Properties of creatine kinase-BB from canine and human brain tissues

Miller, J.H.; Wei, Robert

doi:10.1016/s0009-9120(85)80017-5

Cited by 6 publications

(3 citation statements)

References 31 publications

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“…We observed that about 90% of BB CK is extracted (detached from membrane) from normal brain under similar conditions. Such an easiness of BB CK extraction with low molarity saline buffers was also reported by other authors (Chandler, 1987;Miller and Wei, 1985).…”

Section: Discussionsupporting

confidence: 82%

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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Section: Discussionsupporting

confidence: 82%

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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“…However, some authors have reported the presence of MM-CK. Some of the reports (Murone and Ogotam, 1973;Mercer, 1974;Nealon and Henderson, 1975;Goulle et al, 1979;Miller and Wei, 1985) should be judged with caution, as separation methods that did not differentiate between MM-CK and Mt-CK were used, and non-inhibited adenylate kinase could interfere (Klein and Jeunelot, 1978;Lyndsey and Diamond, 1978;Desjardins, 1982;Urdal et al, 1983). But type MM-CK has also been detected in human brain using immunological techniques (Lyndsey and Diamond, 1978;Heinbokel et al, 1982), and it has been isolated from human temporal lobe and hippocampus (Hamburg et al, 1990); moreover, M-CK message has been detected by these authors.…”

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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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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“…Partial Purification of Cytosolic CK Isoenzymes Cytosolic CK isoenzymes, CK MM and CK MB, were partially purified from human heart and human skeletal muscle using modifications of the procedures of Blum et al [9], Roberts and Grace [3] and Miller and Wei [12]. Briefly, the CK isoenzymes were iso lated from human heart and skeletal muscle obtained at autopsy within 8 h of death.…”

Section: Methodsmentioning

confidence: 99%

Kinetic Characterization of Human Heart and Skeletal Muscle CK Isoenzymes

Schneider

Ga²,

Apple³

1988

Enzyme

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The purpose of this study was to investigate the kinetic properties of human creatine kinase (CK) isoenzymes partially purified from heart and skeletal muscle. Utilizing the backward CK-catalyzed reaction of creatine phosphate + ADP ^ creatine + ATP, K values for heart and skeletal muscle CK MM (3.7 mmol/1) were significantly (p < 0.05) greater than CK MB (2.1 mmol/1) which were significantly (p < 0.05) greater than mitochondrial CK (1.8 mmol/1) at variable creatine phosphate and fixed ADP concentrations. However, K(m) values for similar isoenzymes from the two different tissues, i.e., CK MB from heart vs. skeletal muscle, were not different. These results show that kinetic analysis of CK isoenzymes cannot differentiate the tissue source of elevated blood CK isoenzymes after the acute stress of long distance running or after acute myocardial infarction.

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Properties of creatine kinase-BB from canine and human brain tissues

Cited by 6 publications

References 31 publications

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

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

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

Kinetic Characterization of Human Heart and Skeletal Muscle CK Isoenzymes

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