Die Bedeutung von Kreatinphosphat und Adenosintriphosphat im Hinblick auf Energiebereitstellung, -transport und -verwertung im normalen und insuffizienten Herzmuskel

Nagle, Stanley C.

doi:10.1007/bf01484859

Cited by 23 publications

(6 citation statements)

References 67 publications

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“…These considerations are fully in keeping with models of the "functional compartmentation" of adenine nucleotides and of components of the creatine/phosphocreatine/CK system within the muscle cell (2,23,24,48,56,67). According to such models, the ADP produced in muscle contraction does not diffuse to the mitochondria to be converted to ATP.…”

Section: Same As W But At 35~mentioning

confidence: 91%

“…Creatine and phosphocreatine diffuse readily into and out of the intramyofibrillar space, whereas adenine nucleotides (which are in any case present in lesser amounts) do not (31,47,48). Assuming further that soluble CK does not penetrate freely into the intramyofibrillar space, the CK bound at the M-line would have a crucial function, since ADP produced by myosin-ATPase action could only be rephosphorylated by the CK located in the myofibrils.…”

Section: Same As W But At 35~mentioning

confidence: 99%

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Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Wallimann¹,

Turner²,

Eppenberger³

1977

The Journal of Cell Biology

185

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Purified, repeatedly washed, skeletal muscle myofibrils contain approx. 0.2 U of creatine kinase (CK) activity (equivalent to 2.5 micrograms CK) per milligram dry weight; this firmly bound CK activity is estimated to represent 3-5% of the total cellular CK. It had been shown previously that the myofibrillar CK, which can be quantitatively extracted at low ionic strength and purified to homogeneity, is very similar, if not identical, to the bulk MM-CK. It is shown that the two protein preparations also have the same peptide pattern after cyanogen bromide fractionation and very similar specific activities, confirming their identity. The earlier demonstration that the bound CK is specifically located at the M-lines of isolated myofibrils has been confirmed by immunofluorescence. Antibodies directed against purified MM- and BB-CK were used in the indirect fluorescent antibody technique to study the specificity of myofibril binding sites for different forms of CK. With myofibrils from adult muscle, which has only MM-CK, as well as from early developmental stages in which BB-CK is the predominant isoenzyme, M-type CK was localized exclusively at the M-line, while greater or lesser amounts of B-type CK were found at the Z-line. The data provide strong evidence that the MM-CK at the M-lines in skeletal myofibrils is not adventitiously bound but is rather an integral element in the M-line structure. The amount of CK bound is reasonably consistent with the earlier proposal that the CK molecules might be the transverse M-bridges and appears to be sufficient to regenerate all of the ATP hydrolyzed during muscle contraction.

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Section: Same As W But At 35~mentioning

confidence: 91%

Section: Same As W But At 35~mentioning

confidence: 99%

Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.

Wallimann¹,

Turner²,

Eppenberger³

1977

The Journal of Cell Biology

185

View full text Add to dashboard Cite

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“…In 1970 S. Nagle published two papers in the journal Klinische Wochenschrift, one of which had a title 'Die Bedeutung von Kreatinphosphat und Adenosintriphosphat im Hertzmuskel' [242,243]. In 1970 S. Nagle published two papers in the journal Klinische Wochenschrift, one of which had a title 'Die Bedeutung von Kreatinphosphat und Adenosintriphosphat im Hertzmuskel' [242,243].…”

Section: Metabolic Wave (Propagation Of Local Oscillations) In Structunclassified

“…In 1970 S. Nagle published two papers in the journal Klinische Wochenschrift, one of which had a title 'Die Bedeutung von Kreatinphosphat und Adenosintriphosphat im Hertzmuskel' [242,243]. In this way the shift of creatine kinase from equilibrium distributes, or propagates, from myofibrils to mitochondria in wave-like manner, 'somit pflanzt sich der Auslenkungeffekt gewissermassen wellenformig fort' [242], finally resulting in the local cyclic changes of ADP near mitochondria. He came to several interesting conclusions: ATP diffusion seems to be restricted in the cells and the main part on energy is transported in the cytoplasm via equilibrium creatine kinase reaction without direct physical diffusion of ATR but in the way of facilitated diffusion (high energy phosphoryl group transfer via enzymatic equilibrium creatine kinase reaction) and via the same reaction the feedback signal, a change of ADR goes back to mitochondria in the following way: in the contraction cycle ADP is released in myofibrillar space and this induces the cyclic shift in the creatine kinase reaction equilibrium in the next, adjacent point ('Raumelement') of cytoplasmic space, which leads to restoration of myofibrillar ATP but in this 'Raumelement' creatine is produced from phosphocreatine, that in turn will shift the equilibrium in the next point ('Raumelement').…”

Section: Metabolic Wave (Propagation Of Local Oscillations) In Structmentioning

confidence: 99%

“…What was unknown to Nagle in that time was the existence of coupled kinases. These dynamic cytoplasmic microcompartments of ATP may be representative of the 'Raumelements' of Nagle [242]. In myofibrils it is unidirectionally driven in the steady state by myosin ATPase in direction of phosphocreatine utilization, this is a kinetically favorable reaction and close spatial localization of these two proteins in the same cellular compartment makes their interaction very efficient (see the chapter by R. Ventura-Clapier and Veksler in this issue).…”

Section: Metabolic Wave (Propagation Of Local Oscillations) In Structmentioning

confidence: 99%

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Metabolic compartmentation and substrate channelling in muscle cells

Saks¹,

Khuchua²,

Vasilyeva³

et al. 1994

Mol Cell Biochem

216

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The published experimental data and existing concepts of cellular regulation of respiration are analyzed. Conventional, simplified considerations of regulatory mechanism by cytoplasmic ADP according to Michaelis-Menten kinetics or by derived parameters such as phosphate potential etc. do not explain relationships between oxygen consumption, workload and metabolic state of the cell. On the other hand, there are abundant data in literature showing microheterogeneity of cytoplasmic space in muscle cells, in particular with respect to ATP (and ADP) due to the structural organization of cell interior, existence of multienzyme complexes and structured water phase. Also very recent experimental data show that the intracellular diffusion of ADP is retarded in cardiomyocytes because of very low permeability of the mitochondrial outer membrane for adenine nucleotides in vivo. Most probably, permeability of the outer mitochondrial membrane porin channels is controlled in the cells in vivo by some intracellular factors which may be connected to cytoskeleton and lost during mitochondrial isolation. All these numerous data show convincingly that cellular metabolism cannot be understood if cell interior is considered as homogenous solution, and it is necessary to use the theories of organized metabolic systems and substrate-product channelling in multienzyme systems to understand metabolic regulation of respiration. One of these systems is the creatine kinase system, which channels high energy phosphates from mitochondria to sites of energy utilization. It is proposed that in muscle cells feed-back signal between contraction and mitochondrial respiration may be conducted by metabolic wave (propagation of oscillations of local concentration of ADP and creatine) through cytoplasmic equilibrium creatine and adenylate kinases and is amplified by coupled creatine kinase reaction in mitochondria. Mitochondrial creatine kinase has experimentally been shown to be a powerful amplifier of regulatory action of weak ADP fluxes due to its coupling to adenine nucleotide translocase. This phenomenon is also carefully analyzed.

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