Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

Tsung, Swei H.

doi:10.1093/clinchem/22.2.173

Cited by 200 publications

(35 citation statements)

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“…It has been reported that M-CK constitutes 35 % of total CK activity in the postmortem human brain (Hamburg et al, 1990). However, human brain extracts obtained directly at surgery did not contain significant amounts of M-CK (Tsung, 1976), and other human brain extracts contained specific CK activities which were 30-fold higher than those reported from Hamburg and coworkers (Tsung, 1976;McBride and Rodgerson, 1984). Thus, it seems likely that the figure reported by Hamburg et al (1990) was overestimated due to postmortem artefacts.…”

Section: Isoenzyme-specific Localization Of Creatine Kinase Isoenzymementioning

confidence: 65%

Creatine Kinase Isoenzymes in Chicken Cerebellum: Specific Localization of Brain‐type Creatine Kinase in Bergmann Glial Cells and Muscle‐type Creatine Kinase in Purkinje Neurons

Hemmer

Zanolla

Furter‐Graves

et al. 1994

Eur J of Neuroscience

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Creatine kinase isoenzymes were localized in the chicken cerebellum by the use of isoenzyme-specific anti-chicken creatine kinase antibodies. Brain-type creatine kinase was found in high amounts in the molecular layer, particularly in Bergmann glial cells but also in other cells of the cerebellar cortex, e.g. in astrocytes and in the glomerular structures, as well as in cells of the deeper nuclei. A mitochondrial creatine kinase isoform was primarily localized to the glomerular structures in the granule cell layer and was also identified in Purkinje neurons. Surprisingly, a small amount of the muscle-type creatine kinase isoform was identified in cerebellar extracts by immunoprecipitation, immunoblotting and native enzyme electrophoresis, and was shown to be localized exclusively in Purkinje neurons. Cell type-specific expression of brain- and muscle-type creatine kinase in Bergmann glial cells and Purkinje neurons, respectively, may serve to adapt cellular ATP regeneration to the different energy requirements in these specialized cell types. The presence of brain-type creatine kinase in Bergmann glial cells and astrocytes is discussed within the context of the energy requirements for ion homeostasis (K+ resorption), as well as for metabolite and neurotransmitter trafficking. In addition, the presence of muscle-type creatine kinase in Purkinje neurons, which also express other muscle-specific proteins, is discussed with respect to the unique calcium metabolism of these neurons and their role in cerebellar motor learning.

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Section: Isoenzyme-specific Localization Of Creatine Kinase Isoenzymementioning

confidence: 65%

Creatine Kinase Isoenzymes in Chicken Cerebellum: Specific Localization of Brain‐type Creatine Kinase in Bergmann Glial Cells and Muscle‐type Creatine Kinase in Purkinje Neurons

Hemmer

Zanolla

Furter‐Graves

et al. 1994

Eur J of Neuroscience

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“…When corrections for the differences in working temperature are considered, the CK activities observed are, with one exception (Ogunro et al .. 1977), higher than any other reported in the literature (Tables I and III). Generally, neither sex nor age of the subjects are indicated in various papers dealing with this topic (Kleine, 1967;Lujf, 1973;Neumeier et al .• 1977;Ogunro et al .• 1977;Sobel et al .. 1977;Tsung, 1976). Unsatisfactory information is furnished as to the origin of the samples (e.g., "heart muscle") (lockers-Wretou and Pfleiderer, 1975;Lujf, 1973;Miyoshi et al .. 1975;Neumeier et al .. 1977;Ogunro et al .• 1977).…”

Section: Comparison With Data From Other Investigatorsmentioning

confidence: 99%

“…For instance, with regard to CK, activities of approximately 80-2,100 U/g wet weight have been reported. Other critical aspects concerning the published material are the use of samples obtained at variable times postmortem (Jockers-Wretou and Pfleiderer, 1975;Kleine, 1967;Miyoshi et al .• 1975), the application of various extraction and analysis procedures which may not be optimal (Jockers-Wretou and Pfleiderer, 1975;Kleine, 1967), as well as the small number of cases studied (Lujf, 1973;Tsung, 1976). Furthermore, in many papers the working temperature is not indicated, and in others it is variable (25, 30, or 37°C) (Table I).…”

Section: Introductionmentioning

confidence: 99%

Enzyme activities of human myocardium: Creatine kinase and hexose phosphate isomerase

Haralambie

1980

Clinical Cardiology

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Creatine kinase (CK) and hexose phosphate isomerase (PHI) activities were determined in 36 samples of human heart muscle obtained from patients during cardiovascular surgery. With one exception, CK activities were higher than any reported so far in the literature (papillary muscle, left ventricle: 2,521 +/- 776 IU/g wet weight at 37 degrees C). PHI Activities, the first time measured, are comparable to those in skeletal muscle (200-400 U/g, higher in papillary muscle than in the right auricle). The activities of both enzymes determined correlate significantly (all samples considered together: r = 0.773; p < 0.001). Results are discussed with respect to their possible clinical interest as well as their significance for myocardial metabolism.

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“…As for the BB isoenzyme, the brain contains large amounts. Other tissues also rich in the BB dimer are the prostate, lung, urinary bladder, uterus, thyroid, pancreas, stomach, intestine, and kidney [2].…”

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confidence: 99%

Creatine phosphokinase isoenzymes in human prostatic tissues: A comparison between benign hyperplasia and adenocarcinoma

et al. 1985

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The objective of this study was to determine the distribution of creatine phosphokinase (CPK) into its three isoenzymes, MM, MB, and BB, in human prostatic tissue, in patients with benign hyperplasia (BPH) and adenocarcinoma. Specimens were obtained from 23 patients with adenocarcinoma of the prostate and 25 patients with benign hyperplasia. We also had the opportunity to analyze the CPK content in two normal prostates, the first from a 16 1/2-year-old boy and the second from a 9 1/2-year-old child. Our results showed prostate tissue to contain almost exclusively the BB isoenzyme with traces of the MB and MM dimers in both cancer and BPH as well as the specimen of normal prostate from the 16 1/2-year-old boy. As for the 9 1/2-year-old child, we found the following distribution: 39% MM, 21% MB, and 40% BB dimer. A comparison of the CPK-BB content in benign hyperplasia and adenocarcinoma revealed no significant difference between the two groups. Furthermore, we tried to correlate prostatic tissue CPK-BB levels with another possible tumor marker of the prostate, prostatic acid phosphatase (PAP) measured in the cytosol. No correlation was found between these two markers. We also studied the relationship of CPK-BB and PAP content in prostatic tissue to nuclear and cytosolic androgen receptor content in human prostatic tissue. We found some correlation between CPK-BB and androgen cytosolic receptors as well as between PAP content and androgen cytosolic receptors in patients with benign hyperplasia. No such correlation was found in the group with adenocarcinoma. In conclusion, this study does not show that the measurement of CPK-BB in the prostatic tissue could be used as an index of tissue malignancy.

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Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

Cited by 200 publications

References 1 publication

Creatine Kinase Isoenzymes in Chicken Cerebellum: Specific Localization of Brain‐type Creatine Kinase in Bergmann Glial Cells and Muscle‐type Creatine Kinase in Purkinje Neurons

Creatine Kinase Isoenzymes in Chicken Cerebellum: Specific Localization of Brain‐type Creatine Kinase in Bergmann Glial Cells and Muscle‐type Creatine Kinase in Purkinje Neurons

Enzyme activities of human myocardium: Creatine kinase and hexose phosphate isomerase

Creatine phosphokinase isoenzymes in human prostatic tissues: A comparison between benign hyperplasia and adenocarcinoma

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