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J Biol Chem, Vol. 274, Issue 25, 17518-17524, June 18, 1999
From the Departments of Internal Medicine and of Cellular and
Molecular Physiology, Yale University School of Medicine,
New Haven, Connecticut 06520-8029
We investigated whether the renal brush border
Na+/H+ exchanger NHE3 exists in
assemblies with other proteins in native kidney membranes. To this end
we generated monoclonal antibodies (mAbs) against affinity purified
NHE3 protein complexes. Hybridomas were selected based on ability to
immunoprecipitate NHE3. One of the resulting mAbs (10A3) labeled a high
molecular mass (>200 kDa) protein and stained primarily the coated pit
region of the proximal tubule in a manner similar to that described for
megalin (gp330). We then confirmed that both mAb 10A3 and a known
anti-megalin mAb immunoprecipitated and immunoblotted the same protein,
namely megalin. mAb 10A3 specifically co-precipitated NHE3 but not
villin or NaPi-2 from solubilized renal membranes,
indicating specificity of the NHE3-megalin interaction. When
immunoprecipitations were performed using either 10A3 or anti-NHE3 mAb
2B9 after separation of solubilized renal proteins by sucrose velocity
gradient centrifugation, we found that NHE3 exists in two states with
distinct sedimentation coefficients, a 9.6 S megalin-free form and a
21 S megalin-bound form, and that when NHE3 assembles with megalin,
epitopes within the carboxyl-terminal 131 amino acids of NHE3 are
blocked. Taken together, these findings indicate that a significant
pool of NHE3 exists as a multimeric complex with megalin in the brush
border of the proximal tubule.
Specific Association of Megalin and the
Na+/H+ Exchanger Isoform NHE3 in the Proximal
Tubule
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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