What does this research mean for the field?

Phosphorylation of cardiac myosin-binding protein-C (cMyBP-C) regulates the kinetics and amplitude of cardiac contraction by accelerating cross-bridge binding to actin and detachment, and its impairment contributes to systolic and diastolic dysfunction in heart failure. Novelty: ClaimNovelty.SYNTHESIS. Consensus alignment: ConsensusAlignment.NEUTRAL.

December 31, 2014Circulation ResearchOpen Access

Cardiac MyBP-C Regulates the Rate and Force of Contraction in Mammalian Myocardium

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Population

Mammalian myocardium

Comparison

Phosphorylation of cardiac myosin-binding… vs Dephosphorylated state

Design

Review

Authors

RMRichard L. MossUniversity of Vermont DFDaniel P. FitzsimonsUniversity of Idaho JRJ. Carter RalpheUniversity of Wisconsin–Madison

Discussion

Member takes

Implication

May underlie heart failure contractile defects; leaves open targeted modulation for future trials.

Structured PICO

Population

Mammalian myocardium

Intervention

Phosphorylation of cardiac myosin-binding protein-C (cMyBP-C)

Comparator

Dephosphorylated state

Outcome

Kinetics and amplitude of cardiac contractionsurrogate

Phosphorylation of cMyBP-C is a key regulator of cardiac contraction kinetics and amplitude, and its dysfunction may contribute to the pathophysiology of heart failure.

Cite This Study

Moss et al. (2014) studied this question.

synapsesocial.com/papers/6a1be651ea84844e355f2618 https://doi.org/10.1161/circresaha.116.300561

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Cardiac MyBP-C Regulates the Rate and Force of Contraction in Mammalian Myocardium

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Cardiac MyBP-C Regulates the Rate and Force of Contraction in Mammalian Myocardium

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider