Multiple reaction monitoring to identify site-specific troponin I phosphorylated residues in the failing human heart.

ABSTRACT:

Background

Human cardiac troponin I is known to be phosphorylated at multiple amino acid residues by several kinases. Advances in mass spectrometry allow sensitive detection of known and novel phosphorylation sites and measurement of the level of phosphorylation simultaneously at each site in myocardial samples.

Methods and results

On the basis of in silico prediction and liquid chromatography/mass spectrometry data, 14 phosphorylation sites on cardiac troponin I, including 6 novel residues (S4, S5, Y25, T50, T180, S198), were assessed in explanted hearts from end-stage heart failure transplantation patients with ischemic heart disease or idiopathic dilated cardiomyopathy and compared with samples obtained from nonfailing donor hearts (n=10 per group). Thirty mass spectromet

SUBMITTER: Zhang P 

PROVIDER: S-EPMC3733556 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature