Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway.
Obesity is a common disease over the world and is tightly associated with diabetes mellitus, cardiovascular and cancer disease. Although our previous study showed that the synthetic vanadium-protein (V-P) complex had a better effect on antioxidant and antidiabetic, the relative molecular mechanisms...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2020-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0239547 |
| _version_ | 1819125736438497280 |
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| author | Shuang Zhang Lei Yan Sang Moo Kim |
| author_facet | Shuang Zhang Lei Yan Sang Moo Kim |
| author_sort | Shuang Zhang |
| collection | DOAJ |
| description | Obesity is a common disease over the world and is tightly associated with diabetes mellitus, cardiovascular and cancer disease. Although our previous study showed that the synthetic vanadium-protein (V-P) complex had a better effect on antioxidant and antidiabetic, the relative molecular mechanisms are still entirely unknown. Hence, we investigated the effect of the synthetic V-P complex on adipocyte differentiation (adipogenesis) using human preadipocytes to clarify its molecular mechanisms of action. The primary human preadipocytes were cultured with and without V-P complex during adipocyte differentiation. The cell proliferation, lipid accumulation, and the protein expression of transcription factors and related enzymes were determined for the differentiated human preadipocytes. In this study, the 20 μg/mL of V-P complex reduced the lipid and triglyceride (TG) content by 74.47 and 57.39% (p < 0.05), respectively, and down-regulated the protein expressions of peroxisome proliferator-activated receptor-γ (PPARγ), CCAAT/enhancer-binding protein alpha (C/EBPα), sterol regulatory element-binding protein 1 (SREBP-1) and fatty acid synthase (FAS). Additionally, the V-P complex significantly up-regulated the protein levels of total β-catenin (t-β-catenin), nuclear β-catenin (n-β-catenin), phosphorylated adenosine monophosphate-activated protein kinase alpha (p-AMPKα) and liver kinase B1 (p-LKB1). These showed that the inhibitory effect of V-P complex on human adipogenesis was mediated by activating Wnt/β-catenin and LKB1/AMPK-dependent signaling pathway. Therefore, the synthetic V-P complex could be considered as a candidate for prevention and treatment of obesity. |
| first_indexed | 2024-12-22T07:44:53Z |
| format | Article |
| id | doaj.art-3a191ccd678d45c2943234e95e87cbdc |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T07:44:53Z |
| publishDate | 2020-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-3a191ccd678d45c2943234e95e87cbdc2022-12-21T18:33:39ZengPublic Library of Science (PLoS)PLoS ONE1932-62032020-01-01159e023954710.1371/journal.pone.0239547Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway.Shuang ZhangLei YanSang Moo KimObesity is a common disease over the world and is tightly associated with diabetes mellitus, cardiovascular and cancer disease. Although our previous study showed that the synthetic vanadium-protein (V-P) complex had a better effect on antioxidant and antidiabetic, the relative molecular mechanisms are still entirely unknown. Hence, we investigated the effect of the synthetic V-P complex on adipocyte differentiation (adipogenesis) using human preadipocytes to clarify its molecular mechanisms of action. The primary human preadipocytes were cultured with and without V-P complex during adipocyte differentiation. The cell proliferation, lipid accumulation, and the protein expression of transcription factors and related enzymes were determined for the differentiated human preadipocytes. In this study, the 20 μg/mL of V-P complex reduced the lipid and triglyceride (TG) content by 74.47 and 57.39% (p < 0.05), respectively, and down-regulated the protein expressions of peroxisome proliferator-activated receptor-γ (PPARγ), CCAAT/enhancer-binding protein alpha (C/EBPα), sterol regulatory element-binding protein 1 (SREBP-1) and fatty acid synthase (FAS). Additionally, the V-P complex significantly up-regulated the protein levels of total β-catenin (t-β-catenin), nuclear β-catenin (n-β-catenin), phosphorylated adenosine monophosphate-activated protein kinase alpha (p-AMPKα) and liver kinase B1 (p-LKB1). These showed that the inhibitory effect of V-P complex on human adipogenesis was mediated by activating Wnt/β-catenin and LKB1/AMPK-dependent signaling pathway. Therefore, the synthetic V-P complex could be considered as a candidate for prevention and treatment of obesity.https://doi.org/10.1371/journal.pone.0239547 |
| spellingShingle | Shuang Zhang Lei Yan Sang Moo Kim Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. PLoS ONE |
| title | Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. |
| title_full | Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. |
| title_fullStr | Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. |
| title_full_unstemmed | Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. |
| title_short | Vanadium-protein complex inhibits human adipocyte differentiation through the activation of β-catenin and LKB1/AMPK signaling pathway. |
| title_sort | vanadium protein complex inhibits human adipocyte differentiation through the activation of β catenin and lkb1 ampk signaling pathway |
| url | https://doi.org/10.1371/journal.pone.0239547 |
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