ArticleJournal of molecular and cellular cardiology2026
Thin filament interaction and Ca
Article in Journal of molecular and cellular cardiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Troponin T (TnT), the tropomyosin (Tm)-binding subunit of troponin, plays a central role in regulating striated muscle contractility. The recently identified Tm-binding site 3 in the highly conserved C-terminal end segment of TnT has a troponin I (TnI)-like inhibitory function. A restrictive proteolytic removal of the N-terminal hypervariable region (amino acids 1-71) of cardiac TnT (cTnT-ND) in vivo in adaptation to inotropy-afterload mismatch slows down ventricular end-systolic velocity to increase ejection time and stroke volume through a conformational modulation that enhances the function of Tm-binding site 3. Mutations in this segment of cTnT cause hyperactivation of cardiac muscle and hypertrophic cardiomyopathy (HCM). Here we characterized isolated C-terminal end 14 amino acids (275-288) peptide of cTnT (cTnT-C14) for interactions with Tm, F-actin, and F-actin-Tm thin filament using localized surface plasmon resonance (LSPR). Wild-type cTnT-C14 peptide showed saturable strong binding to Tm and F-actin in LSPR, which is significantly weakened by HCM mutation R278C, K280N or R286C. Contractility studies of permeabilized mouse cardiac muscle strips found that the HCM mutant peptides all lost the known Ca
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