Creatine Kinase BB Isoenzyme in CSF in Neurologic Diseases

Pfeiffer, Frederick E.; Homburger, Henry A.; Yanagihara, Takehiko

doi:10.1001/archneur.1983.04050030063012

Cited by 45 publications

(9 citation statements)

References 14 publications

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“…Inspection of the graphical¬ ly displayed profiles of serial CKB determinations among individual con¬ trol patients indicated relatively flat lines (Fig 1, bottom right). However, the CKB profiles of patients with acute cerebrovascular diseases were heterogeneous, with some having prominent peaks, fluctuations, or flat patterns ( well for the control patients (r = .84), for the patients with transient vascu¬ lar events (r = .82) and, to a lesser extent, for the patients with subaAccepted for publication Aug 13,1983. From the Departments of Neurology (Drs Pfeiffer and Yanagihara) and Laboratory Medicine (Dr Homburger), Mayo Clinic and Mayo Foundation, Rochester, Minn.…”

Section: Resultsmentioning

confidence: 99%

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Serum Creatine Kinase B Concentrations in Acute Cerebrovascular Diseases

Pfeiffer¹,

Homburger²,

Yanagihara³

1984

Archives of Neurology

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Section: Resultsmentioning

confidence: 99%

“…When individual mean CKB, SD, and CV were taken into consideration, 13 (76%) of 17 patients in the early group of ischemie stroke showed abnormalities. There was a tendency for patients with large infarctions to show higher CKB values.…”

Section: Serum Biochemical Markers Existmentioning

confidence: 99%

Serum Creatine Kinase B Concentrations in Acute Cerebrovascular Diseases

Pfeiffer¹,

Homburger²,

Yanagihara³

1984

Archives of Neurology

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“…For creatine kinase the importance of the MM isoenzyraes in muscular dystrophy and of the MB isoenzyme in acute myocardial infarction is well known. Increased BBCK CSF concentration was found in various other neurologic diseases, but the level does not appear elevated in the case of inactive, chronic or degenerative disease [6]. It is well known that BBCK sera concentration is increased in acute stroke [7], cardiac arrest [4][5][6][7][8][9][10][11][12][13] and head injury [3][4][5] and this increase suggests that clinical brain damage may cause release of brain tissue enzymes into the peripheral blood [2].…”

Section: Discussionmentioning

confidence: 96%

Creatine kinase BB activity in serum of patients with acute stroke: correlation with the severity of brain damage

et al. 1987

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BB-CK activity was measured in 11 patients with stroke and in 10 controls. Blood samples were taken 36 hours after the clinical stroke onset in every patient. Sera were stored at -80 degrees and analyzed within two months. The creatine kinase isoenzymatic pattern was determined by ion-exchange column separation and gradient elution system. The mean BB-CK concentration in patients with stroke was significantly higher than in controls (p less than 0.01). In the group of "stroke" patients we found a correlation between severity of brain damage, as suggested by the clinical picture and CT scans, and serum values of BB-CK.

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“…However, the anti-PGM antibody used did not differentiate between the type M-and the type B-PGM subunit (Egea et al, 1992). Type BB-CK has been found in both human neuronal and glial cells (Thompson et al, 1980;Pfeiffer et al, 1983;Yoshimine et al, 1983;Worley et al, 1985). ABBREVIATIONS BPGP, 2,3-bisphosphoglycerate phosphatase; CK, creatine kinase; PGM, phosphoglycerate mutase…”

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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Creatine Kinase BB Isoenzyme in CSF in Neurologic Diseases

Cited by 45 publications

References 14 publications

Serum Creatine Kinase B Concentrations in Acute Cerebrovascular Diseases

Serum Creatine Kinase B Concentrations in Acute Cerebrovascular Diseases

Creatine kinase BB activity in serum of patients with acute stroke: correlation with the severity of brain damage

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

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