M. Abe et al., PRODUCTION AND IMMUNODIAGNOSTIC APPLICATIONS OF ANTIHUMAN LIGHT-CHAINMONOCLONAL-ANTIBODIES, American journal of clinical pathology, 100(1), 1993, pp. 67-74
Hybridomas producing antihuman light chain monoclonal antibodies (MoAb
s) were derived from fusion of SP2/O mouse myeloma cells with splenic
lymphocytes from mice repeatedly immunized with purified kappa- and la
mbda-type Bence Jones proteins representative of the major V(kappa) (V
(kappaI), V(kappaII), V(kappaIII), V(kappaIV)) and V(lambda) (V(lambda
I), V(lambdaII/V) V(lambdaIII), V(lambdaIV), V(lambdaVI)) subgroups or
gene families. Monoclonal antibodies were obtained that had specifici
ty for constant-region (C(L)) determinants common to all kappa or lamb
da light chains (C(kappa) and C(lambda), respectively) as well as for
variable-region (V(L)) epitopes unique to each of the V(kappa) or V(la
mbda) subgroups. The capability of these reagents to recognize C(L) an
d V(L) determinants on monoclonal immunoglobulin (Ig) molecules was de
monstrated in fluid-phase antigen-capturing enzyme-linked immunosorben
t assay (ELISA), solid-phase ELISA, and immunoblotting. In addition, t
hese antilight chain MoAbs were used to establish immunocytochemically
the kappa or lambda type and V(L)-subgroup nature of light chains exp
ressed by the cytoplasmic Ig of monoclonal plasma cell and surface Ig
of B-lymphocyte populations, respectively. These antibodies facilitate
d the immunohistochemical detection and characterization of light-chai
n-associated amyloid (AL amyloid) and other types of light-chain-relat
ed tissue deposits. Furthermore, the anti-C(L)-specific MoAbs were use
d to measure serum and urinary Igkappa and Iglambda concentrations. Qu
antification of Bence Jones protein excretion, even in the presence of
other urinary proteins, was possible using the highly sensitive anti-
C(kappa) and anti-C(lambda) MoAbs reactive only with free light chains
. The ability to identify and characterize, through the use of these a
ntihuman light chain MoAbs, light-chain-related epitopes at the protei
n, cellular, and tissue level has clinical importance in the diagnosis
and treatment of patients with monoclonal plasma cell and related B-c
ell immunoproliferative diseases.