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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
Published on: June 29, 2016
Myeloma light chains are ligands for cubilin (gp280)
V Batuman1, P J Verroust, G L Navar
1Department of Medicine/Section of Nephrology, Tulane University School of Medicine, Tulane Environmental Astrobiology Center,, New Orleans, Louisiana 70112, USA.
The American Journal of Physiology
|August 5, 1998
Summary
Cubilin (gp280) acts as a receptor for myeloma light chains in the kidney, facilitating their endocytosis and trafficking. Further research is needed to identify additional binding sites.
Area of Science:
- Nephrology
- Molecular Biology
- Cell Biology
Background:
- Myeloma light chains are known to be endocytosed by kidney cells.
- The specific receptor responsible for this process has remained unidentified.
Purpose of the Study:
- To identify the molecular receptor involved in myeloma light chain endocytosis in the kidney.
- To characterize the interaction between cubilin and myeloma light chains.
Main Methods:
- Immunoaffinity purification of cubilin.
- Displacement assays using polyclonal antisera to cubilin.
- Surface plasmon resonance to assess binding kinetics.
- In vitro studies on endosomal fusion and endocytosis inhibition.
Main Results:
- Cubilin coeluted with light chains during purification.
- Anti-cubilin antibodies partially inhibited light chain binding and endocytosis.
- Cubilin demonstrated binding to multiple light chain species.
- Excess light chains inhibited endosomal fusion, indicating complex trafficking roles.
Conclusions:
- Cubilin is a physiologically relevant binding site for myeloma light chains in renal proximal tubule cells.
- Cubilin plays a role in the endocytosis and trafficking of light chains.
- Additional or alternative binding sites for light chains may exist.

