title: Urinary uromodulin carries an intact ZP domain generated by a conserved C-terminal proteolytic cleavage.
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.
authors: Dulbecco Telethon Institute, Molecular Genetics of Renal Disorders, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy.
authors: Sara
authors: S
authors: Santambrogio
authors: Angela
authors: A
authors: Cattaneo
authors: Ilenia
authors: I
authors: Bernascone
authors: Thomas
authors: T
authors: Schwend
authors: Luca
authors: L
authors: Jovine
authors: Angela
authors: A
authors: Bachi
authors: Luca
authors: L
authors: Rampoldi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D006801:Humans; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009088:Mucoproteins / Q000737:chemistry* / Q000378:metabolism / Q000652:urine*; D017434:Protein Structure, Tertiary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D058949:Uromodulin
chemical_list: D009088:Mucoproteins; C548612:UMOD protein, human; C548613:Umod protein, mouse; D058949:Uromodulin