Title : Upregulation of N-acetylglucosaminyltransferase-V by heparin-binding EGF-like growth factor induces keratinocyte proliferation and epidermal hyperplasia.

Pub. Date : 2012 Jul

PMID : 22716246






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Oligosaccharide modification by N-acetylglucosaminyltransferase-V (GnT-V), a glycosyltransferase encoded by the Mgat5 gene that catalyses the formation of beta1,6 GlcNAc (N-acetylglucosamine) branches on N-glycans, is thought to be associated with cancer growth and metastasis. n-glycans mannoside acetylglucosaminyltransferase 5 Mus musculus
2 Oligosaccharide modification by N-acetylglucosaminyltransferase-V (GnT-V), a glycosyltransferase encoded by the Mgat5 gene that catalyses the formation of beta1,6 GlcNAc (N-acetylglucosamine) branches on N-glycans, is thought to be associated with cancer growth and metastasis. n-glycans mannoside acetylglucosaminyltransferase 5 Mus musculus
3 Oligosaccharide modification by N-acetylglucosaminyltransferase-V (GnT-V), a glycosyltransferase encoded by the Mgat5 gene that catalyses the formation of beta1,6 GlcNAc (N-acetylglucosamine) branches on N-glycans, is thought to be associated with cancer growth and metastasis. n-glycans mannoside acetylglucosaminyltransferase 5 Mus musculus
4 Overexpression of GnT-V in cancer cells enhances the signalling of growth factors such as epidermal growth factor (EGF) and transforming growth factor-beta by increasing galectin-3 binding to polylactosamine structures on receptor N-glycans. n-glycans mannoside acetylglucosaminyltransferase 5 Mus musculus
5 These results indicate that a high expression of GnT-V in keratinocytes contributes to HB-EGF-mediated epidermal hyperproliferation by inhibiting endocytosis of EGF receptors bearing beta1,6 GlcNAc on their N-glycans. n-glycans mannoside acetylglucosaminyltransferase 5 Mus musculus