Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein

D Pennica, WJ Kohr, WJ Kuang, D Glaister… - Science, 1987 - science.org
D Pennica, WJ Kohr, WJ Kuang, D Glaister, BB Aggarwal, EY Chen, DV Goeddel
Science, 1987science.org
The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein
with in vitro immunosuppressive properties, was determined through isolation and
characterization of complementary DNA and genomic clones. The amino acid sequence
encoded by one of the exons of the uromodulin gene has homology to the low-density-
lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization
analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided …
The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.
AAAS