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May 28, 1999Circulation ResearchOpen Access

Adenylate Kinase–Catalyzed Phosphotransfer in the Myocardium

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Why the study?

Does adenylate kinase-catalyzed phosphotransfer compensate for impaired intracellular energy flux in the failing heart?

Population

Isolated mitochondria/actomyosin system and intact myocardium (normal and pacing-induced failing heart models)

Comparison

Assessment of adenylate kinase-catalyzed… vs Normal hearts vs. pacing-induced failing hearts

Design

Preclinical

Authors

PDPetras P. DzejaKVKonradas VitkevičiusMRMargaret M. Redfield

Discussion

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Overview

May support adenylate kinase compensation in failing hearts; leaves open human relevance and therapeutic targeting.

Key Points

  • To determine the contribution of adenylate kinase–catalyzed phosphotransfer to myocardial bioenergetics under normal conditions and in heart failure.
  • Assessed actomyosin contraction and mitochondrial respiration in an isolated mitochondria/actomyosin model exposed to adenylate kinase substrates and inhibitors.
  • Quantified phosphotransfer rates and total ATP turnover in intact normal and pacing-induced failing myocardium using 18O-phosphoryl labeling paired with gas chromatography and mass spectrometry.
  • In intact normal myocardium, adenylate kinase–catalyzed phosphotransfer contributed 10% to total ATP turnover, whereas creatine kinase contributed 89%.
  • In pacing-induced failing hearts, adenylate kinase–catalyzed phosphotransfer increased by 134% to supply 21% of total ATP turnover, while creatine kinase contribution decreased to 40%.
  • Inhibition of adenylate kinase activity reduced both actomyosin contraction and mitochondrial respiration, confirming its role in linking energy production to contraction.

Structured PICO

Does adenylate kinase-catalyzed phosphotransfer compensate for impaired intracellular energy flux in the failing heart?

P
Population
Isolated mitochondria/actomyosin system and intact myocardium (normal and pacing-induced failing heart models)
I
Intervention
Assessment of adenylate kinase-catalyzed phosphotransfer
C
Comparator
Normal hearts vs. pacing-induced failing hearts
O
Outcome
Rate of adenylate kinase-catalyzed phosphotransfer and its contribution to total ATP turnoversurrogate

Adenylate kinase acts as a compensatory mechanism for intracellular energy flux in the failing heart, increasing its contribution to ATP turnover as creatine kinase activity declines.

Cite This Study

Dzeja et al. (1999) studied this question.

synapsesocial.com/papers/6a77917f576efb0ddaf7733bhttps://doi.org/10.1161/01.res.84.10.1137
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Kinetics and compartmentation of energy metabolism in intact skeletal muscle determined from 18O labeling of metabolite phosphoryls1991 · 44 citations
  2. 2Enalapril Treatment Increases Cardiac Performance and Energy Reserve Via the Creatine Kinase Reaction in Myocardium of Syrian Myopathic Hamsters With Advanced Heart Failure1995 · 97 citations
  3. 3Myocardial Phosphocreatine-to-ATP Ratio Is a Predictor of Mortality in Patients With Dilated Cardiomyopathy1997 · 751 citations
  4. 4Mitochondrial ATP-sensitive K<sup>+</sup>channels modulate cardiac mitochondrial function1998 · 301 citations
  5. 5Role of MgADP in the development of diastolic dysfunction in the intact beating rat heart.1997 · 104 citations