Location and properties of two isoenzymes of cardiac adenylate kinase

Walker, E J; Dow, Jocelyn W.

doi:10.1042/bj2030361

Cited by 31 publications

(21 citation statements)

References 32 publications

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“…The extent of mitochondrial AK activity depends very much on the method of preparation, the tissue, and the species. It could be varied from as high as 40% in intact crude mitochondrial preparation obtained from hypo-osmatic bovine cardiac homogenates down to 0.3 % of the total activity in bovine aorta smooth muscle cells [19]. It is usually found to be around 10% and the rest accounted as cytosolic isoenzyme.…”

Section: Muscle Adenylate Kinasementioning

confidence: 98%

“…Part of the cytosolic AK is bound to myofibrils and is called myofibrillar AK [17][18][19]. The mitochondrial AK is located between the mitochondrial membranes with fatty acid-CoA ligase [14,19]. The extent of mitochondrial AK activity depends very much on the method of preparation, the tissue, and the species.…”

Section: Muscle Adenylate Kinasementioning

confidence: 99%

“…The cytosolic AK (AK1) is polymorphic in man (AKI*I and AKI*2) and AKI*I accounts for 95 % of the AK1 isoenzyme [16]. Part of the cytosolic AK is bound to myofibrils and is called myofibrillar AK [17][18][19]. The mitochondrial AK is located between the mitochondrial membranes with fatty acid-CoA ligase [14,19].…”

Section: Muscle Adenylate Kinasementioning

confidence: 99%

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Interaction of creatine kinase and adenylate kinase systems in muscle cells

Savabi

1994

Mol Cell Biochem

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Elsewhere in this book the important role of creatine kinase and its metabolites in high energy phosphate metabolism and transport in muscle cells has been reviewed. The emphasis of this review article is mainly on the compartmentalized catalytic activity of adenylate kinase in relation to creatine kinase isoenzymes, and other enzymes of energy production and utilization processes in muscle cells. At present the role of adenylate kinase is considered simply to equilibrate the stores of adenine nucleotides. Recent studies by us and others, however, suggest an entirely new view of the metabolic importance of adenylate kinase in muscle function. This view offers a closer interaction between adenylate kinase and creatine kinase, in the process of energy production (at mitochondrial and glycolytic sites), and energy utilization (at myofibrillar sites and perhaps other sites such as sarcoplasmic reticular, sarcolemmal membrane, etc.), thus being an integral part of the high energy phosphate transport system. This review article opens up the opportunity to further examine the metabolism of adenine nucleotides and their fluxes through the adenylate kinase system in intact muscle cells. Using an intact system, having a preserved integrity of their compartmentalized enzymes and substrates, is essential in clarifying the exact role of adenylate kinase in high energy phosphate metabolism in muscle cells.

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Section: Muscle Adenylate Kinasementioning

confidence: 98%

Section: Muscle Adenylate Kinasementioning

confidence: 99%

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Interaction of creatine kinase and adenylate kinase systems in muscle cells

Savabi

1994

Mol Cell Biochem

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“…It has been shown that the mitochondrial adenylate kinase (AK2 isoform) in heart muscle has the highest affinity (lowest K m ) for AMP (≤10 μM) amongst AMP metabolizing enzymes. 7,18 In addition, in the mitochondria-like kinetoplast organelle, the K m for AMP (AK2) is 74 μM.…”

Section: Discussionmentioning

confidence: 99%

AMP promotes oxygen consumption and ATP synthesis in heart mitochondria through the adenylate kinase reaction: an NMR spectroscopy and polarography study

Doliba

Babsky

Doliba

et al. 2015

Cell Biochemistry & Function

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Adenylate kinase plays an important role in cellular energy homeostasis by catalysing the interconversion of adenine nucleotides. The goal of present study was to evaluate the contribution of the adenylate kinase reaction to oxidative ATP synthesis by direct measurements of ATP using (31) P NMR spectroscopy. Results show that AMP can stimulate ATP synthesis in the presence or absence of ADP. In particular, addition of 1 mM AMP to the 0.6 mM ADP superfusion system of isolated superfused mitochondria (contained and maintained in agarose beads) led to a 25% increase in ATP synthesis as measured by the increase in βATP signal. More importantly, we show that AMP can support ATP synthesis in the absence of ADP, demonstrated as follows. Superfusion of mitochondria without ADP led to the disappearance of ATP γ, α and β signals and the increase of Pi . Addition of AMP to the medium restored the production of ATP, as demonstrated by the reappearance of γ, α and β ATP signals, in conjunction with a decrease in Pi , which is being used for ATP synthesis. Polarographic studies showed Mg(2+) dependence of this process, confirming the specificity of the adenylate kinase reaction. Furthermore, data obtained from this study demonstrate, for the first time, that different aspects of the adenylate kinase reaction can be evaluated with (31) P NMR spectroscopy. SIGNIFICANCE OF RESEARCH PARAGRAPH: The data generated in the present study indicate that (31) P NMR spectroscopy can effectively be used to study the adenylate kinase reaction under a variety of conditions. This is important because understanding of adenylate kinase function and/or malfunction is essential to understanding its role in health and disease. The data obtained with (31) P NMR were confirmed by polarographic studies, which further strengthens the robustness of the NMR findings. In summary, (31) P NMR spectroscopy provides a sensitive tool to study adenylate kinase activity in different physiological and pathophysiological conditions, including but not exclusive of, cancer, ischemic injury, hemolytic anemia and neurological problems such as sensorineural deafness.

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“…An apparent Mr could be estimated as 23.5 kilodaltons. This Mr of monomer en zyme differed slightly from the other enzyme in bovine heart muscle (21,500), rabbit skel etal muscle (cytosolic, 21,000), and bovine heart mitochondria (31,500) [31,32], Fur ther genetic studies may be necessary for the structural analyses. As before, in the case of the rabbit-and calf-muscle enzymes [30], the steady-state kinetics of the aortic smooth muscle AK, at pH 7.4 (25 °C) and essentially fixed (172) at 0.16-0.18 seem to be adequately expressed by a random quasi-equilibrium type of mechanism with a rate-limiting step largely at the interconversion of the ternary com plexes.…”

Section: Partial Purification Of Ak Isoform From Bovine Aorta Smooth mentioning

confidence: 99%

Multiforms of Mammalian Adenylate Kinase and Its Monoclonal Antibody against AK(1)

Kurokawa

Takenaka²,

Sumida³

et al. 1990

Enzyme

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An attempt has been made to determine the intracellular distribution of the multiforms of the adenylate kinase (AK) isoenzymes in mammalian tissues, to shed some light on their physiological roles, especially in energy metabolism. The adenylate kinase zymograms obtained from isoelectric focusing yielded two typical isoform patterns; (1) with a pi ≥ 9 and 8.6, specific for bovine skeletal muscle, heart, aorta and brain, and (2) with a pi = 7.9 and 7.1, specific for liver and kidney. Pattern (1) was attributed to the cytosolic isoenzyme (AKi) as demonstrated by immunostaining with anti-AK(1). Pattern (2) was attributed to the mitochondrial isoenzyme (AK(2)). These results were largely confirmed by chromatofocusing experiments. The AKi isoenzyme was partially purified from the cytosol fraction of bovine aortic smooth muscle and had an apparent M(r) of 23.5 kilodaltons. Its kinetic features are discussed from a comparative standpoint. Finally, the human serum AK(1) isoform was also detected by Western blotting with a monoclonal antibody directed against crystalline porcine muscle AK(1). These results are to form the basis of further studies on the ‘aberrant’ adenylate kinase isoenzyme from the serum of Duchenne muscular dystrophies.

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Location and properties of two isoenzymes of cardiac adenylate kinase

Cited by 31 publications

References 32 publications

Interaction of creatine kinase and adenylate kinase systems in muscle cells

Interaction of creatine kinase and adenylate kinase systems in muscle cells

AMP promotes oxygen consumption and ATP synthesis in heart mitochondria through the adenylate kinase reaction: an NMR spectroscopy and polarography study

Multiforms of Mammalian Adenylate Kinase and Its Monoclonal Antibody against AK(1)

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