Modulation of myosin by cardiac myosin binding protein-C peptides improves cardiac contractility in ex-vivo experimental heart failure models.

ABSTRACT: Cardiac myosin binding protein-C (cMyBP-C) is an important regulator of sarcomeric function. Reduced phosphorylation of cMyBP-C has been linked to compromised contractility in heart failure patients. Here, we used previously published cMyBP-C peptides 302A and 302S, surrogates of the regulatory phosphorylation site serine 302, as a tool to determine the effects of modulating the dephosphorylation state of cMyBP-C on cardiac contraction and relaxation in experimental heart failure (HF) models in vitro. Both peptides increased the contractility of papillary muscle fibers isolated from a mouse model expressing cMyBP-C phospho-ablation (cMyBP-C^AAA) constitutively. Peptide 302A, in particular, could also improve the force redevelopment rate (k_tr) in papillary muscle fibers

SUBMITTER: Hou L 

PROVIDER: S-EPMC8921245 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature