Journal of Experimental Medicine, Vol 158, 1769-1774, Copyright © 1983 by Rockefeller University Press
A tumor-associated antigen specific for human kappa myeloma cells
HA Boux, RL Raison, KZ Walker, GE Hayden and A Basten
A monoclonal antibody (K-1-21) raised against a kappa Bence Jones protein
exhibits unique binding properties to malignant plasma cells. K- 1-21 is an
IgG1 kappa antibody that reacts with human kappa light chains in free form,
but shows no reactivity with heavy chain- associated kappa light chains. By
immunofluorescence, K-1-21 binds to the surface of LICR LON/HMy2 (HMy2)
kappa myeloma cells and to plasma cells from a majority (8/11) of patients
with various types of kappa myeloma; it did not bind to the surface of
normal cells, nor to malignant cells of non-kappa myeloma origin. Flow
cytometry analysis of K-1-21 binding to HMy2 cells indicated that the
surface reactivity of K- 1-21 could be completely inhibited by
preincubation of the antibody with purified kappa light chains, whereas no
inhibition occurred after preincubation with lambda chains or intact human
IgG. Thus, the epitope recognized by K-1-21 on the cell surface may be
similar, if not identical, to the determinant recognized on soluble free
kappa light chains, and constitutes a tumor-associated antigen with
selectivity for kappa myeloma cells. K-1-21 may therefore have clinical
potential in patients with kappa myeloma.
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