Please use this identifier to cite or link to this item:
|Title:||A fucose-containing O-glycoepitope on bovine and human nucleolin||Authors:||Aldi, Silvia
DELLA GIOVAMPAOLA, Cinzia
|Keywords:||A431; human cancer cells; CVEC; glycoepitopes; nucleolin; RNA-interference||Issue Date:||2009||Project:||None||Journal:||GLYCOBIOLOGY||Abstract:||
In this paper, we demonstrate the existence and localizationof fucosyl-containing O-glycoforms of nucleolin in culturedbovine endothelial cells (CVEC) and malignant culturedhuman A431 cells. The tool for this discovery was anantibody raised against gp273, a glycoprotein ligand for thesperm–egg interaction in the mollusc bivalve Unio elongatulus.The function and immunological properties of gp273mainly depend on clustered Lewis-like, fucose-containingO-glycans. Here an anti-gp273 antibody was used to evaluatewhether glycoepitopes similar to those of gp273 are partof potential ligands of selectins in endothelial cells.We foundthat anti-gp273 strongly and exclusively interacted with a110 kDa protein in CVEC and A431 tumor cells. After partialpurification, mass spectrometry identified the proteinas nucleolin. This was confirmed by comparing anti-gp273and anti-nucleolin antibody immunoblotting after nucleolindepletion.We confirmed that anti-gp273 binding to nuclearand extranuclear nucleolin was against a fucose-containingO-glycoepitope by immunoblot analysis of the protein afterchemically removing O-glycans and by lectin-blot analysisof control and nucleolin-depleted samples. Using anti-gp273IgG, we detected nucleolin on the plasma membrane andcytoplasm. O-glycosylation may regulate the plethora offunctions in which nucleolin is involved.
|Appears in Collections:||Publications|
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.