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Articles by Chi Zhang
Total Records ( 3 ) for Chi Zhang
  Jun-Wei Cao , Li-Bing Ma , Yong Zhang , Xiao-Ning He , Cong-Ming Bi , Shu-Ying Peng , Song Hua , Jian-Hong Shu , Wu-JiaFu Sai , Xiang-Chen Li , Chi Zhang and Zhi-Peng Zhang
  Expression sequences of human Lactoferrin (LF) and Internal Ribozyme Entry Site (IRES) were successfully connected by double enzyme digestion and directed cloning and recombination plasmid pIL was constructed. Mammary gland specific expression plasmid pEBHIL of human lysozyme and human LF was constructed by BamHI restrictive enzyme digestion. Plasmid pEBHIL was introduced to cow mammary gland epithelial cells after liposome transfection. Positive cells were determined by G418 and PCR after EGFP expression observed by fluorescent microscope and proliferated and induced by hormone. The results of Western Blotting analysis on cell supernatant showed that transfected cells had expressed and secreted human lysozyme (MW 14.7 ku) and human LTF (MW 40 ku).
  Jing Zheng , Wan-Hua Shen , Ting-Jia Lu , Yang Zhou , Qian Chen , Zi Wang , Ting Xiang , Yong-Chuan Zhu , Chi Zhang , Shumin Duan and Zhi-Qi Xiong
  Endocytosis of Trk (tropomyosin-related kinase) receptors is critical for neurotrophin signal transduction and biological functions. However, the mechanism governing endocytosis of TrkB (tropomyosin-related kinase B) and the specific contributions of TrkB endocytosis to downstream signaling are unknown. In this study, we report that blocking clathrin, dynamin, or AP2 in cultured neurons of the central nervous system inhibited brain-derived neurotrophic factor (BDNF)-induced activation of Akt but not ERK. Treating neurons with the clathrin inhibitor monodansylcadaverine or a peptide that blocks dynamin function specifically abrogated Akt pathway activation in response to BDNF but did not affect the response of other downstream effectors or the up-regulation of immediate early genes neuropeptide Y and activity-regulated cytoskeleton-associated protein. Similar effects were found in neurons expressing small interfering RNA to silence AP2 or a dominant negative form of dynamin that inhibits clathrin-mediated endocytosis. In PC12 cells, ERK but not Akt activation required TrkA endocytosis following stimulation with nerve growth factor, whereas the opposite was true when TrkA-expressing neurons were stimulated with nerve growth factor in the central nervous system. Thus, the specific effects of internalized Trk receptors probably depend on the presence of cell type-specific modulators of neurotrophin signaling and not on differences inherent to Trk receptors themselves. Endocytosis-dependent activation of Akt in neurons was found to be critical for BDNF-supported survival and dendrite outgrowth. Together, these results demonstrate the functional requirement of clathrin- and dynamin-dependent endocytosis in generating the full intracellular response of neurons to BDNF in the central nervous system.
  Jie-Min Jia , Qian Chen , Yang Zhou , Sheng Miao , Jing Zheng , Chi Zhang and Zhi-Qi Xiong
  The ability of synapses to undergo changes in structure and function in response to alterations of neuronal activity is an essential property of neural circuits. One way that this is achieved is through global changes in the molecular composition of the synapse; however, it is not clear how these changes are coupled to the dynamics of neuronal activity. Here we found that, in cultured rat cortical neurons, bidirectional changes of neuronal activity led to corresponding alterations in the expression of brain-derived neurotrophic factor (BDNF) and phosphorylation of its receptor tropomyosin-related kinase B (TrkB), as well as in the level of synaptic proteins. Exogenous BDNF reversed changes in synaptic proteins induced by chronic activity blockade, while inhibiting Trk kinase activity or depleting endogenous BDNF abolished the concentration changes induced by chronic activity elevation. Both tetrodotoxin and bicuculline had significant, but opposite, effects on synaptic protein ubiquitination in a time-dependent manner. Furthermore, exogenous BDNF was sufficient to increase ubiquitination of synaptic proteins, whereas scavenging endogenous BDNF or inhibiting Trk kinase activity prevented the ubiquitination of synaptic proteins induced by chronic elevation of neuronal activity. Inhibiting the proteasome or blocking protein polyubiquitination mimicked the effect of tetrodotoxin on the levels of synaptic proteins and canceled the effects of BDNF. Our study indicates that BDNF-TrkB signaling acts upstream of the ubiquitin proteasome system, linking neuronal activity to protein turnover at the synapse.
 
 
 
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