutants, which were then expressed in Vero E6 cells. The oligosaccharide chain on residue N928 of G2 was found to be crucial for cell fusion after exposure to a low pH. These results suggest that G2 is likely to be the fusion protein of HTNV.
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Feng Zheng,Lixian Ma,Lihua Shao,Gang Wang,Fengzhe Chen,Ying Zhang,Song Yang 한국미생물학회 2007 The journal of microbiology Vol.45 No.1
The Hantaan virus (HTNV) is an enveloped virus that is capable of inducing low pH-dependent cell fusion. We molecularly cloned the viral glycoprotein (GP) and nucleocapsid (NP) cDNA of HTNV and expressed them in Vero E6 cells under the control of a CMV promoter. The viral gene expression was assessed using an indirect immunofluorescence assay and immunoprecipitation. The transfected Vero E6 cells expressing GPs, but not those expressing NP, fused and formed a syncytium following exposure to a low pH. Monoclonal antibodies (MAbs) against envelope GPs inhibited cell fusion, whereas MAbs against NP did not. We also investigated the N-linked glycosylation of HTNV GPs and its role in cell fusion. The envelope GPs of HTNV are modified by N-linked glycosylation at five sites: four sites on G1 (N134, N235, N347, and N399) and one site on G2 (N928). Site-directed mutagenesis was used to construct eight GP gene mutants, including five single N-glycosylation site mutants and three double-site mutants, which were then expressed in Vero E6 cells. The oligosaccharide chain on residue N928 of G2 was found to be crucial for cell fusion after exposure to a low pH. These results suggest that G2 is likely to be the fusion protein of HTNV.
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