A murine monoclonal IgM antibody specific for blood group P antigen (globoside)

A murine monoclonal IgM antibody specific for blood group P antigen (globoside) Summary A murine monoclonal IgM erythrocyte antibody appeared to have anti‐P (anti‐globoside) specificity. The antibody was a relatively weak cold agglutinin, but a strong haemolysin and its reactivity with red cells was markedly enhanced by enzyme treatment. This antibody was used to study the cell and tissue distribution of globoside. Globoside was not only detectable on red cells and erythroblasts, but also on endothelial cells and on subsets of platelets, megakaryocytes and fibroblasts. It was not detectable on granulocytes, monocytes and most peripheral blood lymphocytes. Neither was it present on erythroblast precursors (CFU‐E, BFU‐E), pro‐erythroblasts or on the cells of the pro‐erythroblastic cell lines K562 and HEL. However, K562 cells expressed globoside when induced to mature into erythroblasts by sodium butyrate. Cells of patients with various leukaemias were also tested. A significant number of positively reacting cells was frequently (six out of 18) seen in cases with a CML blast crisis (CML‐BC) and rarely in AML (four out of 37 cases). In CML‐BC the P‐positive cells were probably erythroblasts and/or megakaryoblasts. Thus, globoside appeared to be an interesting marker in CML‐BC of the erythroblastic or mixed erythroblastic‐megakaryoblastic type. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png British Journal of Haematology Wiley

A murine monoclonal IgM antibody specific for blood group P antigen (globoside)

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Publisher
Wiley
Copyright
Copyright © 1986 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0007-1048
eISSN
1365-2141
D.O.I.
10.1111/j.1365-2141.1986.tb07492.x
Publisher site
See Article on Publisher Site

Abstract

Summary A murine monoclonal IgM erythrocyte antibody appeared to have anti‐P (anti‐globoside) specificity. The antibody was a relatively weak cold agglutinin, but a strong haemolysin and its reactivity with red cells was markedly enhanced by enzyme treatment. This antibody was used to study the cell and tissue distribution of globoside. Globoside was not only detectable on red cells and erythroblasts, but also on endothelial cells and on subsets of platelets, megakaryocytes and fibroblasts. It was not detectable on granulocytes, monocytes and most peripheral blood lymphocytes. Neither was it present on erythroblast precursors (CFU‐E, BFU‐E), pro‐erythroblasts or on the cells of the pro‐erythroblastic cell lines K562 and HEL. However, K562 cells expressed globoside when induced to mature into erythroblasts by sodium butyrate. Cells of patients with various leukaemias were also tested. A significant number of positively reacting cells was frequently (six out of 18) seen in cases with a CML blast crisis (CML‐BC) and rarely in AML (four out of 37 cases). In CML‐BC the P‐positive cells were probably erythroblasts and/or megakaryoblasts. Thus, globoside appeared to be an interesting marker in CML‐BC of the erythroblastic or mixed erythroblastic‐megakaryoblastic type.

Journal

British Journal of HaematologyWiley

Published: May 1, 1986

References

  • Studies on the biosynthetic pathway of human P erythrocyte antigens using somatic cells in culture
    Fellous, Fellous; Gerbal, Gerbal; Tessier, Tessier; Frezal, Frezal; Dausset, Dausset; Salmon, Salmon
  • Studies on the biosynthetic pathway of human P erythrocyte antigen using genetic complementation tests between fibroblasts from rare p and p k phenotype donors
    Fellous, Fellous; Gerbal, Gerbal; Nobillot, Nobillot; Wiels, Wiels
  • Differential reactivity of fetal and adult human erythrocytes to antisera directed against glycolipids of human erythrocytes
    Hakomori, Hakomori
  • Monoclonal antibodies against human glycoprotein IIIa
    Tetteroo, Tetteroo; Lansdorp, Lansdorp; Leeksma, Leeksma; Borne, Borne
  • Monoclonal antibody against a Burkitt‐lymphoma‐associated antigen
    Wiels, Wiels; Fellous, Fellous; Tunsz, Tunsz

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