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J Appl Physiol (July 30, 2004). doi:10.1152/japplphysiol.01090.2003
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Submitted on October 8, 2003
Accepted on July 23, 2004

Light chains are a ligand for megalin

R. Bryan S. Klassen1, Patricia L Allen2, Vecihi Batuman2, Kimberly Crenshaw3, and Timothy G Hammond3*

1 Department of Chemistry, Xavier University, New Orleans, LA, USA; Department of Medicine, New Orleans Veterans Affairs Medical Center, New Orleans, LA, USA
2 Tulane/VA Environmental Astrobiology Center, Tulane University School of Medicine, New Orleans, LA, USA; Department of Medicine, New Orleans Veterans Affairs Medical Center, New Orleans, LA, USA
3 Department of Chemistry, Xavier University, New Orleans, LA, USA

* To whom correspondence should be addressed. E-mail: thammond{at}tulane.edu.

Cubilin and megalin are giant glycoprotein receptors abundant on the luminal surface of proximal tubular cells of the kidney. We have shown previously that light chains are a ligand for cubilin. As cubilin and megalin share a number of common ligands, we further investigated the ligand specificity of these receptors. Two lines of evidence suggest that light chains are a ligand for megalin: (1) anti-megalin antiserum largely displaces brush border light chain binding more than anti-cubilin antiserum, and (9) direct binding studies on isolated proteins using surface plasmon resonance techniques confirm that megalin binds light chains. The megalin-light chain interaction is divalent ion dependent, and similar for both {kappa} and {lambda} light chains. A fit of the data on light chain binding to megalin over a concentration range 0.078 -- 2.5 mg/mL leads to an estimated dissociation constant of 6 x 10-5 M, corresponding approximately to one light chain-binding site per megalin. These data suggest that light chains bind the tandem megalin-cubilin complex. And some light chains bind preferentially with higher affinity to megalin rather than cubilin.




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