What does this research mean for the field?

Cardiac contractility is regulated by the shifting of the NH2 terminus of Myosin Binding Protein C (MyBP-C) between binding to actin and myosin, which alters maximum calcium-activated force and calcium sensitivity. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

November 24, 2003The Journal of General PhysiologyOpen Access

Effect of MyBP-C Binding to Actin on Contractility in Heart Muscle

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Population

Heart muscle (skinned fibers)

Comparison

Addition of high concentration of C0C2 fragments… vs Extraction of MyBP-C

Design

Preclinical

Authors

IKIrina KulikovskayaCalifornia University of Pennsylvania GMGeorge McClellanUnited States Food and Drug Administration JFJeanne FlavignyUniversité Paris-Sud

Discussion

Member takes

Implication

May inform MyBP-C targeting in diastolic dysfunction; leaves open in vivo translation from animal models.

Structured PICO

Population

Heart muscle (skinned fibers)

Intervention

Addition of high concentration of C0C2 fragments to disrupt endogenous C0 interactions

Comparator

Extraction of MyBP-C

Outcome

Contractility (maximum Ca-activated force [Fmax] and Ca sensitivity)surrogate

Cardiac contractility may be regulated by shifting the binding of the NH2 terminus of MyBP-C between actin and myosin, which could impact diastolic filling.

Cite This Study

Kulikovskaya et al. (2003) studied this question.

synapsesocial.com/papers/6a1be653ea84844e355f261c https://doi.org/10.1085/jgp.200308941

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Effect of MyBP-C Binding to Actin on Contractility in Heart Muscle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Effect of MyBP-C Binding to Actin on Contractility in Heart Muscle

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider