| Vanadyl ions binding to GroEL （HSP60） and inducing its depolymerization |
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| 引用本文： | LEI WanHua LIU HuiXue ZHONG LiJun YANG XiaoDa WANG Kui. Vanadyl ions binding to GroEL （HSP60） and inducing its depolymerization[J]. 科学通报(英文版), 2007, 52(20): 2775-2781. DOI: 10.1007/s11434-007-0380-0 |
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| 作者姓名： | LEI WanHua LIU HuiXue ZHONG LiJun YANG XiaoDa WANG Kui |
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| 作者单位： | [1]Department of Chemical Biology, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing 100083, China; [2]Medical and Healthy Analysis Center, Peking University Health Science Center, Beijing 100083, China; [3]National Laboratory of Natural and Biomimetric Drugs, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing 100083, China |
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| 基金项目： | Supported by the National Natural Science Foundation of China （Grant No. 20331020） and 985 Program and Beijing City Research Programs of Science ＆ Technology |
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| 摘 要： | Several vanadium compounds have been known for the hypoglycemic and anticancer effects. However, the mechanisms of the pharmacological and toxicological effects were not clear. In this work, we in- vestigated the potential targets of vanadium in mitochondria. Vanadyl ions were found to bind to mi- tochondria from rat liver with a stoichiometry of 244±58 nmol/mg protein and an apparent dissocia- tion constant (Kd) of (2.0±0.8)×10·16 mol/L. Using size exclusion chromatography, a vanadium-binding protein was isolated and identified to be the 60-kDa heat shock protein (HSP60) by mass spectrometry analysis and immunoassays. Additionally, binding of vanadyl ions was found to result in depolymeri- zation of homo-oligomeric HSP60 (GroEL). HSP60 is an indispensable molecular chaperone and in- volved in many kinds of pathogenesis of inflammatory and autoimmune diseases, e.g. type 1 diabetes. Our results suggested that HSP60 could be a novel important target involved in the biological and/or toxicological effects of vanadium compounds.
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| 关 键 词： | 糖尿病 线粒体 钒 疗效 |
| 收稿时间： | 2006-12-18 |
| 修稿时间： | 2006-12-18 |
Vanadyl ions binding to GroEL (HSP60) and inducing its depolymerization |
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| Lei WanHua,Liu HuiXue,Zhong LiJun,Yang XiaoDa,Wang Kui. Vanadyl ions binding to GroEL (HSP60) and inducing its depolymerization[J]. Chinese science bulletin, 2007, 52(20): 2775-2781. DOI: 10.1007/s11434-007-0380-0 |
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| Authors: | Lei WanHua Liu HuiXue Zhong LiJun Yang XiaoDa Wang Kui |
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| Affiliation: | (1) Department of Chemical Biology, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing, 100083, China;(2) Medical and Healthy Analysis Center, Peking University Health Science Center, Beijing, 100083, China;(3) National Laboratory of Natural and Biomimetric Drugs, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing, 100083, China |
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| Abstract: | Several vanadium compounds have been known for the hypoglycemic and anticancer effects. However, the mechanisms of the pharmacological and toxicological effects were not clear. In this work, we investigated the potential targets of vanadium in mitochondria. Vanadyl ions were found to bind to mitochondria from rat liver with a stoichiometry of 244±58 nmol/mg protein and an apparent dissociation constant (K d) of (2.0±0.8)×10−16 mol/L. Using size exclusion chromatography, a vanadium-binding protein was isolated and identified to be the 60-kDa heat shock protein (HSP60) by mass spectrometry analysis and immunoassays. Additionally, binding of vanadyl ions was found to result in depolymerization of homo-oligomeric HSP60 (GroEL). HSP60 is an indispensable molecular chaperone and involved in many kinds of pathogenesis of inflammatory and autoimmune diseases, e.g. type 1 diabetes. Our results suggested that HSP60 could be a novel important target involved in the biological and/or toxicological effects of vanadium compounds. Supported by the National Natural Science Foundation of China (Grant No. 20331020) and 985 Program and Beijing City Research Programs of Science & Technology |
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| Keywords: | vanadium mitochondria HSP60 diabetes |
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