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- 저자 : ( Yechan Joh ) (검색결과 3 건)
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Mitochondrial Complex I Inhibition Accelerates Amyloid Toxicity
Yechan Joh,Won-Seok Choi 한국발생생물학회 2017 발생과 생식 Vol.21 No.4
Alzheimer's disease (AD) is neurodegenerative disease, characterized by the progressive decline of memory, cognitive functions, and changes in personality. The major pathological features in postmortem brains are neurofibrillary tangles and amyloid beta (Aβ) deposits. The majority of AD cases are sporadic and age-related. Although AD pathogenesis has not been established, aging and declining mitochondrial function has been associated. Mitochondrial dysfunction has been observed in AD patients' brains and AD mice models, and the mice with a genetic defect in mitochondrial complex I showed enhanced Aβ level in vivo. To elucidate the role of mitochondrial complex I in AD, we used SH-SY5Y cells transfected with DNA constructs expressing human amyloid precursor protein (APP) or human Swedish APP mutant (APP-swe). The expression of APP-swe increased the level of Aβ protein in comparison with control. When complex I was inhibited by rotenone, the increase of ROS level was remarkably higher in the cells overexpressing APP-swe compared to control. The number of dead cell was significantly increased in APP-swe-expressing cells by complex I inhibition. We suggest that complex I dysfunction accelerate amyloid toxicity and mitochondrial complex I dysfunction in aging may contribute to the pathogenesis of sporadic AD.
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Mitochondrial Complex I Inhibition Accelerates Amyloid Toxicity
Joh, Yechan,Choi, Won-Seok The Korean Society of Developmental Biology 2017 발생과 생식 Vol.21 No.4
Alzheimer's disease (AD) is neurodegenerative disease, characterized by the progressive decline of memory, cognitive functions, and changes in personality. The major pathological features in postmortem brains are neurofibrillary tangles and amyloid beta ($A{\beta}$) deposits. The majority of AD cases are sporadic and age-related. Although AD pathogenesis has not been established, aging and declining mitochondrial function has been associated. Mitochondrial dysfunction has been observed in AD patients' brains and AD mice models, and the mice with a genetic defect in mitochondrial complex I showed enhanced $A{\beta}$ level in vivo. To elucidate the role of mitochondrial complex I in AD, we used SH-SY5Y cells transfected with DNA constructs expressing human amyloid precursor protein (APP) or human Swedish APP mutant (APP-swe). The expression of APP-swe increased the level of $A{\beta}$ protein in comparison with control. When complex I was inhibited by rotenone, the increase of ROS level was remarkably higher in the cells overexpressing APP-swe compared to control. The number of dead cell was significantly increased in APP-swe-expressing cells by complex I inhibition. We suggest that complex I dysfunction accelerate amyloid toxicity and mitochondrial complex I dysfunction in aging may contribute to the pathogenesis of sporadic AD.
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( Yong Feng He ),( Hang Gun Kim ),( Tae Yong Ryu ),( Kwang Youl Lee ),( Won Seok Choi ),( Kyeong Man Kim ),( Mei Zheng ),( Yechan Joh ),( Jae Hyuk Lee ),( Dong Deuk Kwon ),( Qun Lu ),( Kwonseop Kim ) 전남대학교 약품개발연구소 2014 약품개발연구지 Vol.23 No.-
&-catenin was first considered as a brain spedfic protein, strong evidence of&-catenin overexpression in various cancers, including prostate cancer, has been accumulated. Phosphorylation of a-catenin by Akt and GSK313 has been studied in various cell lines. However, tyrosine phosphorylation of &-catenin in prostate cancer cells remains unknown. In the current study, we demonstrated that Src kinase itself phosphorylates &-catenin on its tyrosine residues in prostate cancer cells and further illustrated that Yl073, Yll12 and Yl176 of &-catenin are predominant sites responsible for tyrosine phosphorylation mediated by c-Src. Apart from c-Src, other Src family kinases, including Fgr, Fyn and Lyn, can also phosphorylate a-catenin. We also found that c-Src-mediated Tyr-phosphorylation of &-catenin increases its stability via decreasing its affinity to GSK313 and enhances its ability of indudng nuclear distribution of j3-catenin through interrupting the integrity of the E-cadherin. Taken together, these results indicate that c-Src can enhance the oncogenic function of&-catenin in prostate cancer cells. ⓒ 2013 Elsevier B.V. All rights reserved.
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