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    发布时间:2019-07-01 13:50:19    点击:673

2019年7月2日Prof. Hui Zhang学术报告


  目:Multi-omic analysis of tumor tissues reveals a large number of glycopeptides and their association with glycosylation enzymes
报告人:Hui Zhang Professor
  : Department of Pathology, School of Medicine, Johns Hopkins University
 点:化学楼G211
  间:2019年7月2日(星期二)下午15:00
联系人:刘震 教授 (zhenliu@nju.edu.cn)
 
摘要:
Protein glycosylation plays fundamental roles in many cellular processes, and its dysregulation is associated with human diseases. Here, we describe the analysis of proteins from breast cancer xenograft tissues, revealing a large number of previously unidentified N-linked glycopeptides. More importantly, our approach allowed for a large-scale analysis of sialoglycopeptides in conjunction with the analysis of phosphopeptides. Combined MS/MS analyses of proteomic and phosphoproteomic datasets resulted in the identification of thousands of intact N-linked glycopeptides derived from breast cancer xenograft tissues. This analysis revealed an extensive number of glycopeptides hidden in the proteome and co-enriched in phosphopeptide-enriched proteomic data. We then performed genomic, proteomic, and glycoproteomic analysis of human high-grade serous ovarian carcinoma (HGSOC) and non-cancerous tissues, and found that abundance at glycosites was regulated by the overall glycoprotein expression, while glycosylation at each individual glycosylation site contained glycosylation-site-specific heterogeneity and it was regulated by the protein abundance of the glycoproteins as well as the levels of glycosylation enzymes that were involved in the glycosylation biosynthesis pathway. This study bridges the gaps among alterations in gene and protein expression, protein glycosylation, and phosphorylation by providing the most complete landscape of glycoproteome in related to proteome and genome, which would be beneficial for stratifying other protein modifications for changes of cancer gene products based on genetic alterations. Furthermore, using the data from glycoproteomics, proteomics, and genomics, we defined and demonstrated the possibility of classifying the pathological outcome of cancer from normal tissues of HGSOC using glycans on the glycoproteins from tissues.  
 
简历:
Dr. Hui Zhang is a professor of pathology who specializes in proteomics with particular emphasis on protein modifications. She is the director of the Mass Spectrometry Core Facility, Center for Biomarker Discovery and Translation. She obtained her BSc and MSc from Peking University and PhD from University of Pennsylvania. After PDF training, Dr Zhang was appointed as Scientist and Senior Scientist at Cell Signaling Technology and Institute for Systems Biology. From 2006 to now, She served as principle members of the Department of Pathology at Johns Hopkins University. Dr. Zhang studies protein modifications on the proteome scale and the effects of protein modifications on protein functions and diseases. In recent years, her lab has developed several novel glycoproteomic and glycomic technologies to study structures of cell surface glycoproteins and secreted glycoproteins. Currently, her group focuses on understanding the functions of protein modifications in biology and human diseases. Dr. Zhang has authored or co-authored about 200 peer-reviewed papers, including a number of papers published in Nature (2), Cell (1), Nature Biotechnology (3), Nature Protocols (3), Nature Method (1) and Nature Communications (1). So far, her publications have been cited by more than 13,800 times and her h-index is 52.

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