Alterations in the interactome of serine/threonine protein phosphatase type-1 in atrial fibrillation patients.

ABSTRACT:

Background

Atrial fibrillation (AF) is the most common sustained cardiac arrhythmia, yet current pharmacological treatments are limited. Serine/threonine protein phosphatase type-1 (PP1), a major phosphatase in the heart, consists of a catalytic subunit (PP1c) and a large set of regulatory (R)-subunits that confer localization and substrate specificity to the holoenzyme. Previous studies suggest that PP1 is dysregulated in AF, but the mechanisms are unknown.

Objectives

The purpose of this study was to test the hypothesis that PP1 is dysregulated in paroxysmal atrial fibrillation (PAF) at the level of its R-subunits.

Methods

Cardiac lysates were coimmunoprecipitated with anti-PP1c antibody followed by mass spectrometry-based, quantitative profiling of associated R-subu

SUBMITTER: Chiang DY 

PROVIDER: S-EPMC4690213 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature