{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Papadaki M"],"funding":["Austrian Science Fund FWF","NHLBI NIH HHS"],"pagination":["1-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8766917"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["162"],"pubmed_abstract":["Diabetes doubles the risk of developing heart failure (HF). As the prevalence of diabetes grows, so will HF unless the mechanisms connecting these diseases can be identified. Methylglyoxal (MG) is a glycolysis by-product that forms irreversible modifications on lysine and arginine, called glycation. We previously found that myofilament MG glycation causes sarcomere contractile dysfunction and is increased in patients with diabetes and HF. The aim of this study was to discover the molecular mechanisms by which MG glycation of myofilament proteins cause sarcomere dysfunction and to identify therapeutic avenues to compensate. In humans with type 2 diabetes without HF, we found increased glycation of sarcomeric actin compared to non-diabetics and it correlated with decreased calcium sensitivit"],"journal":["Journal of molecular and cellular cardiology"],"pubmed_title":["Myofilament glycation in diabetes reduces contractility by inhibiting tropomyosin movement, is rescued by cMyBPC domains."],"pmcid":["PMC8766917"],"funding_grant_id":["R01 HL136737","R01 HL141086","I 4168","R01 HL147570"],"pubmed_authors":["von Lewinski D","Papadaki M","Campbell SG","Harris SP","Kirk JA","Kampaengsri T","Rainer PP","Greenberg MJ","Barrick SK"],"additional_accession":[]},"is_claimable":false,"name":"Myofilament glycation in diabetes reduces contractility by inhibiting tropomyosin movement, is rescued by cMyBPC domains.","description":"Diabetes doubles the risk of developing heart failure (HF). As the prevalence of diabetes grows, so will HF unless the mechanisms connecting these diseases can be identified. Methylglyoxal (MG) is a glycolysis by-product that forms irreversible modifications on lysine and arginine, called glycation. We previously found that myofilament MG glycation causes sarcomere contractile dysfunction and is increased in patients with diabetes and HF. The aim of this study was to discover the molecular mechanisms by which MG glycation of myofilament proteins cause sarcomere dysfunction and to identify therapeutic avenues to compensate. In humans with type 2 diabetes without HF, we found increased glycation of sarcomeric actin compared to non-diabetics and it correlated with decreased calcium sensitivit","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2025-04-21T15:23:33.355Z","creation":"2025-04-21T15:23:33.355Z"},"accession":"S-EPMC8766917","cross_references":{"pubmed":["34487755"],"doi":["10.1016/j.yjmcc.2021.08.012"]}}