Impaired assembly and post-translational regulation of 26S proteasome in human end-stage heart failure.

ABSTRACT:

Background

This study examined the hypothesis that 26S proteasome dysfunction in human end-stage heart failure is associated with decreased docking of the 19S regulatory particle to the 20S proteasome. Previous studies have demonstrated that 26S proteasome activity is diminished in human end-stage heart failure associated with oxidation of the 19S regulatory particle Rpt5 subunit. Docking of the 19S regulatory particle to the 20S proteasome requires functional Rpt subunit ATPase activity and phosphorylation of the α-type subunits.

Methods and results

An enriched proteasome fraction was prepared from 7 human nonfailing and 10 failing heart explants. Native gel electrophoresis assessed docking of 19S to 20S proteasome revealing 3 proteasome populations (20S, 26S, and 30S prote

SUBMITTER: Day SM 

PROVIDER: S-EPMC3864674 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature