ArticleMolecular biology reports2002
Modeling the energy transfer pathways. creatine kinase activities and heterogeneous distribution of ADP in the perfused heart.
Article in Molecular biology reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- A comprehensive review of the bioenergetics of fatty acid and glucose metabolism in the healthy and failing heart in nondiabetic condition.Heart failure reviews · 2017Review
- Mitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?Frontiers in physiology · 2013Article
- Creatine kinase overexpression improves ATP kinetics and contractile function in postischemic myocardium.American journal of physiology. Heart and circulatory physiology · 2012Article
- Energy metabolism in heart failure.The Journal of physiology · 2004Review
- Heterogeneity of ADP diffusion and regulation of respiration in cardiac cells.Biophysical journal · 2003Article
- On the origin of intracellular compartmentation and organized metabolic systems.Molecular and cellular biochemistryReview
- Structural and functional adaptations of striated muscles to CK deficiency.Molecular and cellular biochemistryReview
- CK flux or direct ATP transfer: versatility of energy transfer pathways evidenced by NMR in the perfused heart.Molecular and cellular biochemistryReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The exchange scheme of high energy phosphate transport in a whole heart relies on a system of CK functioning in different ways. This suggests that the CKs are able to act both like a shuttle and like a buffer for the energy transfer. The challenge is to understand how these two functions are balanced in the CK system. One key of this balance is the knowledge of the local concentrations of the ADP nucleotide. These concentrations cannot be directly measured, but they may be derived by computation. In the present report we introduce the known properties of the enzymes catalyzing the exchange of high energy phosphate into the model of flux pathways derived from NMR experiments to compute both the maximum activity of each enzyme and the local concentrations of all the substrates. We show that the ADP distribution must be heterogeneous for the system to work. Its concentration is 50% higher in the vicinity of ATPase sites and 50% lower in the intermembrane space of the mitochondria than in the cytosol. Another result of this analysis is that the apparent large unbalance of the CKmito pathway is imposed by the adenosine nucleotide transferase fluxes. This analysis proves that it is possible to deduce biochemistry the local concentrations of a substrate by combining data originating from NMR, and enzymology into a common model.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.