Phosphoproteomic profiling reveals vasopressin-regulated phosphorylation sites in collecting duct.

ABSTRACT: Protein phosphorylation is an important component of vasopressin signaling in the renal collecting duct, but the database of known phosphoproteins is incomplete. We used tandem mass spectrometry to identify vasopressin-regulated phosphorylation events in isolated rat inner medullary collecting duct (IMCD) suspensions. Using multiple search algorithms to identify the phosphopeptides from spectral data, we expanded the size of the existing collecting duct phosphoproteome database from 367 to 1187 entries. Label-free quantification in vasopressin- and vehicle-treated samples detected a significant change in the phosphorylation of 29 of 530 quantified phosphopeptides. The targets include important structural, regulatory, and transporter proteins. The vasopressin-regulated sites included two kn

SUBMITTER: Bansal AD 

PROVIDER: S-EPMC2834543 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature