International Journal of Hematology

DOI: 10.1007/s12185-018-2452-0 Pages: 139-144

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

1. Fujita Health University Graduate School of Medicine

2. Fujita Health University, Department of Pharmacology, School of Medicine

3. Fujita Health University, Department of Physiology, Faculty of Medical Management and Information Science, School of Health Sciences

4. Fujita Health University, Department of Biology, Faculty of Rehabilitation, School of Health Sciences

5. Nara Medical University, Department of Blood Transfusion Medicine

6. Fujita Health University, Department of Biology, Faculty of Medical Technology, School of Health Sciences

Correspondence to:
Taei Matsui
Tel: +81-562-93-2954
Email: tmatsui@fujita-hu.ac.jp

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Abstract

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.

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