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Article

PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness.

Circulation research - 25 Sept 2009

Hidalgo Carlos, Hudson Bryan, Bogomolovas Julius, Zhu Yi, Anderson Brian, Greaser Marion, Labeit Siegfried, Granzier Henk

Abstract excerpt

RATIONALE: Protein kinase C (PKC) regulates contractility of cardiac muscle cells by phosphorylating thin- and thick- filament-based proteins. Myocardial sarcomeres also contain a third myofilament, titin, and it is unknown whether titin can be phosphorylated by PKC and whether it affects passive tension. OBJECTIVE: The purpose of this study was to examine the effect of PKC on titin phosphorylation and...

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Identifiers

PMID: 19679839
DOI: 10.1161/CIRCRESAHA.109.198465
PMCID: PMC2764991

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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