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A novel membrane antigen selectively expressed on terminally differentiated
human B cells
T Goto, SJ Kennel, M Abe, M Takishita, M Kosaka, A Solomon and S Saito
First Department of Internal Medicine, School of Medicine, University of
Tokushima, Japan.
A monoclonal antibody (MoAb) that defines a novel terminal B-cell-
restricted antigen, termed HM1.24, was developed against a human plasma
cell line. The MoAb, designated anti-HM1.24, reacted with five different
human myeloma cell lines, as well as with monoclonal neoplastic plasma
cells obtained from the bone marrow or peripheral blood of patients with
multiple myeloma or Waldenstrom's macroglobulinemia. The HM1.24 antigen was
also expressed by mature Ig- secreting B cells (plasma cells and
lymphoplasmacytoid cells) but not by other cells contained in the
peripheral blood, bone marrow, liver, spleen, kidney, or heart of normal
individuals or patients with non- plasma-cell-related malignancies. The
anti-HM1.24 MoAb bound to human myeloma RPMI 8226 cells with an affinity
constant of 9.2 x 10(8) M-1, indicating approximately 84,000 sites/cell. By
immunoprecipitation assay under reducing conditions, this MoAb identified a
membrane glycoprotein that had a molecular weight of 29 to 33 kD. Our
studies indicate that the HM1.24-related protein represents a specific
marker of late-stage B-cell maturation and potentially serves as a target
antigen for the immunotherapy of multiple myeloma and related plasma cell
dyscrasias.
Volume 84,
Issue 6,
pp. 1922-1930,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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