Ontology highlight
ABSTRACT: Background
O-GlcNAcylation is the enzymatic addition of a sugar, O-linked β-N-Acetylglucosamine, to the serine and threonine residues of proteins, and is abundant in diabetic conditions. We have previously shown that O-GlcNAcylation can trigger arrhythmias by indirectly increasing pathological Ca2+ leak through the cardiac ryanodine receptor (RyR2) via Ca2+/calmodulin-dependent kinase II (CaMKII). However, RyR2 is well known to be directly regulated by other forms of serine and threonine modification, therefore, this study aimed to determine whether RyR2 is directly modified by O-GlcNAcylation and if this also alters the function of RyR2 and Ca2+ leak.Methods
O-GlcNAcylation of RyR2 in diabetic human and animal hearts was determined using we
SUBMITTER: Okolo CA
PROVIDER: S-EPMC10576323 | biostudies-literature | 2023 Oct
REPOSITORIES: biostudies-literature