Proteome-wide measurement of protein half-lives and translation rates in vasopressin-sensitive collecting duct cells.

ABSTRACT: Vasopressin regulates water excretion, in part, by controlling the abundances of the water channel aquaporin-2 (AQP2) protein and regulatory proteins in the renal collecting duct. To determine whether vasopressin-induced alterations in protein abundance result from modulation of protein production, protein degradation, or both, we used protein mass spectrometry with dynamic stable isotope labeling in cell culture to achieve a proteome-wide determination of protein half-lives and relative translation rates in mpkCCD cells. Measurements were made at steady state in the absence or presence of the vasopressin analog, desmopressin (dDAVP). Desmopressin altered the translation rate rather than the stability of most responding proteins, but it significantly increased both the translation rate and

SUBMITTER: Sandoval PC 

PROVIDER: S-EPMC3810089 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature