Please use this identifier to cite or link to this item: http://dspace.sctimst.ac.in/jspui/handle/123456789/595
Title: IgA1 is the premier serum glycoprotein recognized by human galectin-1 since T antigen (Gal beta 1 -> 3GalNAc-) is far superior to non-repeating N-acetyl lactosamine as ligand
Authors: Sangeetha, SR
Appukuttan, PS
Keywords: Immunology
Issue Date: 2005
Publisher: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Citation: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. 35; 5; 269-276
Abstract: Human heart galectin-1 (HHL) was separated by high pressure liquid chromatography from endogenous glycoproteins co-purified with it during affinity chromatography. These glycoproteins offered excellent ligands for HHL binding and were rich in T antigen (Gal beta 1 -> 3 GalNAc-) of O-linked oligosaccharides. In enzyme linked lectin assay and hemagglutination inhibition assay, human IgA1, bovine fetuin and other O-glycosylated T antigen-bearing glycoproteins bound to the lectin efficiently in contrast to single N-acetyl lactosamine (LacNAc)bearing N-linked oligosaccharides released from them and to IgG which is not O-glycosylated. HHL binding to IgA1 and fetuin was unaffected by removal of their N-linked oligosaccharides by a-mannosidase. When immobilized, O-glycosylated serum proteins but not IgG could capture HHL from its solutions. Desialylated or polymeric IgA1 was better inhibitor than monomeric IgA1. The findings suggest a possible role for galectin-1 in anchoring of microbial and cancer cells known to be rich in T antigen, in high serum IgA1 turn over and in tissue sequestering of IgA1 immune complexes especially after their microbial desialylation in IgA nephropathy and other immune complex-mediated disorders. (c) 2005 Elsevier B.V. All rights reserved.
URI: http://dx.doi.org/10.1016/j.ijbiomac.2005.03.004
http://dspace.sctimst.ac.in/jspui/handle/123456789/595
Appears in Collections:Journal Articles

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.