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Science 18 September 1987:
Vol. 237. no. 4821, pp. 1479 - 1484
DOI: 10.1126/science.3498215
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Articles
Science, Vol 237, Issue 4821, 1479-1484
Copyright © 1987 by American Association for the Advancement of Science
Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines
C Hession,
JM Decker,
AP Sherblom,
S Kumar,
CC Yue,
RJ Mattaliano,
R Tizard,
E Kawashima,
U Schmeissner,
S Heletky,
and
al. et
The protein portion of the immunosuppressive glycoprotein uromodulin is identical to the Tamm-Horsfall urinary glycoprotein and is synthesized in the kidney. Evidence that the glycoproteins are the same is based on amino acid sequence identity, immunologic cross-reactivity, and tissue localization to the thick ascending limb of Henle's loop. Nucleic acid sequencing of clones for uromodulin isolated from a complementary DNA bank from human kidney predicts a protein 639 amino acids in length, including a 24--amino acid leader sequence and a cysteine-rich mature protein with eight potential glycosylation sites. Uromodulin and preparations of Tamm-Horsfall glycoprotein bind to recombinant murine interleukin-1 (rIL-1) and human rIL-1 alpha, rIL-1 beta, and recombinant tumor necrosis factor (rTNF). Uromodulin isolated from urine of pregnant women by lectin adherence is more immunosuppressive than material isolated by the original salt-precipitation protocol of Tamm and Horsfall. Immunohistologic studies demonstrate that rIL-1 and rTNF bind to the same area of the human kidney that binds to antiserum specific for uromodulin. Thus, uromodulin (Tamm-Horsfall glycoprotein) may function as a unique renal regulatory glycoprotein that specifically binds to and regulates the circulating activity of a number of potent cytokines, including IL-1 and TNF.
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