Haipeng Liu

Publications (2)6.16 Total impact

• Article: Hippocampal synaptic dysregulation of exo/endocytosis-associated proteins induced in a chronic mild-stressed rat model.

  Y Hu, J Zhou, L Fang, H Liu, Q Zhan, D Luo, C Zhou, J Chen, Q Li, P Xie
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  ABSTRACT: Although major depressive disorder (MDD) is a serious neuropsychiatric illness, it's pathogenesis remains unclear. Current evidence suggests that the abnormal transmission and plasticity of hippocampal synapses play an important role in the pathogenesis of MDD. In this study, a two-dimensional gel-based proteomic approach to profile alterations of synaptosome protein expression was applied in the hippocampus of rats subjected to chronic mild stress. Through mass spectrometry and database searching, 19 differentially expressed proteins were identified, of which 5 were up-regulated and 14 were down-regulated in the chronic mild-stressed group as compared with the control group. Subsequently, several proteins of interest were further validated by Western blotting. A detailed analysis of protein functions and disease relevance revealed that synaptic exo/endocytosis-associated proteins were dysregulated in the chronic mild-stressed rats. The present study is the first reported synaptoproteomic analysis of the chronic mild-stressed rat hippocampus. The synaptic exo/endocytosis-associated proteins may participate in a central mechanism that underlies the abnormal transmission and plasticity of hippocampal synapses found in the chronic mild-stressed rats, and provides guidance to advance our understanding of the pathogenesis of MDD.
  Neuroscience 08/2012; · 3.38 Impact Factor
• Article: Preparation and application of a partially degradable gel in mass spectrometry-based proteomic analysis.

  Jian Zhou, Yongbo Hu, Yong Lin, Haipeng Liu, Peng Xie
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  ABSTRACT: In-gel digestion is an attractive route in mass spectrometry-based proteomic analysis, which, however, often suffers from a certain amount of sample loss mainly due to insufficient protein digestion and peptide extraction. To address this, herein we establish a partially degradable gel-assisted protein digestion and peptide recovery method by means of a simple replacement of bis-acrylamide (BA) with bis-acrylylcystamine (BAC). Concretely, the protein sample solubilized using high concentrations of sodium dodecyl sulfate (SDS) and urea were directly entrapped and immobilized into BAC-crosslinked gel by vacuum-dried gel absorption followed by fixation treatment. After removal of SDS and urea by repeated washing, the proteins were subjected to in-gel digestion and the gel was reductively treated. The tryptic peptides were recovered from the partial degradation of the gel and analyzed afterwards by capillary liquid chromatography coupled with tandem mass spectrometry (CapLC-MS/MS). Compared with conventional BA-crosslinked gel method, this new method increased the numbers of identified proteins and unique peptides by 20.2% and 20.4%, respectively. The further statistical analysis demonstrated that the method improved the recovery of tryptic peptides particularly larger and/or hydrophobic peptides, thereby significantly facilitating protein identification. Thus, the newly developed method is a promising alternative for BA-crosslinked gel-based shotgun workflows and has potential application in the related fields of protein chemistry and proteomics.
  Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 08/2011; 879(28):2957-62. · 2.78 Impact Factor