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Urinary uromodulin carries an intact ZP domain generated by a conserved C-terminal proteolytic cleavage |
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| Authors: | Santambrogio Sara Cattaneo Angela Bernascone Ilenia Schwend Thomas Jovine Luca Bachi Angela Rampoldi Luca |
| Affiliation: | a Dulbecco Telethon Institute, Molecular Genetics of Renal Disorders, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy b Functional Proteomics, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy c Karolinska Institutet, Department of Biosciences and Nutrition, Hälsovägen 7, S-141 57 Huddinge, Sweden |
| Abstract: | Uromodulin (or Tamm-Horsfall protein) is the most abundant protein in human urine under physiological conditions. Little is known about the molecular mechanism of uromodulin secretion. By extensive Mass Spectrometry analyses we mapped the C-termini of human and murine urinary proteins demonstrating that urinary uromodulin is generated by a conserved C-terminal proteolytic cleavage and retains its entire ZP domain. |
| Keywords: | Uromodulin Zona pellucida domain Mass Spectrometry |
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