Mitochondrial creatine kinase (EC 2.7.3.2) in the brain

Wevers, Ron A.; Reutelingsperger, Chris; Dam, B. E. Van; Soons, J.B.J.

doi:10.1016/0009-8981(82)90333-3

Cited by 33 publications

(14 citation statements)

References 15 publications

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“…However, the absence of type MM-CK in the electrophoretograms of extracts of the temporal lobe and hippocampus indicates that the very high levels of MM-CK (about 35% of the total CK activity) found in these regions by Hamburg et al (1990) were probably overestimated as a result of post-mortem artefacts, as already suggested by others (Hemer et al, 1994). Our results showing the presence of Mt-CK in the various regions of adult human brain agree with the data from others on Mt-CK protein (Wevers et al, 1977(Wevers et al, , 1981Petronia et al, 1980;Chandler et al, 1984) and mRNA (Hass and Strauss, 1990;Payne and Strauss, 1994).…”

Section: Discussionsupporting

confidence: 92%

“…But, as Schon and co-workers (Shanske et al, 1987;Sakoda et al, 1988) have indicated, a lack of detection of M-PGM transcript does not exclude low transcription of M-PGM message in the brain. Most authors have reported that BB-CK is the only CK cytosolic isoenzyme present in human brain based upon electrophoretic (Deul and Van Breemen, 1964;Sjovall and Voigt, 1964;Dawson and Fine, 1967;Kumudavalli and Watts, 1968;Allard and Cabrol, 1970;Smith, 1972;Klein et al, 1973;Ogunro et al, 1977;Petronia et al, 1980;Urdal et al, 1983;Chandler et al, 1984;Chastain et al, 1988), chromatographic (Roberts et al, 1975;Tsung, 1976) and immunological techniques (Jockers-Wretou and Pfleiderer, 1975;Wevers et al, 1981;Chandler et al, 1984;Chastain et al, 1988). However, some authors have reported the presence of MM-CK.…”

Section: Discussionmentioning

confidence: 99%

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Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Durany

Joseph²,

Cruz-Sánchez³

et al. 1997

Br J Cancer

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Summary The distribution of phosphoglycerate mutase (EC 5.4.2.1, PGM), 2,3-bisphosphoglycerate phosphatase (EC 3.1.3.13, BPGP) and creatine kinase (EC 2.7.3.2, CK) activity and isoenzymes in various regions of adult human brain and in brain tumours (astrocytomas, anaplastic astrocytomas, glioblastomas and meningiomas) has been determined using electrophoresis. PGM and cytosolic CK exist in mammalian tissues as three isoenzymes that result from the homodimeric and heterodimeric combinations of two subunits [types M (muscle) and B (brain)] coded by separated genes. In addition, a dimeric from and an octameric form of mitochondrial CK exist in mammals. Type BB-PGM was the major PGM isoenzyme found in normal brain, although type MB-PGM and type MM-PGM were also detected. All brain tumours possessed lower PGM activity than normal brain, and meningiomas showed higher BPGP activity. In astrocytic tumours, the proportion of type MB-and type MM-PGM decreased, and in meningiomas these isoenzymes were not detected. Type BB-CK and mitochondrial CK were the only CK isoenzymes detected in normal brain. Astrocytomas possessed lower CK activity than anaplastic astrocytomas and glioblastomas and, in addition, tended to possess lower CK content than normal brain. No qualitative changes of the normal CK isoenzyme pattern were observed in the tumours.Keywords: 2,3-bisphosphoglycerate phosphatase; creatine kinase; phosphoglycerate mutase; activity and isoenzymes; human brain; brain tumour Most isoenzyme transitions that occur in neoplastic tissues represent a shift from a differentiated to an undifferentiated pattern. The transitions to a more differentiated pattern are much less frequent and involve a great alteration in the control of gene expression. Omenn and co-workers (Omenn and Cheung, 1974;Omenn and Hermodson, 1975) described in human brain tumours a transition in the phosphoglycerate mutase phenotype from the normal brain pattern to a more differentiated muscle-type pattern that correlated with the degree of malignancy of the tumours and that could constitute a good brain tumour marker. As the series of tumours studied by Omenn and Cheung (1974) and Omenn and Hermodson (1975) was small and the distribution of phosphoglycerate mutase isoenzymes in human brain was poorly known, the present study was undertaken. In addition to phosphoglycerate mutase, we have determined creatine kinase, which possesses isoenzymes with a tissue distribution similar to those of phosphoglycerate mutase.Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) is a glycolytic enzyme present in mammalian cells in substantial amounts that catalyses the interconversion of 3-phosphoglycerate and 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. In addition to the mutase activity, it possesses 2,3-bisphosphoglycerate phosphatase Fothergill-Gilmore and Watson, 1989). Creatine kinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2, CK) is an ubiquitous enzyme that functions in the transfer of energy from t...

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Durany

Joseph²,

Cruz-Sánchez³

et al. 1997

Br J Cancer

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“…In the KPB-extracts of schizophrenic brains, the activity of CK was significantly decreased and was equal to 83 ± 23 IU/g wet wt. Inasmuch as it is known that brain may contain different CK isoenzymes (Wevers et al, 1981), it was of interest to estimate the CK isoenzyme spectrum of the total KPBextracts. The results of quantitative electrophoresis of KPB-extracts of the brain in agarose gels are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Intracellular alterations of the creatine kinase isoforms in brains of schizophrenic patients

Klushnik

Spunde

Yakovlev

et al. 1991

Molecular and Chemical Neuropathology

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Postmortem brain tissues of schizophrenic patients were found to contain 5-10 times less water-soluble creatine kinase (BB CK) and 1.5-3 times less mitochondrial creatine kinase as compared to control. The major part of BB CK in schizophrenic brain tissues, contrary to control, was found to be insoluble in water (particulate form of BB CK) and could be extracted from brain tissue with strong denaturating agents. The particulate form of BB CK did not have any enzymatic activity but activity was found after the solubilization of this isoenzyme. The observed BB CK translocation into the particulate inactive form and the decrease of mitochondrial CK content to schizophrenic brains may reflect changes in the synthesis and the utilization of creatine phosphate.

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“…In the sixties, Jacobs et al [45] and Swanson [46] reported on CK activity associated with brain mitochondria, which was later identified and characterized as genuine brain Mi-CK [32, 47,48] representing the ubiquitous isoform Mia-CK [2,3,32]. Mia-CK, which was also char acterized extensively [2,3,6,32], was found to be local ized preferentially as octamers in m itochondrial bound ary mem brane contact site fractions o f brain m ito chondria [49], In addition, in several early studies the presence of muscle-type M-CK in brain was also postu lated [for review see 40].…”

Section: Energy Requirem Ents In the Brainmentioning

confidence: 99%

Functional Aspects of Creatine Kinase in Brain

Hemmer

Wallimann²

1993

Dev Neurosci

161

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The distinct isoenzyme-specific localization of creatine kinase (CK) isoenzymes found recently in brain suggests an important function for CK in brain energetics and points to adaptation of the CK system to the special energy requirements of different neuronal and glial cell types. For example, the presence of brain-type B-CK in Bergmann glial cells and astrocytes is very likely related to the energy requirements for ion homeostasis (K⁺-resorption) in the brain, as well as for metabolite and neurotransmitter trafficking between glial cells and neurons. In contrast, the presence of muscle-type M-CK, found exclusively in Purkinje neurons which also express other muscle-specific protein, is very likely related to the unique calcium metabolism of these neurons. In addition, the developmentally late appearance of mitochondrial CK (Mi-CK) during brain development indicates an important function for Mi-CK in the oxidative energy metabolism of the brain. The physiological importance of the phosphocreatine circuit fully operating in adult brain has been corroborated by recent data from in vivo ³¹P-NMR magnetization transfer measurements. Future investigations should concentrate on the possible involvement of CK in diseases of the CNS with altered energy metabolism, aspects of which are also discussed here.

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Mitochondrial creatine kinase (EC 2.7.3.2) in the brain

Cited by 33 publications

References 15 publications

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumours

Intracellular alterations of the creatine kinase isoforms in brains of schizophrenic patients

Functional Aspects of Creatine Kinase in Brain

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