Human MUC4 mucin induces ultra-structural changes and tumorigenicity in pancreatic cancer cells
نویسندگان
چکیده
منابع مشابه
MUC4 mucin interacts with and stabilizes the HER2 oncoprotein in human pancreatic cancer cells.
MUC4, a high-molecular weight transmembrane glycoprotein, is overexpressed in pancreatic cancer and is implicated in its pathogenesis. It is a heterodimeric protein containing a large extracellular, heavily glycosylated subunit, MUC4alpha, and a transmembrane growth factor-like subunit, MUC4beta. In the present study, we have shown the interaction of human MUC4 with the receptor tyrosine kinase...
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The MUC4 mucin is a high molecular weight, membrane-bound, and highly glycosylated protein. It is a multi-domain protein that is putatively cleaved into a large mucin-like subunit (MUC4α) and a C-terminal growth-factor like subunit (MUC4β). MUC4 plays critical roles in physiological and pathological conditions and is aberrantly overexpressed in several cancers, including those of the pancreas, ...
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Transmembrane proteins MUC4, EGFR and HER2 are shown to be critical in invasion and metastasis of pancreatic cancer. Besides, we and others have demonstrated de novo expression of MUC4 in ~70-90% of pancreatic cancer patients and its stabilizing effects on HER2 downstream signaling in pancreatic cancer. Here, we found that use of canertinib or afatinib resulted in reduction of MUC4 and abrogati...
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MUC4 is a type I membrane-bound mucin expressed at the apical pole of normal polarized epithelial cells. MUC4 apomucin is characterized by a long hyperglycosylated extracellular domain, Epidermal Growth Factor (EGF)-like domains, a hydrophobic transmembrane domain, and a short cytoplasmic tail. MUC4 also contains NIDO, AMOP and vWF-D domains that are unique in the apomucin family. In cancers, M...
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Background: Glycation of proteins is a non-enzymatic spontaneous process that occurs in diabetes mellitus and aging, altering the structure and function of proteins. IgG undergoes glycation leading to changes in its reactivity to antigen and fixation of complement. Objective: This study aimed at revealing the effect of glycation on the interaction of IgG with anti-IgG using electroimmunoassay...
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ژورنال
عنوان ژورنال: British Journal of Cancer
سال: 2007
ISSN: 0007-0920,1532-1827
DOI: 10.1038/sj.bjc.6603868