Effects of plasma glycosyltransferase on the ABO(H) blood group antigens of human von Willebrand factor

Von Willebrand factor (VWF) is one of the plasma protein carrying ABO(H) blood group antigens, but the combining process of these antigens is not clear. In the present study, we examined whether plasma glycosyltransferase affects the blood group antigens on VWF. VWF expressing H-antigen (H-VWF) from...

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Bibliographic Details
Published in:International journal of hematology 2018-08, Vol.108 (2), p.139-144
Main Authors: Kano, Taiki, Kondo, Kazunao, Hamako, Jiharu, Matsushita, Fumio, Sakai, Kazuya, Matsui, Taei
Format: Article
Language:English
Subjects:
ABO system
Antigens
Blood group O
Blood groups
Bovine serum albumin
Enzyme-linked immunosorbent assay
Glycosylation
Glycosyltransferase
Hematology
Medicine
Medicine & Public Health
N-acetylgalactosaminyltransferase
Oncology
Original Article
Plasma
Post-translation
Serum albumin
Sugar
Von Willebrand factor
Western blotting
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Summary:Von Willebrand factor (VWF) is one of the plasma protein carrying ABO(H) blood group antigens, but the combining process of these antigens is not clear. In the present study, we examined whether plasma glycosyltransferase affects the blood group antigens on VWF. VWF expressing H-antigen (H-VWF) from blood group O and bovine serum albumin conjugated with H-antigen (H-BSA) were incubated with recombinant α1-3- N -acetylgalactosaminyltransferase (rA-transferase) and A-plasma with or without an additional UDP-GalNAc. Transformed antigens were detected by western blotting and ELISA, using an anti-A antibody. Both H-VWF and H-BSA acquired the A-antigen after incubation with rA-transferase and UDP-GalNAc. Incubation with A-plasma very weakly converted the H-antigen on BSA and VWF to A-antigen only in the presence of supplemented UDP-GalNAc. This conversion was enhanced on desialylation of H-VWF. These results indicate that sugar chains of plasma VWF can be modified by the external glycosyltransferase, but that plasma glycosyltransferase has no effect on the blood group antigens of VWF due to its low activity and the lack of donor sugars. Further, sialic acid residues of VWF may exert a protective effect against post-translational glycosylation. Our results clearly exclude the possibility that blood group antigens of VWF are constructed extracellularly in plasma.
ISSN:0925-5710
1865-3774
DOI:10.1007/s12185-018-2452-0