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Volume 271, Number 46, Issue of November 15, 1996 pp. 28792-28797
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Receptor-associated Protein and Members of the Low Density Lipoprotein Receptor Family Share a Common Epitope
AN EXTENDED MODEL FOR THE DEVELOPMENT OF PASSIVE HEYMANN NEPHRITIS

(Received for publication, July 22, 1996, and in revised form, August 27, 1996)

Thomas Hiesberger Dagger , Regina Hodits , Robert Ullrich , Markus Exner , Dontscho Kerjaschki , Wolfgang J. Schneider Dagger and Johannes Nimpf Dagger

From the Dagger  Department of Molecular Genetics, Biocenter and University of Vienna, Dr. Bohrgasse 9/2, A-1030 Vienna, Austria and  Department of Clinical Pathology, Section of Ultrastructural Pathology and Cell Biology, University of Vienna, A-1090 Vienna, Austria

Heymann nephritis is an experimental rat model for human membranous glomerulonephritis. Two target antigens have been identified in the proximal tubule brush border of rat kidneys. One of them is megalin, a 600-kDa membrane protein that belongs to the family of low density lipoprotein receptor (LDLR)-related proteins. The other one is receptor-associated protein (RAP), a polypeptide of 40 kDa that associates with members of the LDLR family. Here we show that antibodies produced against recombinant human RAP strongly cross-react with the chicken oocyte receptor for very low density lipoprotein and vitellogenin (LR8), and with two other members of the LDLR family, LDLR-related protein and megalin. The interaction of this antibody with LR8 showed binding characteristics exactly as those demonstrated for the physiological ligands of this receptor, in that binding of the antibody: (i) is Ca2+-dependent; (ii) is abolished by unfolding of the cysteine-rich binding domain by reduction; and (iii) interferes with the binding of very low density lipoprotein and vitellogenin. Immunopurification of the LR8-specific subpopulation of the polyclonal antiserum yielded an IgG fraction strongly reacting with LR8 as well as with RAP. Using recombinant fragments of RAP and peptide mapping, the cross-reacting epitope(s) could be narrowed down to three short sequences (5-7 residues) in the COOH-terminal part of the protein. After immunization with RAP, anti-LR8 antibodies and anti-RAP antibodies arise simultaneously, indicating that the receptor-specific activity is not due to anti-idiotypic antibodies. These findings suggest the existence of a common epitope(s) on RAP and members of the LDL receptor family. Based on these results, we present an extended molecular model for the development of passive Heymann nephritis.


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