NDT Advance Access originally published online on April 19, 2005
Nephrology Dialysis Transplantation 2005 20(7):1290-1294; doi:10.1093/ndt/gfh851
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© The Author [2005]. Published by Oxford University Press on behalf of ERA-EDTA. All rights reserved. For Permissions, please email: journals.permissions@oupjournals.org
Editorial Comment
Tamm–Horsfall protein or uromodulin: new ideas about an old molecule
Divisions of Nephrology and Genetics, Université catholique de Louvain Medical School, B-1200 Brussels, Belgium
Correspondence and offprint requests to: Olivier Devuyst, MD, PhD, Division of Nephrology, UCL Medical School, 10 Avenue Hippocrate, B-1200 Brussels, Belgium. Email: devuyst@nefr.ucl.ac.be
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The discovery and re-discovery of Tamm–Horsfall protein/uromodulin |
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More than 50 years ago, Tamm and Horsfall isolated a mucoprotein from the human urine, and showed that the protein was able to interact and inhibit viral haemagglutination [1,2]. Of interest, the protein was found to be heavily glycosylated, containing up to 30% of its mass in carbohydrates [3]. It was then discovered that the Tamm–Horsfall protein (THP), as it was readily named, was the most abundant protein in normal human urine, with a migration pattern at
90 kDa in SDS–PAGE [4]. In 1985, Muchmore and Decker [5] identified a 85 kDa glycoprotein in the urine of pregnant women. The protein was named uromodulin, due to its potent immunosuppressive activity reflecting its ability to inhibit antigen-induced T-cell proliferation and monocyte cytotoxicity in vitro [5]. Besides the molecular mass and the abundance in urine, the characterization of uromodulin revealed |
Uromodulin: biochemical properties and distribution |
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Role and pathophysiology of uromodulin |
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Pathogenic mutations of UMOD impair uromodulin trafficking |
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Uromodulin knock-out mouse models |
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Of mouse and man: unsolved issues and future perspectives in uromodulin research |
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Conclusion |
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