author_facet Chen, Hong-Min
Dai, Jia-Jia
Zhu, Rui
Sang, Xue-Yu
Peng, Fang-Fang
Yu, Hong
Zhang, Bai-Fang
Chen, Hong-Min
Dai, Jia-Jia
Zhu, Rui
Sang, Xue-Yu
Peng, Fang-Fang
Yu, Hong
Zhang, Bai-Fang
author Chen, Hong-Min
Dai, Jia-Jia
Zhu, Rui
Sang, Xue-Yu
Peng, Fang-Fang
Yu, Hong
Zhang, Bai-Fang
spellingShingle Chen, Hong-Min
Dai, Jia-Jia
Zhu, Rui
Sang, Xue-Yu
Peng, Fang-Fang
Yu, Hong
Zhang, Bai-Fang
Bioscience Reports
RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
Cell Biology
Molecular Biology
Biochemistry
Biophysics
author_sort chen, hong-min
spelling Chen, Hong-Min Dai, Jia-Jia Zhu, Rui Sang, Xue-Yu Peng, Fang-Fang Yu, Hong Zhang, Bai-Fang 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20192759 <jats:title>Abstract</jats:title> <jats:p>High glucose (HG)-induced mitochondrial dynamic changes and oxidative damage are closely related to the development and progression of diabetic kidney disease (DKD). Recent studies suggest that regulators of calcineurin 1 (RCAN1) is involved in the regulation of mitochondrial function in different cell types, so we investigate the role of RCAN1 in mitochondrial dynamics under HG ambience in rat glomerular mesangial cells (MCs). MCs subjected to HG exhibited an isoform-specific up-regulation of RCAN1.4 at both mRNA and protein levels. RCAN1.4 overexpression induced translocation of Dynamin related protein 1 (Drp1) to mitochondria, mitochondrial fragmentation and depolarization, accompanied by increased matrix production under normal glucose and HG ambience. In contrast, decreasing the expression of RCAN1.4 by siRNA inhibited HG-induced mitochondrial fragmentation and matrix protein up-regulation. Moreover, both mitochondrial fission inhibitor Mdivi-1 and Drp1 shRNA prevented RCAN1.4-induced fibronectin up-regulation, suggesting that RCAN1.4-induced matrix production is dependent on its modulation of mitochondrial fission. Although HG-induced RCAN1.4 up-regulation was achieved by activating calcineurin, RCAN1.4-mediated mitochondrial fragmentation and matrix production is independent of calcineurin activity. These results provide the first evidence for the HG-induced RCAN1.4 up-regulation involving increased mitochondrial fragmentation, leading to matrix protein up-regulation.</jats:p> RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells Bioscience Reports
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publisher Portland Press Ltd.
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series Bioscience Reports
source_id 49
title RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_unstemmed RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_full RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_fullStr RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_full_unstemmed RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_short RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_sort rcan1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
topic Cell Biology
Molecular Biology
Biochemistry
Biophysics
url http://dx.doi.org/10.1042/bsr20192759
publishDate 2020
physical
description <jats:title>Abstract</jats:title> <jats:p>High glucose (HG)-induced mitochondrial dynamic changes and oxidative damage are closely related to the development and progression of diabetic kidney disease (DKD). Recent studies suggest that regulators of calcineurin 1 (RCAN1) is involved in the regulation of mitochondrial function in different cell types, so we investigate the role of RCAN1 in mitochondrial dynamics under HG ambience in rat glomerular mesangial cells (MCs). MCs subjected to HG exhibited an isoform-specific up-regulation of RCAN1.4 at both mRNA and protein levels. RCAN1.4 overexpression induced translocation of Dynamin related protein 1 (Drp1) to mitochondria, mitochondrial fragmentation and depolarization, accompanied by increased matrix production under normal glucose and HG ambience. In contrast, decreasing the expression of RCAN1.4 by siRNA inhibited HG-induced mitochondrial fragmentation and matrix protein up-regulation. Moreover, both mitochondrial fission inhibitor Mdivi-1 and Drp1 shRNA prevented RCAN1.4-induced fibronectin up-regulation, suggesting that RCAN1.4-induced matrix production is dependent on its modulation of mitochondrial fission. Although HG-induced RCAN1.4 up-regulation was achieved by activating calcineurin, RCAN1.4-mediated mitochondrial fragmentation and matrix production is independent of calcineurin activity. These results provide the first evidence for the HG-induced RCAN1.4 up-regulation involving increased mitochondrial fragmentation, leading to matrix protein up-regulation.</jats:p>
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author Chen, Hong-Min, Dai, Jia-Jia, Zhu, Rui, Sang, Xue-Yu, Peng, Fang-Fang, Yu, Hong, Zhang, Bai-Fang
author_facet Chen, Hong-Min, Dai, Jia-Jia, Zhu, Rui, Sang, Xue-Yu, Peng, Fang-Fang, Yu, Hong, Zhang, Bai-Fang, Chen, Hong-Min, Dai, Jia-Jia, Zhu, Rui, Sang, Xue-Yu, Peng, Fang-Fang, Yu, Hong, Zhang, Bai-Fang
author_sort chen, hong-min
container_issue 1
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container_title Bioscience Reports
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description <jats:title>Abstract</jats:title> <jats:p>High glucose (HG)-induced mitochondrial dynamic changes and oxidative damage are closely related to the development and progression of diabetic kidney disease (DKD). Recent studies suggest that regulators of calcineurin 1 (RCAN1) is involved in the regulation of mitochondrial function in different cell types, so we investigate the role of RCAN1 in mitochondrial dynamics under HG ambience in rat glomerular mesangial cells (MCs). MCs subjected to HG exhibited an isoform-specific up-regulation of RCAN1.4 at both mRNA and protein levels. RCAN1.4 overexpression induced translocation of Dynamin related protein 1 (Drp1) to mitochondria, mitochondrial fragmentation and depolarization, accompanied by increased matrix production under normal glucose and HG ambience. In contrast, decreasing the expression of RCAN1.4 by siRNA inhibited HG-induced mitochondrial fragmentation and matrix protein up-regulation. Moreover, both mitochondrial fission inhibitor Mdivi-1 and Drp1 shRNA prevented RCAN1.4-induced fibronectin up-regulation, suggesting that RCAN1.4-induced matrix production is dependent on its modulation of mitochondrial fission. Although HG-induced RCAN1.4 up-regulation was achieved by activating calcineurin, RCAN1.4-mediated mitochondrial fragmentation and matrix production is independent of calcineurin activity. These results provide the first evidence for the HG-induced RCAN1.4 up-regulation involving increased mitochondrial fragmentation, leading to matrix protein up-regulation.</jats:p>
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spelling Chen, Hong-Min Dai, Jia-Jia Zhu, Rui Sang, Xue-Yu Peng, Fang-Fang Yu, Hong Zhang, Bai-Fang 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20192759 <jats:title>Abstract</jats:title> <jats:p>High glucose (HG)-induced mitochondrial dynamic changes and oxidative damage are closely related to the development and progression of diabetic kidney disease (DKD). Recent studies suggest that regulators of calcineurin 1 (RCAN1) is involved in the regulation of mitochondrial function in different cell types, so we investigate the role of RCAN1 in mitochondrial dynamics under HG ambience in rat glomerular mesangial cells (MCs). MCs subjected to HG exhibited an isoform-specific up-regulation of RCAN1.4 at both mRNA and protein levels. RCAN1.4 overexpression induced translocation of Dynamin related protein 1 (Drp1) to mitochondria, mitochondrial fragmentation and depolarization, accompanied by increased matrix production under normal glucose and HG ambience. In contrast, decreasing the expression of RCAN1.4 by siRNA inhibited HG-induced mitochondrial fragmentation and matrix protein up-regulation. Moreover, both mitochondrial fission inhibitor Mdivi-1 and Drp1 shRNA prevented RCAN1.4-induced fibronectin up-regulation, suggesting that RCAN1.4-induced matrix production is dependent on its modulation of mitochondrial fission. Although HG-induced RCAN1.4 up-regulation was achieved by activating calcineurin, RCAN1.4-mediated mitochondrial fragmentation and matrix production is independent of calcineurin activity. These results provide the first evidence for the HG-induced RCAN1.4 up-regulation involving increased mitochondrial fragmentation, leading to matrix protein up-regulation.</jats:p> RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells Bioscience Reports
spellingShingle Chen, Hong-Min, Dai, Jia-Jia, Zhu, Rui, Sang, Xue-Yu, Peng, Fang-Fang, Yu, Hong, Zhang, Bai-Fang, Bioscience Reports, RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells, Cell Biology, Molecular Biology, Biochemistry, Biophysics
title RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_full RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_fullStr RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_full_unstemmed RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_short RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_sort rcan1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
title_unstemmed RCAN1.4 mediates high glucose-induced matrix production by stimulating mitochondrial fission in mesangial cells
topic Cell Biology, Molecular Biology, Biochemistry, Biophysics
url http://dx.doi.org/10.1042/bsr20192759