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RISS 인기검색어
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- 저자 : HAN Jeung Whan (검색결과 110 건)
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數種動物의 膵組織內 Protein Methylases의 活性度 分布에 관한 硏究
李香雨,韓正煥 成均館大學校 科學技術硏究所 1984 論文集 Vol.35 No.1
Post- translational modification of amino acid residue side-chains in protein has come to be a well known biochemical phenomenon. These reactions include methylation, carboxylation, acetylation, phosphorylation, and hydroxylation. One such side-chain modification of protein, protein methylation is being investigated actively with regard to bacterial chemotaxis, cytochrome c, gene regulation, and carnitine biosynthesis. The methylated amino acids occur in nature in highly specialized proteins. These methylated amino acids are formed by reactions catalyzed by protein methylase Ⅰ, Ⅱ and Ⅲ. In recent studies it was reported that protein carboxymethylation is involved in amylase secretion of parotid gland by isoproterenol. It was also suggested that a small part of the total cellular protein carboxymethylation is directly involved in pancreatic enzyme secretion. On the contrary, other authors reported that there is no relationship between protein carboxymethylation and secretion in pancreas and parotid. In this study we first examined the activities of protein methylase I, II, and III in pancreatic tissues of various animals, such as rat, mouse, guinea pig, rabbit, pig, cow, cat, chicken, and frog. The following results were obtained; 1. The activities of protein methylases were generally high in pancreatic tissues of cat, pig, and rabbit. Specifically, the activity of protein methylase I was very high in pancreatic tissue of cat, but low in the tissue of rat. Bovine pancreas had been shown to be the richest source for protein methylase Ⅱ, while the activity of protein methylase Ⅲ was relatively high in pancreatic tissue of cat. 2. The activities of protein methylase Ⅰ, Ⅱ, and Ⅲ in pancreatic tissue of chicken were generally high. 3. Interestingly, the activities of protein methylase Ⅰ, Ⅱ, and Ⅲ were not detected in pancreatic tissue of frog which is amphibian.
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Role of hydrogen peroxide in p70^(s6k) signaling pathway
Han, Jeung-Whan 이화여자대학교 세포신호전달연구센터 2000 고사리 세포신호전달 심포지움 Vol. No.2
We investigated a possible role of reactive oxygen species(ROS) in p70^(s6k) activation, which plays an important role in the progression of cells from G_(0)/G₁ to S phase of the cell cycle by translational upregulation of a family of mRNA transcripts that encode for components of the protein synthetic machinery. Treatment of mouse epidermal cell JB6 with H₂O₂ generated extracellularly by glucose/glucose oxidase led to the activation of p70^(s6k) and p90^(rsk), and to phosphorylation of p42^(mapk)/p44^(mapk). The activation of p70^(s6k) and p90^(rsk) was dose-dependent and transient, maximal activities being in extracts treated for 15 and 30 min, respectively. Further characterization of ROS-induced activation of p70^(s6k) using specific inhibitors for p70^(s6k) signaling pathway, rapamycin and wortmannin, revealed that ROS acted upstream of rapamycin sensitive component FRAP/RAFT, and wortmannin sensitive component PI3K, because both inhibitors caused the inhibition of ROS-induced p70^(s6k) activity. In addition, Ca^(2+) chelation also inhibited ROS-induced activation of p70^(s6k), indicating that Ca^(2+) is a mediator of p70^(s6k) activation by ROS. However, down regulation of TPA-responsive PKC by chronic pretreatment with TPA or a specific PKC inhibitor Ro-31-8220 did not block the activation of p70^(s6k) by ROS, indicating that the activation of TPA-responsive PKC was not required for stimulation of p70^(s6k) activity by H₂O₂ in JB6 cells. Exposure of JB6 cells to PDGF or EGF led to a rapid increase in H₂O₂, phosphorylation, and activation of p70^(s6k), which were antagonized by the pretreatment of catalase. Taken together, the results suggest that ROS act as a messenger in growth factor-induced p70^(s6k) signaling pathway.
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