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In heart failure patients, decreased phosphorylation of cMyBP-C has been attributed to reduced contractility. We used previously published cMyBP-C peptides 302A and 302S, surrogates of the regulatory phosphorylation site serine 302, as a way to determine the effects of modulating the dephosphorylation state of cMyBP-C on cardiac contraction and relaxation in experimental heart failure models in vitro. Both peptides increased the contractility of papillary muscle fibers isolated from a mouse model that exhibits cMyBP-C phospho-ablation constitutively. In particular, Peptide 302A could also increase the force redevelopment rate in papillary muscle fibers from cMyBP-C AAA mice. These results combined show that modulation of cMyBP-C dephosphorylation status can be a therapeutic strategy to increase myosin function, sarcomere contraction, and relaxation after an adverse cardiac event. Hence, targeting cMyBP-C could potentially increase overall cardiac function as a complement to standard-care drugs in HF patients.
Source link: https://europepmc.org/article/MED/35288601
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