ArticleProceedings of the National Academy of Sciences of the United States of America1997
Identification of the second cluster of ligand-binding repeats in megalin as a site for receptor-ligand interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 74 citations in OpenAlex.
- Megalin: from structure to function.Nature reviews. Nephrology · 2026Review
- Receptor-mediated endocytosis by Megalin: Exploring its role in ligand interaction and disease mechanisms.Genes & diseases · 2026Review
- Antigens in membranous nephropathy: discovery and clinical implications.Nature reviews. Nephrology · 2025Review
- Efficiency of succinylated gelatin and amino acid infusions for kidney uptake reduction of radiolabeled αvβ6-integrin targeting peptides: considerations on clinical safety profiles.European journal of nuclear medicine and molecular imaging · 2024Article
- Cryo-EM structures elucidate the multiligand receptor nature of megalin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Towards the Magic Radioactive Bullet: Improving Targeted Radionuclide Therapy by Reducing the Renal Retention of Radioligands.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Article
- Tc-99m-labeled RGD-conjugated alpha-melanocyte stimulating hormone hybrid peptides with reduced renal uptake.Amino acids · 2015Article
- Megalin contributes to kidney accumulation and nephrotoxicity of colistin.Antimicrobial agents and chemotherapy · 2013Article
- Mapping the binding region on the low density lipoprotein receptor for blood coagulation factor VIII.The Journal of biological chemistry · 2013Article
- Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin.The Journal of biological chemistry · 2013Article
- Article
- Renal uptake of different radiolabelled peptides is mediated by megalin: SPECT and biodistribution studies in megalin-deficient mice.European journal of nuclear medicine and molecular imaging · 2011Article
- Intrarenal renin angiotensin system revisited: role of megalin-dependent endocytosis along the proximal nephron.The Journal of biological chemistry · 2010Article
- Albumin-derived peptides efficiently reduce renal uptake of radiolabelled peptides.European journal of nuclear medicine and molecular imaging · 2010Article
- Receptor-mediated endocytosis in renal proximal tubule.Pflugers Archiv : European journal of physiology · 2009Review
- Article
- The cellular biochemistry of cholesterol and statins: insights into the pathophysiology and therapy of Alzheimer's disease.CNS drug reviews · 2004Review
- Autoantibodies to low-density-lipoprotein-receptor-related protein 2 (LRP2) in systemic autoimmune diseases.Arthritis research & therapy · 2003Article
- Functional and structural properties of lipid-associated apolipoprotein J (clusterin).The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Megalin is a large cell surface receptor that mediates the binding and internalization of a number of structurally and functionally distinct ligands from the lipoprotein and protease:protease inhibitor families. To begin to address how megalin is able to bind ligands with unique structurally properties, we have mapped a binding site for apolipoprotein E (apoE)-beta very low density lipoprotein (beta VLDL), lipoprotein lipase, aprotinin, lactoferrin, and the receptor-associated protein (RAP) within the primary sequence of the receptor. RAP is known to inhibit the binding of all ligands to megalin. We identified a ligand-binding site on megalin by raising mAb against purified megalin, selected for a mAb whose binding to megalin is inhibited by RAP, and mapped the epitope for this mAb. mAb AC10 inhibited the binding of apoE-beta VLDL, lipoprotein lipase, aprotinin, and lactoferrin to megalin in a concentration-dependent manner. When cDNA fragments encoding the four cysteine-rich ligand-binding repeats in megalin were expressed in a baculovirus system and immunoblotted with AC10, it recognized only the second cluster of ligand-binding repeats. The location of the epitope recognized by mAb AC10 within this domain was pinpointed to amino acids 1111-1210. From these studies we conclude that the binding of apoE-beta VLDL, lactoferrin, aprotinin, lipoprotein lipase, and RAP to megalin is either competitively or sterically inhibited by mAb AC10 suggesting that these ligands bind to the same or closely overlapping sites within the second cluster of ligand-binding repeats.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.