Development of LC-MS Method for Detection of Mutant Uromodulin Protein

M. Yasuda Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

K. Kaneko Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

H. Hachisu Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

M. Ochiai Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

T. Yamanobe Central Laboratory of Analytical Biochemistry, School of Medicine, Teikyo University, Tokyo, Japan

K. Mawatari Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

K. Nakagomi Laboratory of Analytical Chemistry, School of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan

N. Minoura Graduate School of Bionics, Tokyo University of Technology, Tokyo, Japan

M. Hosoyamada Division of Pharmacotherapeutics, Faculty of Pharmacy, Keio University, Tokyo, Japan

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Abstract

Mutations in the uromodulin gene cause the autosomal disorders familial juvenile hyperuricemic nephropathy (FJHN) and medullary cystic kidney disease type 2 (MCKD2). However, methods to detect the mutant form of the uromodulin protein have not been developed. In this study, we developed a liquid chromatography-mass spectrometry (LC-MS) method for detection of the mutated uromodulin peptide (C148W). Our method can distinguish the mutant peptide, GWHWE, from wildtype peptide, GWHC*E. Using MS/MS analysis with a selected reaction monitoring (SRM) mode, peptide-specific fragment ions (m/z 714 → 381, 471, 567, and 679 for GWHWE and m/z 688 → 381, 445, 541, and 653 for GWHC*E) were detected.

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Development of LC-MS Method for Detection of Mutant Uromodulin Protein

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Development of LC-MS Method for Detection of Mutant Uromodulin Protein

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