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November 15, 1977Biochemical JournalOpen Access

Phosphorylation of the inhibitory subunit of troponin in perfused hearts of mice deficient in phosphorylase kinase. Evidence for the phosphorylation of troponin by adenosine 3′:5′-phosphate-dependent protein kinase in vivo

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Population

Perfused hearts from control and phosphorylase kinase-deficient (I strain) mice

Comparison

Perfusion with 0.1 micrometer-DL-isoprenaline vs Control mice hearts

Design

Preclinical

Authors

PEP. EnglandRutgers, The State University of New Jersey

Discussion

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Implication

Supports PKA-mediated troponin I phosphorylation in beta-adrenergic inotropy; extends biochemical data but leaves open human translation.

Structured PICO

P
Population
Perfused hearts from control and phosphorylase kinase-deficient (I strain) mice
I
Intervention
Perfusion with 0.1 micrometer-DL-isoprenaline
C
Comparator
Control mice hearts
O
Outcome
Troponin I phosphorylation and phosphorylase a levelssurrogate

This study provides in vivo evidence that troponin I is phosphorylated by cyclic AMP-dependent protein kinase rather than phosphorylase kinase during beta-adrenergic stimulation.

Cite This Study

P. England (1977) studied this question.

synapsesocial.com/papers/6a87bd050d75ae11a0ad2702https://doi.org/10.1042/bj1680307
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Phosphorylation of troponin and the effects of interactions between the components of the complex1974 · 230 citations
  2. 2The phosphorylation sites of troponin T from white skeletal muscle and the effects of interaction with troponin C on their phosphorylation by phosphorylase kinase1977 · 67 citations
  3. 3Phosphorylation of the Inhibitor Component of Troponin by Phosphorylase Kinase1972 · 125 citations
  4. 4On the question of translocation of heart cAMP-dependent protein kinase.1975 · 108 citations