李蓬
代谢性疾病如肥胖症,糖尿病,动脉粥样硬化等的发生和发展机制,主要研究脂肪细胞和肝细胞中的脂肪积累,分泌及分解的分子机制以及与胰岛素敏感性的关系。在细胞水平上研究线粒体的功能,脂滴的形成,融合及与内质网的关系。
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- 姓名:李蓬
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学术头衔:
博士生导师, 享受国务院特殊津贴专家,
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学科领域:
生物化学
- 研究兴趣:代谢性疾病如肥胖症,糖尿病,动脉粥样硬化等的发生和发展机制,主要研究脂肪细胞和肝细胞中的脂肪积累,分泌及分解的分子机制以及与胰岛素敏感性的关系。在细胞水平上研究线粒体的功能,脂滴的形成,融合及与内质网的关系。
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4
李蓬, Jing Ye, , John Zhong Li, Yang Liu, Xuanhe Li, Tianshu Yang, Xiaodong Ma, Qing Li, Zemin Yao, and Peng Li, *
Cell Metabolism 9, 177-190, February 4, 2009,-0001,():
-1年11月30日
Secretionof triacylglycerol-enrichedvery-low-density lipoproteins (VLDLs) fromthe liver is vital for maintaining plasma lipid homeostasis. However, the process of VLDL assembly and lipidation is not well characterized. Here, we observed that liver of Cideb null mice had higher levels of triacylglycerols accompanied by low level of VLDL secretion. Furthermore, VLDL particles secreted from hepatocytes of Cideb null mice have low levels of triacylglycerols but normal levels of apoB. We also observed that Cideb is localized to endoplasmic reticulum and lipid droplets. Importantly,wehave identified apoBas a Cideb-interacting protein. By infecting adenoviruses expressing various Cideb truncations into hepatocytes of Cideb null mice, we found that Cideb requires both its apoB-binding and lipid droplet association domains to restore the secretion of triacylglycerol-enriched VLDL particles. Our data suggest that Cideb promotes the formation of triacylglycerol-enriched VLDL particles and provides a molecular insight into VLDL lipidation and maturation in hepatocytes.
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李蓬, Jingzong Qi, , Jingyi Gong, Tongjin Zhao, Jie Zhao, Penny Lam, Jing Ye, John Zhong Li, Jiawei Wu, Hai-Meng Zhou, * and Peng Li, *
The EMBO Journal (2008) 27, 1537-1548,-0001,():
-1年11月30日
We previously showed that Cidea/mice are resistant to diet-induced obesity through the upregulation of energy expenditure. The AMP-activated protein kinase (AMPK), consisting of catalytic a subunit and regulatory subunits b and c, has a pivotal function in energy homoeostasis. We show here that AMPK protein levels and enzymatic activity were significantly increased in the brown adipose tissue of Cidea/mice.We also found that Cidea is colocalized with AMPK in the endoplasmic reticulum and forms a complex with AMPK in vivo through specific interaction with the b subunit of AMPK, but not with the a or c subunit. When co-expressed with Cidea, the stability of AMPK-b subunit was dramatically reduced due to increased ubiquitinationmediated degradation, which depends on a physical interaction between Cidea and AMPK. Furthermore, AMPK stability and enzymatic activity were increased in Cidea/adipocytes differentiated from mouse embryonic fibroblasts or preadipocytes. Our data strongly suggest that AMPK can be regulated by Cidea-mediated ubiquitindependent proteosome degradation, and provide a molecular explanation for the increased energy expenditure and lean phenotype in Cidea-null mice.
AMPK, brown adipose tissue, Cidea, protein degradation, ubiquitination
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李蓬, John Zhong Li, Jing Ye, , Bofu Xue, Jingzhong Qi, Jing Zhang, Zhihong Zhou, Qing Li, Zilong Wen, and Peng Li
DIABETES, VOL. 56, OCTOBER 2007 2523-2532,-0001,():
-1年11月30日
OBJECTIVE—Our previous study suggests that Cidea, a member of Cide family proteins that share sequence homology with the DNA fragmentation factor and are expressed at high levels in brown adipose tissue, plays an important role in the development of obesity. Cideb, another member of Cide family protein, is highly expressed in the liver. We would like to understand the physiological role of Cideb in the regulation of energy expenditure and lipid metabolism. RESEARCH DESIGN AND METHODS—We generated Cidebnull mice by homolog recombination and then fed both wild-type and Cideb-null mice with high-fat diet (58% fat). We then characterized the animals' adiposity index, food intake, whole-body metabolic rate, liver morphology, rate of fatty acid synthesis and oxidation, insulin sensitivity, and gene expression profile. RESULTS—Cideb-null mice had lower levels of plasma triglycerides and free fatty acids and were resistant to high-fat diet-induced obesity and live steatosis. In addition, Cideb mutant mice displayed significantly increased insulin sensitivity and enhanced rate of whole-body metabolism and hepatic fatty acid oxidation. More importantly, Cideb-null mice showed decreased lipogenesis and reduced expression levels of acetyl-CoA carboxylase, fatty acid synthase, and stearol-CoA desaturase. We further demonstrated that expression levels of sterol response element binding protein 1c was significantly decreased in Cidebdeficient mice. CONCLUSIONS—Our data demonstrate that Cideb is a novel important regulator in lipid metabolism in the liver. Cideb may represent a new therapeutic target for the treatment of obesity, diabetes, and liver steatosis. Diabetes 56:2523-2532, 2007
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李蓬, Peng Li, *‡ Deepak Nijhawan, *‡ Imawati Budihardjo, * Srinivasa M. Srinivasula, † Manzoor Ahmad, † Emad S. Alnemri, † and Xiaodong Wang*§
Cell, Vol. 91, 479-489, November 14, 1997,-0001,():
-1年11月30日
We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activa-tion in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cyto-chrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Muta-tion of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic re-sponse in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
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