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Blood, 1 June 2001, Vol. 97, No. 11, pp. 3537-3543
NEOPLASIA
Role of galactosylation in the renal pathogenicity of murine
immunoglobulin G3 monoclonal cryoglobulins
Tsuguo Mizuochi,
Yves Pastore,
Kohdoh Shikata,
Aki Kuroki,
Shuichi Kikuchi,
Thierry Fulpius,
Munehiro Nakata,
Liliane Fossati-Jimack,
Luc Reininger,
Misao Matsushita,
Teizo Fujita, and
Shozo Izui
From the Department of Applied Biochemistry, Tokai
University, Hiratsuka, Kanagawa; the Department of Biochemistry,
Fukushima Medical University, Japan; the Department of
Pathology, Faculty of Medicine, University of Geneva,
Switzerland; and the Institut National de la Santé
et de la Recherche Médicale U 399, Marseilles,
France.
Cryoglobulin activity associated with murine immunoglobulin G3
(IgG3) has been shown to play a significant role in the development of
murine lupuslike glomerulonephritis. A fraction, but not all, IgG3
monoclonal antibodies are capable of inducing a severe acute lupuslike
glomerulonephritis as a result of direct localization of IgG3
cryoglobulins, suggesting the importance of qualitative features of
cryoglobulins in their nephritogenic activities. Here a remarkable
difference is shown in the renal pathogenicity of 2 murine IgG3
monoclonal cryoglobulins, identical in the amino acid sequences of
their heavy and light chains but different in galactosylation patterns
of oligosaccharide side chains because of their synthesis in different
myeloma cells. The antibody lacking the capacity to induce severe
glomerulonephritis displayed an increased proportion of galactosylated
heavy chains. Changes in conformation, as revealed by gel filtration
analysis, reduced cryoglobulin activity, and accelerated clearance
could account for the lack of the renal pathogenicity of the more
galactosylated variant. This observation provides a direct
demonstration for the role of IgG galactosylation in the pathogenic
potential of cryoglobulins.
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