What question did this study set out to answer?

To characterize the subcellular compartmentation, structure, and physiological function of creatine kinase isoenzymes and describe the integrated phosphocreatine circuit model for cellular energy homeostasis.

January 1, 1992Biochemical JournalOpen Access

Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis

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Key result

Creatine kinase isoenzymes and the phosphocreatine circuit regulate cellular energy homeostasis in tissues with high and fluctuating energy demands.

Design

Review

Authors

TWTheo WallimannETH Zurich MWMarkus WyssFirmenich (Switzerland)DBDieter BrdiczkaSanford Burnham Prebys Medical Discovery Institute

Discussion

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Implication

Hypothesis-generating for cardiac bioenergetics; leaves open whether phosphocreatine circuit modulation improves outcomes.

Key Points

To characterize the subcellular compartmentation, structure, and physiological function of creatine kinase isoenzymes and describe the integrated phosphocreatine circuit model for cellular energy homeostasis.
Synthesized biochemical, structural, and physiological findings on the subcellular localization of cytosolic (M-CK, B-CK) and mitochondrial (Mi-CK) creatine kinase isoenzymes.
Evaluated functional coupling of creatine kinase to ATP-generating pathways (glycolysis, oxidative phosphorylation) and ATP-consuming processes across different muscle fiber types.
In muscle, 5-10 % of 'cytosolic' CK is specifically localized at the myofibrillar M-band and functionally coupled to actin-activated Mg2+-ATPase, sufficient to regenerate ATP hydrolyzed during contraction.
Soluble MM-CK and glycolytic complexes specifically co-localize at the I-band, where ATP from glycolysis is rapidly transphosphorylated into phosphocreatine to replenish cellular pools.
Creatine kinase anchors to the sarcoplasmic reticulum and sarcolemma membranes, functionally coupling to ATP-dependent Ca2+-pumps and Na+/K+-pumps to regulate local ATP/ADP ratios during excitation-contraction coupling.

Cite This Study

Wallimann et al. (1992) studied this question. Creatine kinase isoenzymes and the phosphocreatine circuit regulate cellular energy homeostasis in tissues with high and fluctuating energy demands.

synapsesocial.com/papers/6a07fddc7ad161a3abfe10e0 https://doi.org/10.1042/bj2810021

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January 1, 1992Biochemical JournalOpen Access

Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis

View Full Paper

Ask AI

Bookmark

Key result

Creatine kinase isoenzymes and the phosphocreatine circuit regulate cellular energy homeostasis in tissues with high and fluctuating energy demands.

Design

Review

Authors

TWTheo WallimannETH Zurich MWMarkus WyssFirmenich (Switzerland)DBDieter BrdiczkaSanford Burnham Prebys Medical Discovery Institute

Discussion

Member takes

Implication

Hypothesis-generating for cardiac bioenergetics; leaves open whether phosphocreatine circuit modulation improves outcomes.

Key Points

To characterize the subcellular compartmentation, structure, and physiological function of creatine kinase isoenzymes and describe the integrated phosphocreatine circuit model for cellular energy homeostasis.
Synthesized biochemical, structural, and physiological findings on the subcellular localization of cytosolic (M-CK, B-CK) and mitochondrial (Mi-CK) creatine kinase isoenzymes.
Evaluated functional coupling of creatine kinase to ATP-generating pathways (glycolysis, oxidative phosphorylation) and ATP-consuming processes across different muscle fiber types.
In muscle, 5-10 % of 'cytosolic' CK is specifically localized at the myofibrillar M-band and functionally coupled to actin-activated Mg2+-ATPase, sufficient to regenerate ATP hydrolyzed during contraction.
Soluble MM-CK and glycolytic complexes specifically co-localize at the I-band, where ATP from glycolysis is rapidly transphosphorylated into phosphocreatine to replenish cellular pools.
Creatine kinase anchors to the sarcoplasmic reticulum and sarcolemma membranes, functionally coupling to ATP-dependent Ca2+-pumps and Na+/K+-pumps to regulate local ATP/ADP ratios during excitation-contraction coupling.

Cite This Study

Wallimann et al. (1992) studied this question. Creatine kinase isoenzymes and the phosphocreatine circuit regulate cellular energy homeostasis in tissues with high and fluctuating energy demands.

synapsesocial.com/papers/6a07fddc7ad161a3abfe10e0 https://doi.org/10.1042/bj2810021

View Full Paper

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Bookmark