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Mass spectrometry analysis of intact protein N-glycosylation signatures of cells and sera in pancreatic adenocarcinomas
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Mingming XU, Zhaoliang LIU, Wenhua HU, Ying HAN, Zhen WU, Sufeng CHEN, Peng XIA, Jing DU, Xumin ZHANG, Piliang HAO, Jun XIA, Shuang YANG. Mass spectrometry analysis of intact protein N-glycosylation signatures of cells and sera in pancreatic adenocarcinomas[J]. Journal of Zhejiang University Science B, 1998, -1(-1): .
@article{title="Mass spectrometry analysis of intact protein N-glycosylation signatures of cells and sera in pancreatic adenocarcinomas",
author="Mingming XU, Zhaoliang LIU, Wenhua HU, Ying HAN, Zhen WU, Sufeng CHEN, Peng XIA, Jing DU, Xumin ZHANG, Piliang HAO, Jun XIA, Shuang YANG",
journal="Journal of Zhejiang University Science B",
volume="-1",
number="-1",
pages="",
year="1998",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B2200652"
}
%0 Journal Article
%T Mass spectrometry analysis of intact protein N-glycosylation signatures of cells and sera in pancreatic adenocarcinomas
%A Mingming XU
%A Zhaoliang LIU
%A Wenhua HU
%A Ying HAN
%A Zhen WU
%A Sufeng CHEN
%A Peng XIA
%A Jing DU
%A Xumin ZHANG
%A Piliang HAO
%A Jun XIA
%A Shuang YANG
%J Journal of Zhejiang University SCIENCE B
%V -1
%N -1
%P
%@ 1673-1581
%D 1998
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2200652
TY - JOUR
T1 - Mass spectrometry analysis of intact protein N-glycosylation signatures of cells and sera in pancreatic adenocarcinomas
A1 - Mingming XU
A1 - Zhaoliang LIU
A1 - Wenhua HU
A1 - Ying HAN
A1 - Zhen WU
A1 - Sufeng CHEN
A1 - Peng XIA
A1 - Jing DU
A1 - Xumin ZHANG
A1 - Piliang HAO
A1 - Jun XIA
A1 - Shuang YANG
J0 - Journal of Zhejiang University Science B
VL - -1
IS - -1
SP -
EP -
%@ 1673-1581
Y1 - 1998
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2200652
Abstract: pancreatic cancer is among the most malignant cancers, thus early intervention is the key to better survival outcomes. However, no methods have been derived that can reliably identify early precursors of development into malignancy. Therefore, it is urgent to discover early molecular changes during pancreatic tumorigenesis. As aberrant glycosylation is closely associated with cancer progression, numerous efforts have been made to mine glycosylation changes as biomarkers for diagnosis; however, detailed glycoproteomic information, especially site-specific N-glycosylation changes in pancreatic cancer with and without drug treatment, needs to be further explored. Herein, we used comprehensive solid-phase chemoenzymatic glycoproteomics to analyze glycans, glycosites and intact glycopeptides in pancreatic cancer cells and patient sera. The profiling of N-glycans in cancer cells revealed an increase in the secreted glycoproteins from the primary tumor of MIA PaCa-2 cells, whereas human sera, which contain many secreted glycoproteins, had significant changes of glycans at their specific glycosites. These results indicated the potential role for tumor-specific glycosylation as disease biomarkers. We also found that AMG-510, a small molecule inhibitor against KRAS G12C mutation, profoundly reduced the glycosylation level in MIA PaCa-2 cells, suggesting that KRAS plays a role in the cellular glycosylation process, thus glycosylation inhibition contributes to the anti-tumor effect of AMG-510.
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