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Author Sangeetha, S. R. ♦ Appukuttan, P. S.
Source Sree Chitra Tirunal Institute for Medical Sciences & Technology
Content type Text
Publisher International Journal of Biological Macromolecules
File Format PDF
Language English
Subject Domain (in DDC) Technology ♦ Medicine & health ♦ Diseases
Subject Domain (in MeSH) Immune System Phenomena ♦ Biological Sciences
Subject Keyword Immunology
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.
Education Level UG and PG
Learning Resource Type Article
Educational Framework Medical Council of India (MCI)
Journal INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume Number 35
Issue Number 5
Page Count 8
Starting Page 269
Ending Page 276