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Association of the macrophage activating factor (MAF) precursor activity with polymorphism in vitamin D-binding
Hideko Nagasawa1, Hideyuki Sasaki, Yoshihiro Uto
1Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, Tokushima 770-8503, Japan.
Background:
Serum vitamin D-binding protein (Gc protein or DBP) is a highly expressed polymorphic protein, which is a precursor of the inflammation-primed macrophage activating factor, GcMAF, by a cascade of carbohydrate processing reactions. In order to elucidate the relationship between Gc polymorphism and GcMAF precursor activity, we estimated the phagocytic ability of three homotypes of Gc protein, Gc1F-1F, Gc1S-1S and Gc2-2, through processing of their carbohydrate moiety.
Materials And Methods:
We performed Gc typing of human serum samples by isoelectric focusing (IEF). Gc protein from human serum was purified by affinity chromatography with 25-hydroxyvitamin D3-sepharose. A phagocytosis assay of Gc proteins, modified using beta-glycosidase and sialidase, was carried out.
Results:
The Gc1F-1F phenotype was revealed to possess Galbeta1-4GalNAc linkage by the analysis of GcMAF precursor activity using beta1-4 linkage-specific galactosidase from jack bean. The GcMAF precursor activity of the Gc1F-1F phenotype was highest among three Gc homotypes.
Conclusion:
The Gc polymorphism and carbohydrate diversity of Gc protein are significant for its pleiotropic effects.
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