ArticleThe Journal of experimental medicine1996
Induction of passive Heymann nephritis with antibodies specific for a synthetic peptide derived from the receptor-associated protein.
Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Receptor-mediated endocytosis by Megalin: Exploring its role in ligand interaction and disease mechanisms.Genes & diseases · 2026Review
- Molecular mimicry in pauci-immune focal necrotizing glomerulonephritis.Nature medicine · 2008Article
- Experimental membranous nephropathy redux.American journal of physiology. Renal physiology · 2005Review
- T cell lines specific for a synthetic Heymann nephritis peptide derived from the receptor-associated protein.Clinical and experimental immunology · 2000Article
- Nephrin localizes at the podocyte filtration slit area and is characteristically spliced in the human kidney.The American journal of pathology · 1999Article
- The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes.Molecular biology of the cell · 1997Article
- Mapping rat megalin: the second cluster of ligand binding repeats contains a 46-amino acid pathogenic epitope involved in the formation of immune deposits in Heymann nephritis.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Passive Heymann nephritis (pHN) is an experimental rat model for human membranous glomerulopathy. In pHN, the formation of subepithelial immune deposits (ID) involves as antigenic targets the membrane glycoprotein gp330/megalin and the 44-kD receptor-associated protein (RAP). A single binding site for ID- inducing antibodies (Abs) was previously mapped to the 86 NH2-terminal amino acids of RAP (RAP1-86). To further narrow this epitope, Abs eluted from the glomeruli were immunoblotted on membranes that were loaded with overlapping synthetic peptides representing the amino acid sequence of RAP (SPOTs system). Two adjacent Ab-binding domains with the sequences PVRLAF, (amino acids 39-44) and HSD-LKIQE (amino acids 46-53), which were separated by a single L residue at amino acid 45, were detected. Rabbit Abs raised against synthetic peptides containing these domains individually (P31-44 and P46-53) failed to procedure glomerular IDs. By contrast, Abs raised against a larger composite peptide (P31-53) induced IDs within 3d that were firmly cross linked to the glomerular basement membrane. These data suggest that Ab binding in vivo depends on the conformation of the antigenic target sequence that is preserved in the synthetic peptide P31-53, which covers the entire Ab-binding domain of RAP but not in its subdomains, P31-44 and P46-53. Collectively, these results locate the sole ID-inducing epitope of RAP to amino acids 39-53.
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