Ontology highlight
ABSTRACT:
SUBMITTER: Walweel K
PROVIDER: S-EPMC6791359 | biostudies-literature | 2019 May
REPOSITORIES: biostudies-literature
Walweel Kafa K Gomez-Hurtado Nieves N Rebbeck Robyn T RT Oo Ye Wint YW Beard Nicole A NA Molenaar Peter P Dos Remedios Cris C van Helden Dirk F DF Cornea Razvan L RL Knollmann Björn C BC Laver Derek R DR
Journal of molecular and cellular cardiology 20190327
Calmodulin (CaM) is a Ca-binding protein that binds to, and can directly inhibit cardiac ryanodine receptor calcium release channels (RyR2). Animal studies have shown that RyR2 hyperphosphorylation reduces CaM binding to RyR2 in failing hearts, but data are lacking on how CaM regulates human RyR2 and how this regulation is affected by RyR2 phosphorylation. Physiological concentrations of CaM (100 nM) inhibited the diastolic activity of RyR2 isolated from failing human hearts by ~50% but had no e ...[more]