Case report: changes in creatine kinase isoenzymes after myocardial infarction in a patient with prostatic carcinoma.

1980 ◽  
Vol 26 (5) ◽  
pp. 661-663
Author(s):  
R L Alexander

Abstract The detection of serum proteins that can serve as tumor markers has been reported with increased frequency in patients with various localized or metastatic cancers. Many of these reports have concerned patients with prostatic carcinoma, who had normal or increased concentrations of creatine kinase (EC 2.7.3.2) in serum. In many instances the creatine kinase BB isoenzyme was increased in these patients. I describe the case of a patient with carcinoma of the prostate (stage D), who had a myocardial infarction three to four days after admission. The serum activity of the MM, MB, and BB isoenzymes changed markedly after the infarction. These changes and the possible tissue source(s) of this isoenzyme are discussed in relationship to the clinical symptoms of the patient.

1980 ◽  
Vol 26 (5) ◽  
pp. 661-663 ◽  
Author(s):  
R L Alexander

Abstract The detection of serum proteins that can serve as tumor markers has been reported with increased frequency in patients with various localized or metastatic cancers. Many of these reports have concerned patients with prostatic carcinoma, who had normal or increased concentrations of creatine kinase (EC 2.7.3.2) in serum. In many instances the creatine kinase BB isoenzyme was increased in these patients. I describe the case of a patient with carcinoma of the prostate (stage D), who had a myocardial infarction three to four days after admission. The serum activity of the MM, MB, and BB isoenzymes changed markedly after the infarction. These changes and the possible tissue source(s) of this isoenzyme are discussed in relationship to the clinical symptoms of the patient.


1989 ◽  
Vol 75 (6) ◽  
pp. 537-541 ◽  
Author(s):  
Ante Roguljić ◽  
Tayfour Safwan ◽  
Viktor Šeparović

Creatine kinase (CK EC 2.7.3.2) and CK-BB activity was analyzed in 41 malignant tumors of 6 different sites and different histological structures. The same analyses were done on 150 sera of patients with malignant diseases of various localizations. The rate of CK activity was determined kinetical-ly, whereas tissue and serum CK-BB were separated chromatographically (Mercer). Insofar as malignant tumor tissues are concerned, the highest average rate of CK-BB activity was detected in tumors of the prostate (mean 1450 IU/g), and the lowest in tumors of the parotid gland (mean 5.2 IU/g). CK-BB was detected by the Mercer technique in 56 (37.3 %) of 150 analyzed sera of patients with malignant diseases. The rate of CK activity in sera of patients with malignant diseases was 8 to 74 IU/I. In comparison with the site of the malignant process no significant CK serum activity differences were observed. T2-T3 tumors did not significantly influence the activity of either CK or CK-BB in the case of either tissues or sera (T1-T3). Enzyme activity was found to be much higher - both in tumoral tissue and in sera - with T4 tumors. The highest rate of CK-BB activity was found in sera of patients with malignant tumors of the stomach (mean 8.1 IU/I), and the lowest in malignant tumors of the rectum (mean 1.8 IU/I).


1988 ◽  
Vol 34 (3) ◽  
pp. 489-492 ◽  
Author(s):  
S L Chastain ◽  
C H Ketchum ◽  
W E Grizzle

Abstract Creatine kinase (CK; EC 2.7.3.2) isoenzyme BB extracted from brains of rats reportedly undergoes modification at 37 degrees C, leaving an electrophoretic variant that accounts for most of the residual CK activity. This variant, called CK-BB', migrates on electrophoresis similarly to creatine kinase isoenzyme MB. Using electrophoresis and immunoinhibition with antiserum to creatine kinase isoenzyme MM, we found CK-BB to be the only identifiable cytoplasmic isoenzyme in surgical samples from human brain and intestine. In contrast, we found that some samples of brain obtained at autopsy contain CK-BB'. We also found that CK-BB extracted from human brain was converted to CK-BB' upon incubation in serum or plasma at 37 degrees C. We found a similar development of CK-BB' in incubation mixtures of serum or plasma containing CK-BB obtained from surgical samples of human intestine. The development of CK-BB' during infarction of the gastrointestinal system may thus be a source of false-positive CK-MB in the laboratory verification of myocardial infarction when electrophoresis is used as the only method to identify CK isoenzymes.


1985 ◽  
Vol 31 (7) ◽  
pp. 1189-1192 ◽  
Author(s):  
W Stein ◽  
J Bohner

Abstract We describe the influence of autoantibodies that bind creatine kinase BB (CK-BB) on the methods for MB isoenzyme. If these autoantibodies are present in patients' sera, they cause the formation of macro CK type 1 (immunoglobulin-linked CK-BB). In some of these cases they can bind not only endogenous CK-BB but also CK-MB without significantly affecting enzyme activity. Although these antibodies show distinctly less affinity for CK-MB than for CK-BB, they nevertheless bind CK-MB in these particular sera, because their concentration exceeds that of CK-BB isoenzyme. If a person with such autoantibodies has an acute myocardial infarction, the immunoinhibition method for CK-MB, which does not discriminate between CK-MB and CK-BB, will recognize the increase and peak of CK-MB with time, although persistent macro CK activity will be superimposed on the typical isoenzyme pattern. However, isoenzyme electrophoresis and recently introduced immunoenzymometric assays for CK-MB in these cases may be less sensitive for detecting myocardial infarctions, because the typical increase in CK-MB activity may be identified later in the progression of symptoms, or even be missed.


The Prostate ◽  
1981 ◽  
Vol 2 (1) ◽  
pp. 109-119 ◽  
Author(s):  
Lawrence M. Silverman ◽  
John F. Chapman ◽  
Marcie E. Jones ◽  
Gerald B. Dermer ◽  
Thaddeus Pullano ◽  
...  

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