In the current era of large-scale biology, proteomics has evolved as a powerful, new
technique that aims to identify, quantify, and analyze a large number of proteins in a functional
context. Therefore, proteomics can be used to study cellular pathways and identify disease
biomarkers. In this review, we first outline the principles of two important proteomics
techniques that either use difference gel electrophoresis (DIGE) or liquid chromatography
(LC) for protein separation, followed by tandem mass spectrometry (MS/MS). The advantages
and limitations of each technique are discussed, emphasizing the ability of DIGE to
perform quantitative proteomics and the high-throughput and high-sensitivity characteristics
of LC-MS/MS. We have employed both techniques to unravel the molecular machinery of
vasopressin signaling, which governs water homeostasis by recruiting aquaporin-2 (AQP2)
water channels after activation of the vasopressin-2 receptor by vasopressin. Several aspects
of vasopressin signaling in the inner medullary collecting duct (IMCD) were investigated,
including the short- and long-term regulation of AQP2, phosphoproteomics, signaling during
vasopressin escape, and the proteomes of AQP2-bearing vesicles and the IMCD plasma
membranes. We also emphasize that proteomics of body fluids will be the strategy to identify
disease biomarkers, and therefore conclude the review by highlighting the perspectives of
biomarker discovery in urinary exosomes.
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