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Taei Matsui - One of the best experts on this subject based on the ideXlab platform.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

Erik Dabelsteen - One of the best experts on this subject based on the ideXlab platform.

  • ABO Blood-Group Antigens in Oral Cancer
    Journal of dental research, 2005
    Co-Authors: Erik Dabelsteen, S. Gao
    Abstract:

    Tumor progression is often associated with altered glycosylation of the cell-surface proteins and lipids. The peripheral part of these cell-surface glycoconjugates often carries carbohydrate structures related to the ABO and Lewis Blood-Group Antigens. The expression of histo-Blood-Group Antigens in normal human tissues is dependent on the type of differentiation of the epithelium. In most human carcinomas, including oral carcinoma, a significant event is decreased expression of histo-Blood-Group Antigens A and B. The mechanisms of aberrant expression of Blood-Group Antigens are not clear in all cases. A relative down-regulation of the glycosyltransferase that is involved in the biosynthesis of A and B Antigens is seen in oral carcinomas in association with tumor development. The events leading to loss of A transferase activity are related, in some instances, to loss of heterozygosity (LOH) involving chromosome 9q34, which is the locus for the ABO gene, and in other cases, to a hypermethylation of the ABO gene promoter. The fact that hypermethylation targets the ABO locus, but not surrounding genes, suggests that the hypermethylation is a specific tumor-related event. However, since not all situations with lack of expression of A/B Antigens can be explained by LOH or hypermethylation, other regulatory factors outside the ABO promoter may be functional in transcriptional regulation of the ABO gene. Altered Blood Group Antigens in malignant oral tissues may indicate increased cell migration. This hypothesis is supported by studies showing that normal migrating oral epithelial cells like malignant cells show lack of expression of A/B Antigens, and by studies that target ABH Antigens to key receptors controlling adhesion and motility, such as integrins, cadherins, and CD-44.

  • tissue distribution of histo Blood Group Antigens
    Apmis, 2000
    Co-Authors: Vibeke Ravn, Erik Dabelsteen
    Abstract:

    : The introduction of immunohistochemical techniques and monoclonal antibodies to specific carbohydrate epitopes has made it possible to study in detail the tissue distribution of histo-Blood Group Antigens and related carbohydrate structures. The present paper summarizes the available data concerning the histological distribution of histo-Blood Group Antigens and their precursor structures in normal human tissues. Studies performed have concentrated on carbohydrate Antigens related to the ABO, Lewis, and TTn Blood Group systems, i.e. histo-Blood Group Antigens carried by type 1, 2, and 3 chain carrier carbohydrate chains. Histo-Blood Group Antigens are found in most epithelial tissues. Meanwhile, several factors influence the type, the amount, and the histological distribution of histoBlood Group Antigens, i.e. the ABO, Lewis, and saliva-secretor type of the individual, and the cell- and tissue type. Oligosaccharides with Blood-Group specificity are synthesized by the stepwise action of specific gene-encoded glycosyltransferases. In general, this stepwise synthesis of histo-Blood Group Antigens correlates with cellular differentiation. The H and the Se genes both encode an al-2fucosyltransferase, which is responsible for the synthesis of Blood Group antigen H from precursor disaccharides. A new model for the participation of the Se/H-gene-encoded glycosyl transferases in synthesis of terminal histo-Blood Group Antigens in human tissues is proposed; the type and degree of differentiation rather than the embryologic origin determines whether it is the H or the Se gene-encoded transferases that influence expression of terminal histo-Blood Group Antigens in tissues.

  • Tissue distribution of histo‐Blood Group Antigens.
    APMIS : acta pathologica microbiologica et immunologica Scandinavica, 2000
    Co-Authors: Vibeke Ravn, Erik Dabelsteen
    Abstract:

    The introduction of immunohistochemical techniques and monoclonal antibodies to specific carbohydrate epitopes has made it possible to study in detail the tissue distribution of histo-Blood Group Antigens and related carbohydrate structures. The present paper summarizes the available data concerning the histological distribution of histo-Blood Group Antigens and their precursor structures in normal human tissues. Studies performed have concentrated on carbohydrate Antigens related to the ABO, Lewis, and TTn Blood Group systems, i.e. histo-Blood Group Antigens carried by type 1, 2, and 3 chain carrier carbohydrate chains. Histo-Blood Group Antigens are found in most epithelial tissues. Meanwhile, several factors influence the type, the amount, and the histological distribution of histoBlood Group Antigens, i.e. the ABO, Lewis, and saliva-secretor type of the individual, and the cell- and tissue type. Oligosaccharides with Blood-Group specificity are synthesized by the stepwise action of specific gene-encoded glycosyltransferases. In general, this stepwise synthesis of histo-Blood Group Antigens correlates with cellular differentiation. The H and the Se genes both encode an al-2fucosyltransferase, which is responsible for the synthesis of Blood Group antigen H from precursor disaccharides. A new model for the participation of the Se/H-gene-encoded glycosyl transferases in synthesis of terminal histo-Blood Group Antigens in human tissues is proposed; the type and degree of differentiation rather than the embryologic origin determines whether it is the H or the Se gene-encoded transferases that influence expression of terminal histo-Blood Group Antigens in tissues.

Taiki Kano - One of the best experts on this subject based on the ideXlab platform.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

Kazuya Sakai - One of the best experts on this subject based on the ideXlab platform.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

Fumio Matsushita - One of the best experts on this subject based on the ideXlab platform.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.

  • Effects of plasma glycosyltransferase on the ABO(H) Blood Group Antigens of human von Willebrand factor
    International Journal of Hematology, 2018
    Co-Authors: Taiki Kano, Kazunao Kondo, Jiharu Hamako, Fumio Matsushita, Kazuya Sakai, Taei Matsui
    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.