Key result
Cardiomyopathy-related cTnI mutations sensitized acto-S1 ATPase to Ca2+ and increased Ca2+ binding to reconstituted thin filaments with less cooperativity compared to wild-type cTnI.
Population
Reconstituted cardiac thin filaments containing cardiomyopathy-related mutant cardiac troponin I (cTnI)
Comparison
cTnI mutations vs Wild-type cTnI
Design
Preclinical
Authors
Loading...
May promote arrhythmia triggers in cTnI cardiomyopathy; leaves open human translation from animal models.
Cardiomyopathy-related cTnI mutations increase the Ca2+ affinity of cardiac thin filaments, which may be an important factor in triggered arrhythmias associated with cardiomyopathy.
Kobayashi et al. (2006) studied Cardiomyopathy. Cardiomyopathy-related mutant cardiac troponin I (cTnI) vs. Wild-type cTnI was evaluated on Ca2+ binding properties and acto-S1 ATPase activities. Cardiomyopathy-related cTnI mutations sensitized acto-S1 ATPase to Ca2+ and increased Ca2+ binding to reconstituted thin filaments with less cooperativity compared to wild-type cTnI.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: