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Heterogeneity of Degradation of B‐Cell Endocytosed Monoclonal Antibodies Reacting with Different sIgM Epitopes
Author(s) -
RUUD E.,
MICHAELSEN T.,
KINDBERG G. M.,
BERG T.,
FUNDERUD S.,
GODAL T.
Publication year - 1989
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1989.tb01128.x
Subject(s) - immunoglobulin light chain , epitope , monoclonal antibody , antibody , microbiology and biotechnology , chemistry , avidity , degradation (telecommunications) , intracellular , monoclonal , polyclonal antibodies , biology , biochemistry , immunology , telecommunications , computer science
The degradation of a panel of monoclonal antibodies (MoAb) bound to surface IgM (sIgM) was studied in three human Burkitt's lymphoma cell lines. The panel included MoAb that recognize several distinct epitopes associated with the F(cμ) 5 domain, the cμ 2 domain, and δ or λ light chains. The amount of degraded MoAb and the rate of their degradation varied considerably between the various antibodies. Properties of MoAb such as avidity or ability to cross‐link sIgM did not significantly influence their degradation. The most consistent correlation between rate of degradation and MoAb used was the location of the epitope recognized by the individual MoAb. Thus, 7 out of 8 anti‐light chain MoAb were degraded at a higher rate than 5 out of 5 anti‐F(cμ) 5 MoAb. One anti‐cμ 2 MoAb was degraded at a rate similar to the majority of anti‐light chain MoAb. The intracellular transport of an anti‐δ light chain MoAb and an anti‐F(cμ) 5 MoAb was studied in detail by subcellular fractionation in sucrose gradients. We found that the anti‐δ light chain MoAb was transported more rapidly to lysosomes than the anti‐F(cμ) 5 MoAb, showing that they were sorted differently intracellularly.