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- Title
Heterogeneity of Degradation of B-Cell Endocytosed Monoclonal Antibodies Reacting with Different slgM Epitopes.
- Authors
Ruud, E.; Michaelsen, T.; Kindberg, G. M.; Berg, T.; Funderud, S.; Godal, T.
- Abstract
The degradation of a panel of monoclonal antibodies (MoAB) bound to surface IgM (sIgM) was studied in three human Burkitt's lymphorma cell lines. The panel included MoAB that recognize several distinct epitopes associated with the F(Cμ)3 domain, the cμ2 domain, and κ 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 that 5 out of 5 anti-F(cμ)3 MoAb. One anti &cμ2 MoAb was degraded at a rate similar to the majority of anti-light chain MoAb. The intracellular transport of an anti-κ light chain MoAb and an anti-F(cμ)3 MoAb was studied in detail by subcellular fractionation in sucrose gradients. We found that the anti-κ light chain MoAb was transported more rapidly to lysosomes than the anti-F(cμ)3 MoAb, showing that they were sorted differently intracellularly.
- Subjects
IMMUNOGLOBULINS; MONOCLONAL antibodies; EPITOPES; CELL culture; CELL lines
- Publication
Scandinavian Journal of Immunology, 1989, Vol 29, Issue 3, p299
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1989.tb01128.x