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Jung-Min Koh Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Young-Sun Lee Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Chang-Hyun Byun Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Eun-Ju Chang Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Hyunsoo Kim Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Yong Hee Kim Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Hong-Hee Kim Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Ghi Su Kim Division of Endocrinology and Metabolism, Asan Medical Center, University of Ulsan College of Medicine, Seoul 138-736, Republic of Korea
Asan Institute for Life Sciences, Seoul, Republic of Korea
Department of Cell and Developmental Biology, Dental Research Institute, Seoul National University, Seoul, Republic of Korea
Department of Thoracic and Cardiovascular Surgery, University of Ulsan College of Medicine, Asan Medical Center, Seoul, Republic of Korea

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Growing evidence has shown a biochemical link between increased oxidative stress and reduced bone density. Although α-lipoic acid (α-LA) has been shown to act as a thiol antioxidant, its effect on bone cells has not been determined. Using proteomic analysis, we identified six differentially expressed proteins in the conditioned media of α-LA-treated human bone marrow stromal cell line (HS-5). One of these proteins, receptor activator of nuclear factor κB ligand (RANKL), was significantly up-regulated, as confirmed by immunoblotting with anti-RANKL antibody. ELISA showed that α-LA stimulated RANKL production in cellular extracts (membranous RANKL) about 5-fold and in conditioned medium (soluble RANKL) about 23-fold, but had no effect on osteoprotegerin (OPG) secretion. Despite increasing the RANKL/OPG ratio, α-LA showed a dose-dependent suppression of osteoclastogenesis, both in a coculture system of mouse bone marrow cells and osteoblasts and in a mouse bone marrow cell culture system, and reduced bone resorption in a dose-dependent manner. In addition, α-LA-induced soluble RANKL was not inhibited by matrix metalloprotease inhibitors, indicating that soluble RANKL is produced by α-LA without any posttranslational processing. In contrast, α-LA had no significant effect on the proliferation and differentiation of HS-5 cells. These results suggest that α-LA suppresses osteoclastogenesis by directly inhibiting RANKL–RANK mediated signals, not by mediating cellular RANKL production. In addition, our findings indicate that α-LA-induced soluble RANKL is not produced by shedding of membranous RANKL.

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Seul Gi Kang Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea
Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea

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Hyon-Seung Yi Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Min Jeong Choi Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea
Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea

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Min Jeong Ryu Peptron, Inc., Daejeon, Korea

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Saetbyel Jung Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Hyo Kyun Chung Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Joon Young Chang Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea
Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea

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Yong Kyung Kim Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Seong Eun Lee Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea
Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea

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Hyeon-Woo Kim Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea
Department of Medical Science, Chungnam National University School of Medicine, Daejeon, Korea

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Hoil Choi Department of Biochemistry, Chungnam National University School of Medicine, Daejeon, Korea

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Dong Seok Kim Department of Biochemistry, Chungnam National University School of Medicine, Daejeon, Korea

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Ju Hee Lee Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Koon Soon Kim Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Hyun Jin Kim Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Chul-Ho Lee Animal Model Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Korea

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Yuichi Oike Department of Molecular Genetics, Graduate School of Medical Sciences, Kumamoto University, Chuo-ku, Kumamoto, Japan

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Minho Shong Research Center for Endocrine and Metabolic Diseases, Chungnam National University School of Medicine, Daejeon, Korea

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Recent studies revealed that the inhibition of mitochondrial oxidative phosphorylation (OXPHOS) is coupled with the mitochondrial unfolded protein response, thereby stimulating the secretion of non-cell autonomous factors, which may control systemic energy metabolism and longevity. However, the nature and roles of non-cell autonomous factors induced in adipose tissue in response to reduced OXPHOS function remain to be clarified in mammals. CR6-interacting factor 1 (CRIF1) is an essential mitoribosomal protein for the intramitochondrial production of mtDNA-encoded OXPHOS subunits. Deficiency of CRIF1 impairs the proper formation of the OXPHOS complex, resulting in reduced function. To determine which secretory factors are induced in response to reduced mitochondrial OXPHOS function, we analyzed gene expression datasets in Crif1-depleted mouse embryonic fibroblasts. Crif1 deficiency preferentially increased the expression of angiopoietin-like 6 (Angptl6) and did not affect other members of the ANGPTL family. Moreover, treatment with mitochondrial OXPHOS inhibitors increased the expression of Angptl6 in cultured adipocytes. To confirm Angptl6 induction in vivo, we generated a murine model of reduced mitochondrial OXPHOS function using adipose tissue-specific Crif1-deficient mice and verified the upregulation of Angptl6 and fibroblast growth factor 21 (Fgf21) in white adipose tissue. Treatment with recombinant ANGPTL6 protein increased oxygen consumption and Pparα expression through the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway in cultured adipocytes. Furthermore, the ANGPTL6-mediated increase in Pparα expression resulted in increased FGF21 expression, thereby promoting β-oxidation. In conclusion, mitochondrial OXPHOS function governs the expression of ANGPTL6, which is an essential factor for FGF21 production in adipose tissue and cultured adipocytes.

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