Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer
Authors: Voraratt Champattanachai
Pukkavadee Netsirisawan
Parunya Chaiyawat
Thanong Phueaouan
Ratana Charoenwattanasatien
Daranee Chokchaichamnankit
Phaibul Punyarit
Chantragan Srisomsap
Jisnuson Svasti
Chulabhorn Research Institute
Chulabhorn Graduate Institute
Army Institute of Pathology
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jul-2013
Citation: Proteomics. Vol.13, No.14 (2013), 2088-2099
Abstract: O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively. This modification is associated with glucose metabolism, which plays important roles in many diseases including cancer. Although emerging evidence reveals that some tumor-associated proteins are O-GlcNAc modified, the total O-GlcNAcylation in cancer is still largely unexplored. Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level. Using 2D O-GlcNAc immnoblotting and LC-MS/MS analysis, we successfully identified 29 proteins, with seven being uniquely O-GlcNAcylated or associated with O-GlcNAcylation in cancer. Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis. In addition, proteins associated with RNA metabolism, gene expression, and cytoskeleton were highly O-GlcNAcylated or associated with O-GlcNAcylation. Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro. These data indicate that aberrant protein O-GlcNAcylation is associated with breast cancer. Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
ISSN: 16159861
Appears in Collections:Scopus 2011-2015

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.