Research Papers:
Mucin glycosylating enzyme GALNT2 suppresses malignancy in gastric adenocarcinoma by reducing MET phosphorylation
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Abstract
Shin-Yun Liu1, Chia-Tung Shun2, Kuan-Yu Hung3, Hsueh-Fen Juan5, Chia-Lang Hsu5, Min-Chuan Huang1,6, I-Rue Lai1,4
1Graduate Institute of Anatomy and Cell Biology College of Medicine, National Taiwan University, Taipei, Taiwan
2Department of Pathology, National Taiwan University Hospital, Taipei, Taiwan
3Department of Internal Medicine, National Taiwan University Hospital Hsin-Chu Branch, Taipei, Taiwan
4Department of Surgery, National Taiwan University Hospital, Taipei, Taiwan
5Department of Life Science and Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, Taiwan
6Research Center for Developmental Biology and Regenerative Medicine, National Taiwan University, Taipei, Taiwan
Correspondence to:
Min-Chuan Huang, e-mail: [email protected]
I-Rue Lai, e-mail: [email protected]
Keywords: gastric cancer, GALNT2, O-glycosylation, hepatocyte growth factor, receptor tyrosin kinase
Received: August 06, 2015 Accepted: January 17, 2016 Published: January 30, 2016
ABSTRACT
Glycosylation affects malignancy in cancer. Here, we report that N- acetylgalactosaminyltransferase 2 (GALNT2), an enzyme that mediates the initial step of mucin type-O glycosylation, suppresses malignant phenotypes in gastric adenocarcinoma (GCA) by modifying MET (Hepatocyte growth factor receptor) activity. GALNT2 mRNA and protein were downregulated in GCAs, and this reduction was associated with more advanced disease stage and shorter recurrence-free survival. Suppressing GALNT2 expression in GCA cells increased cell growth, migration, and invasion in vitro, and tumor metastasis in vivo. GALNT2 knockdown enhanced phosphorylation of MET and decreased expression of the Tn antigen on MET. Inhibiting MET activity with PHA665752 decreased the malignant phenotypes caused by GALNT2 knockdown in GCA cells. Our results indicate that GALNT2 suppresses the malignant potential of GCA cells and provide novel insights into the significance of O-glycosylation in MET activity and GCA progression.
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