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|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|
|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.|
|Appears in Collections:||Journal Articles|
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