Serum creatine phosphokinase (CPK) isoenzymes after intramuscular injections, surgery, and myocardial infarction: Experimental and clinical studies

Klein, Milton S.; Shell, William E.; Sobel, Burton E.

doi:10.1093/cvr/7.3.412

Cited by 142 publications

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“…It can be seen that MB activity always is under 30% of total CPK activity, in accordance with data obtained with the electrophoresis technique (7)(8)(9). Human myocardial tissue contains about 30% MB isoenzyme (6) and this study thus shows that the necrotic tissue probably releases both MM and MB CPK at the same rate and to the same extent.…”

Section: Discussionsupporting

confidence: 89%

“…(6), the appearance of MB enzyme in the serum is useful for diagnosing myocardial damage. Normal human serum contains only the MM isoenzyme while the MB enzyme appears in serum from patients after an acute myocardial infarction (7)(8)(9). In the present study we have utilized known differences in the kinetic properties of the isoenzymes to detect the MB isoenzyme in serum from such patients with a new procedure not requiring electrophoresis.…”

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confidence: 99%

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Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase

Witteveen

Sobel

DeLuca

1974

Proc. Natl. Acad. Sci. U.S.A.

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Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB,show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the-isoenzyme pattern of the' serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively. (6), the appearance of MB enzyme in the serum is useful for diagnosing myocardial damage. Normal human serum contains only the MM isoenzyme while the MB enzyme appears in serum from patients after an acute myocardial infarction (7)(8)(9). In the present study we have utilized known differences in the kinetic properties of the isoenzymes to detect the MB isoenzyme in serum from such patients with a new procedure not requiring electrophoresis.The method conventionally used for the detection of CPK activity in sera is that of Rosalki (10) and is a coupled enzyme assay. However, this assay cannot be used at very low concentrations of substrates due to a lack of sensitivity. Since we wished to assay CPK at very low substrate concentrations where the difference in activity of the isoenzymes is most apparent, we developed a kinetic method in which the ATP produced is measured by the firefly light-emitting reaction. Thus the reaction CP + ADP = creatine + ATP is followed by coupling the ATP formed with the firefly luciferase reaction in which E ATP + luciferin + 02 --oxyluciferin + AMP + PPi + CO2 + h., where E is luciferase.Under selected conditions the light emission at any moment is proportional to the amount of ATP present at that instant.When CPK is present in the reaction medium, and its substrates, ADP and CP, are added, the rate of increase of emission of light is proportional to the rate of formation of ATP during a measured interval. By using the Rosalki method for CPK activity at high substrate concentrations and the luciferase-coupled assay at low substrate concentrations, it is possible to determine the amount of the three isoenzymes present in a sample. We have used this technique to study the changes in serum CPK isoenzymes in patients with acute myocardial infarction. The data indicate that this is a rapid and sensitive method for detecting the appearance of MB isoenzyme in serum. MATERIALS AND METHODSReagents. Total CPK activity was assayed according to Rosalki (10) using Calbiochem Statpacks. CP and ADP were purchased from Calbiochem. ADP was further purified by chromatography on a DEAE-Sephadex A-25 column to remove ATP contaminants. Luciferase was purified as described by Green and McElroy (11)

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Section: Discussionsupporting

confidence: 89%

mentioning

confidence: 99%

Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase

Witteveen

Sobel

DeLuca

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…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%

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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“…Intramuscular injections may cause serum CK activity to rise [38], but there is no rise in CK-MB activity [39]. Increases in CK are usually small, to twice the upper reference limit or less, unless irritant or hypertonic solutions are injected.…”

Section: Serum Ck After Acute Myocardial Infarctionmentioning

confidence: 99%

Creatine Kinase and the Diagnosis of Myocardial Infarction

Smith

1986

J. Clin. Biochem. Nutr.

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Serum creatine phosphokinase (CPK) isoenzymes after intramuscular injections, surgery, and myocardial infarction: Experimental and clinical studies

Cited by 142 publications

References 0 publications

Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase

Kinetic Properties of the Isoenzymes of Human Creatine Phosphokinase

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

Creatine Kinase and the Diagnosis of Myocardial Infarction

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