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黎明涛, Ming YANG*, Cun-you WAGN, Feng ZHOU, Jing TAO, Tao LIU, Hai-yan WEI, Wei LIU, Ming-tao LI, Xian-song FENG
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-1年11月30日
AIM: A broad-range proteomic approach was applied to investigate the complexity of the mechanisms involved in pancreatic regeneration for identification of new treatment targets and potential markers of pancreatic stem cells. METHODS: A regeneration pancreatic model was induced by partial (90%) pancreatectomy in rats. Changes in protein expression in rat regeneration pancreas at 3 d after partial pancreatectomy, as compared to sham surgery, were analyzed using two-dimensional gel electrophoresis (2-DE), mass spectrometry (MS), and mass fingerprinting. RESULT: Two-DE displayed 91 spots with at least 1.5-fold of differentially expression at the time point of 3 days after pancreatectomy and 53 differentially expressed proteins were identified by peptide mass fingerprinting(PMF). These included embryogenic and cell proliferation-related, lipid and energy metabolism-related, protein and amino acid metabolism-related proteins, signal transduction proteins. CONCLUSION: The proteome profiling technique provided a broad-based and effective approach for the rapid assimilation and identification of adaptive protein changes while pancreas regeneration induced by pancreatectomy. Our data highlight the globe proteome during the pancreatic proliferation and differentiation processes, which is very important and will lead to better understand regulation mechanism of the pancreatic regeneration, and to ultimately reach the target of discovering protein biomarkers of pancreatic stem cells.
Partial pancreatectomy,, Regeneration,, Metabolism,, Stem cell,, Pancreas proteomics
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黎明涛, Neng-Wei Hu, Hong-Mei Zhang, Xiao-Dong Hu, Ming-Tao Li, Tong Zhang, Li-Jun Zhou, and Xian-Guo Liu
J Neurophysiol 89: 2354~2359, 2003;,-0001,():
-1年11月30日
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黎明涛, Jing-Ping Yun, , * Choong-Tsek Liew, Eng Ching Chew, Xiao-Yu Yin, Paul Bo San Lai, Yam Hin Fai, H.K. Richard Li, Mei-Lin Jin, Ming-Xiao Ding, Ming-Tao Li, Han-Liang Lin, and Wan Yee Lau
Journal of Cellular Biochemistry 91: 1269~1279 (2004),-0001,():
-1年11月30日
We explored the feasibility of studying nuclear matrix protein (NMP) expressions of the hepatocytes in normal and cirrhotic rat livers with liver regeneration after partial hepatectomy. Sixteen Wistar healthy rats were studied with experimental liver regeneration and/or liver cirrhosis. Two-dimensional (2-D) gel electrophoresis was used to generate these NMP compositions from these rat liver samples. Several antibodies against cytokeratin, vimentin, actin, B23, HNF4alpha, and heat shock protein 70 were used for identification by Western blot. Totally, 41 strongly stained protein spots were characterized on the 2-D gels. Thirty-four protein spots were detected in all of these rat livers, of which, cytokeratin, vimentin, actin, HNF4alpha, and heat shock protein 70 were identified. B23 was detected in the regenerated livers. Three protein spots (s33, s34, and s35) were detectable only inNMPpreparation extracted from the regenerating rat livers after hepatectomy. Another three protein spots (s36, s37, and s38) were detectable only in NMP preparation extracted from thioacetamide-induced cirrhotic rat livers. Under these conditions including experimental liver regeneration and/or liver cirrhosis, Over thirty higher abundance NMPs of hepatocytes were consistently expressed and considered as common and basic NMPs. Some of the NMPs are specific for liver regeneration and may play a critical role in cell proliferation and cell cycle, and some are specific for liver cirrhosis.
nuclear matrix proteins, liver regeneration, partial hepatectomy, thioacetamide, liver cirrhosis, twodimensional electrophoresis
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黎明涛, Wenming Li‡, Rongbiao Pi‡, Hugh H. N. Chan‡, Hongjun Fu‡, Nelson T. K. Lee‡, Hing Wai Tsang‡, Yongmei Pu§, Donald C. Chang§, Chaoying Li¶‖, Jialie Luo¶, Keming Xiong‖, Zhiwang Li¶, Hong Xue‡, Paul R. Carlier**, Yuanping Pang‡‡, Karl W. K. Tsim§, Mingtao Li§§, and Yifan Han‡¶¶
Vol. 280, No.18, Issue of May 6, pp. 18179~18188, 2005,-0001,():
-1年11月30日
The neuroprotective properties of bis (7)-tacrine, a novel dimeric acetylcholinesterase (AChE) inhibitor, on glutamate-induced excitotoxicity were investigated in primary cultured cerebellar granule neurons (CGNs). Exposure of CGNs to 75
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黎明涛, Mingtao Li, , Daniel A. Linseman, Melissa P. Allen, Mary Kay Meintzer, Xiaomin Wang, Tracey Laessig, Margaret E. Wierman, and Kim A. Heidenreich
The Journal of Neuroscience, September 1, 2001, 21 (17): 6544~6552,-0001,():
-1年11月30日
Myocyte enhancer factor 2 (MEF2) proteins are important regulators of gene expression during the development of skeletal, cardiac, and smooth muscle. MEF2 proteins are also present in brain and recently have been implicated in neuronal survival and differentiation. In this study we examined the cellular mechanisms regulating the activity of MEF2s during apoptosis of cultured cerebellar granule neurons, an established in vitro model for studying depolarization-dependent neuronal survival. All four MEF2 isoforms (A, B, C, and D) were detected by immunoblot analysis in cerebellar granule neurons. Endogenous MEF2A and MEF2D, but not MEF2B or MEF2C, were phosphorylated with the induction of apoptosis. The putative sites that were phosphorylated during apoptosis are functionally distinct from those previously reported to enhance MEF2 transcription. The increased phosphorylation of MEF2A and MEF2D was followed by decreased DNA binding, reduced transcriptional activity, and caspase-dependent cleavage to fragments containing N-terminal DNA binding domains and C-terminal transactivation domains. Expression of the highly homologous N terminus of MEF2A (1–131 amino acids) antagonized the transcriptional activity and prosurvival effects of a constitutively active mutant of MEF2D (MEF2D-VP16). We conclude that MEF2A and MEF2D are prosurvival factors with high transcriptional activity in postmitotic cerebellar granule neurons. When these neurons are induced to undergo apoptosis by lowering extracellular potassium, MEF2A and MEF2D are phosphorylated, followed by decreased DNA binding and cleavage by a caspase-sensitive pathway to N-terminal fragments lacking the transactivation domains. The degradation of MEF2D and MEF2A and the generation of MEF2 fragments that have the potential to act as dominant-inactive transcription factors lead to apoptotic cell death.
MEF2, neurons, apoptosis, trans, c, r, i, p, t, ion, caspase, cerebellum
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