Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Bon-Hyeock Koo"'
Autor:
Bon-hyeock Koo, Yeon-Ju Lee, Na Rae Park, Su Chin Heo, David M. Hudson, Aysel A. Fernandes, Chet S. Friday, Michael W. Hast, David T. Corr, Douglas R. Keene, Sara F. Tufa, Nathaniel A. Dyment, Kyu Sang Joeng
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-14 (2024)
Abstract The biological mechanisms regulating tenocyte differentiation and morphological maturation have not been well-established, partly due to the lack of reliable in vitro systems that produce highly aligned collagenous tissues. In this study, we
Externí odkaz:
https://doaj.org/article/cce7e84906324ac18d089ea546ee2e81
Autor:
Tae Kyeong Kim, Sejin Jeon, Seonjun Park, Seong-Keun Sonn, Seungwoon Seo, Joowon Suh, Jing Jin, Hyae Yon Kweon, Sinai Kim, Shin Hye Moon, Okhee Kweon, Bon-Hyeock Koo, Nayoung Kim, Hae-Ock Lee, Young-Myeong Kim, Young-Joon Kim, Sung Ho Park, Goo Taeg Oh
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-19 (2022)
Maintaining optimal eNOS levels is important during cardiovascular events, although little is known regarding the mechanism of eNOS protection. Here, the authors show a regulatory role of endothelial OASL1 in maintaining eNOS mRNA stability and vascu
Externí odkaz:
https://doaj.org/article/40c92b716381415c80e90e99dcd018a0
Autor:
Bon-hyeock Koo, Dongeui Hong, Hyeon Don Hong, Hyun Kyo Lim, Kwang Lae Hoe, Moo-Ho Won, Young Myeong Kim, Dan E. Berkowitz, Sungwoo Ryoo
Publikováno v:
Experimental and Molecular Medicine, Vol 51, Iss 6, Pp 1-12 (2019)
Vascular disease: Controlling arterial constriction Researchers have illuminated how a protein, arginase II (ArgII), is involved in development of vascular diseases such as atherosclerosis, or narrowing of the arteries by plaque deposits. Blood vesse
Externí odkaz:
https://doaj.org/article/9abe9aa87a9c496e8d460058ef7359bc
Publikováno v:
Cells, Vol 9, Iss 2, p 392 (2020)
Arginase II reciprocally regulates endothelial nitric oxide synthase (eNOS) through a p32-dependent Ca2+ control. We investigated the signaling pathway of arginase II-dependent eNOS phosphorylation. Western blot analysis was applied for examining pro
Externí odkaz:
https://doaj.org/article/bb509a3e44964610beb5b0fa3f26e0c7
Autor:
Bon‐Hyeock Koo, Hye‐Mi Hwang, Bong‐Gu Yi, Hyun Kyo Lim, Byeong Hwa Jeon, Kwang Lae Hoe, Young‐Guen Kwon, Moo‐Ho Won, Young Myeong Kim, Dan E. Berkowitz, Sungwoo Ryoo
Publikováno v:
Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, Vol 7, Iss 18 (2018)
Background Arginase II activity contributes to reciprocal regulation of endothelial nitric oxide synthase (eNOS). We tested the hypotheses that arginase II activity participates in the regulation of Ca2+/Ca2+/calmodulin‐dependent kinase II/eNOS act
Externí odkaz:
https://doaj.org/article/1dae1012683042eebada206f0a47a565
Publikováno v:
BMB Reports. 54:516-521
Although arginase primarily participates in the last reaction of the urea cycle, we have previously demonstrated that arginase II is an important cytosolic calcium regulator through spermine production in a p32-dependent manner. Here, we demonstrated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5badf86caa6a3fc3578ef150ef4bac67
https://doi.org/10.5483/bmbrep.2021.54.10.053
https://doi.org/10.5483/bmbrep.2021.54.10.053
Publikováno v:
Cardiovascular Research. 118:1344-1358
Aims Arginase II (ArgII) plays a key role in the regulation of Ca2+ between the cytosol and mitochondria in a p32-dependent manner. p32 contributes to endothelial nitric oxide synthase (eNOS) activation through the Ca2+/CaMKII/AMPK/p38MAPK/Akt signal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28f3e665edb309025851dc086aa4a0ea
https://doi.org/10.1093/cvr/cvab163
https://doi.org/10.1093/cvr/cvab163
Autor:
Byung Hwa Jeon, Hyun Kyo Lim, Kwanhoon Choi, Bon Hyeock Koo, Ji Young Mun, Young Myeong Kim, Minkyo Jung, Hye Young Yun, Moo Ho Won, Sungwoo Ryoo, Byeong Jun Yoon
Publikováno v:
Molecular Medicine Reports
The p32 protein plays a crucial role in the regulation of cytosolic Ca2+ concentrations ([Ca2+]c) that contributes to the Ca2+-dependent signaling cascade. Using an adenovirus and plasmid p32-overexpression system, the aim of the study was to evaluat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::250b9dbebbdde298d6e77f86d1186c26
http://europepmc.org/articles/PMC7411372
http://europepmc.org/articles/PMC7411372
Autor:
Tae Kyeong Kim, Sejin Jeon, Seonjun Park, Seong-Keun Sonn, Seungwoon Seo, Joowon Suh, Jing Jin, Hyae Yon Kweon, Sinai Kim, Shin Hye Moon, Okhee Kweon, Bon-Hyeock Koo, Nayoung Kim, Hae-Ock Lee, Young-Myeong Kim, Young-Joon Kim, Sung Ho Park, Goo Taeg Oh
Publikováno v:
Nature communications. 13(1)
Endothelial nitric oxide synthase (eNOS) decreases following inflammatory stimulation. As a master regulator of endothelial homeostasis, maintaining optimal eNOS levels is important during cardiovascular events. However, little is known regarding the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af8b1efa86140b29b71e02c312968c3
https://pubmed.ncbi.nlm.nih.gov/36333342
https://pubmed.ncbi.nlm.nih.gov/36333342
Autor:
Moo-Ho Won, Young Myeong Kim, Dan E. Berkowitz, Hyun Kyo Lim, Dongeui Hong, Hyeon Hong, Bon-Hyeock Koo, Kwang Lae Hoe, Sungwoo Ryoo
Publikováno v:
Experimental and Molecular Medicine, Vol 51, Iss 6, Pp 1-12 (2019)
Although arginase II (ArgII) is abundant in mitochondria, Ca2+-accumulating organelles, the relationship between ArgII activity and Ca2+ translocation into mitochondria and the regulation of cytosolic Ca2+ signaling are completely unknown. We investi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bbbcc876ca76f6bdd0e114b3dbf5f20
https://doaj.org/article/9abe9aa87a9c496e8d460058ef7359bc
https://doaj.org/article/9abe9aa87a9c496e8d460058ef7359bc