ArticleJournal of muscle research and cell motility1992
In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve.
Article in Journal of muscle research and cell motility, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 105 citations in OpenAlex.
- Decreased creatine kinase is linked to diastolic dysfunction in rats with right heart failure induced by pulmonary artery hypertension.Journal of molecular and cellular cardiology · 2015Article
- Molecular and subcellular-scale modeling of nucleotide diffusion in the cardiac myofilament lattice.Biophysical journal · 2013Article
- Muscle glycogen stores and fatigue.The Journal of physiology · 2013Review
- Analysis of molecular movement reveals latticelike obstructions to diffusion in heart muscle cells.Biophysical journal · 2012Article
- A three-dimensional simulation model of cardiomyocyte integrating excitation-contraction coupling and metabolism.Biophysical journal · 2011Article
- The creatine kinase system and pleiotropic effects of creatine.Amino acids · 2011Review
- Adenylate kinase and AMP signaling networks: metabolic monitoring, signal communication and body energy sensing.International journal of molecular sciences · 2009Review
- Developmental restructuring of the creatine kinase system integrates mitochondrial energetics with stem cell cardiogenesis.Annals of the New York Academy of Sciences · 2008Article
- Modeling of spatial metabolite distributions in the cardiac sarcomere.Biophysical journal · 2007Article
- Effects of ADP on action potential-induced force responses in mechanically skinned rat fast-twitch fibres.The Journal of physiology · 2004Article
- Reversible binding of glycolytic enzymes and size change in the actin-containing filaments of the frog skeletal muscle.Journal of muscle research and cell motility · 2001Article
- Adenylate kinase 1 gene deletion disrupts muscle energetic economy despite metabolic rearrangement.The EMBO journal · 2000Article
- Protein diffusion in living skeletal muscle fibers: dependence on protein size, fiber type, and contraction.Biophysical journal · 2000Article
- Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps.The Journal of cell biology · 2000Article
- Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ.Journal of muscle research and cell motility · 2000Article
- Reduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium.Molecular and cellular biochemistry · 1999Article
- Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes.Molecular and cellular biochemistry · 1998Article
- Cytoarchitectural and metabolic adaptations in muscles with mitochondrial and cytosolic creatine kinase deficiencies.Molecular and cellular biochemistry · 1998Article
- Arginine kinase expression and localization in growth cone migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Heterogeneous cellular expression of creatine kinase isoenzyme during normal rat heart development.Molecular and cellular biochemistry · 1998Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Creatine kinase isoenzymes (CK = ATP: creatine N-phosphoryl transferase, EC 2.7.3.2) were localized in situ in cryosections of intact sarcomeric muscle by immunocytochemical staining. Similar to cardiac muscle, spermatozoa and photoreceptor cells, mitochondrial-type CK (Mi-CK) localization in skeletal muscle was also restricted to mitochondria. Besides the well-documented localization of muscle-type (M-CK) at the M-line and at the sarcoplasmic reticulum, surprisingly, most of the sarcoplasmic M-CK was also highly compartmentalized and was mainly confined to the I-band. The localization of M-CK at the I-band coincided with that of adenylate kinase and aldolase. In intact muscle, the diffusion equilibrium decisively favours occupancy by all three enzymes of the I-band, with the acto-myosin overlap region of the A-band acting as a molecular sieve, excluding to a large extent all three enzymes from the acto-myosin overlap region. This indicates that in intact muscle, this region of the A-band may be less accessible in vivo to soluble, sarcoplasmic enzymes than thought before. If muscle were permeabilized by chemical skinning before fixation, I-band CK, as well as aldolase and adenylate kinase, were solubilized and disappeared from the myofibrils, but the fraction of M-CK which was specifically associated with the M-line remained bound to the myofibrils. Implications of these findings are discussed with respect to the functional coupling of I-band-CK with glycolysis, to the formation of large multienzyme complexes of glycolytic enzymes with CK and to the supply of energy for muscle contraction in general.
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