Creatine kinase in serum

Szasz, G., Gruber, W., and Bernt, E., Creatine kinase in serum. I. Determination of optimum reaction conditions, Clin. Chem. 22, 650-656, 1976 Holdiness, M.R., Clinical pharmacokinetics of W-acetylcysteine, Clin. Pharmacokinet. 20, 123-134, 1991 Kelley, G.S., Clinical applications of W-acetylcysteine, Altem. Med. Rev. 3, 114-127, 1998 Schumann, G., Bonora, R., Ceriotti, F. et ah, IFCC primary reference procedures for the measurement of catalytic activity concentrations of enzymes at 37°C. Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase, Clin. Chem. Lab. Med. 40, 635-642, 2002 Zafarullah, M., Li, W.Q., Sylvester, J., and Ahmad, M., Molecular mechanisms of A -acetylcysteine actions. Cell. Mol. Life Sci. 60, 6-20, 2003 Marzullo, L., An update of A-acetylcysteine treatment for acute aminoacetophen toxicity in children, Curr. Opin. Pediatr. 17, 239-245, 2005 Aitio, M.L., A-acetylcysteine — passepartout or much ado about nothing Br. J. Clin. Pharmacol. 61, 5-15, 2006. 

E620 Hadberg, A., Hassager, C., Hildebrandt, P. and Christiansen, C. (1990). Comparison of two immunoinhibitory methods with agarose gel-electrophoresis for measuring the MB isoenzyme of creatine kinase in serum from cases of suspected myocardial infarction. J. Clin. Chem. Clin. Biochem. 28, 453-458. 

C19. Coolen, R. B., Herbstman, R., and Hermann, P., Spurious brain creatine kinase in serum from patients with renal disease. Clin. Chem. (Winston-Salem, N.C.) 24, 1636-1638 (1978). 

J. A. Lott, Creatine Kinase in Serum, in Selected Methods for the Small Clinical Chemistry Laboratory (eds. W. R. Faulkner and S. Meites), American Association for Clinical Chemistry, Washington, D.C., 1982, pp. 185-190. 

Szasz, G., W. Gerhardt, and W. Gruber (1978). Creatine kinase in serum 5. Effect of thiols on isoenzyme activity during storage at various temperatures. Clin Chem 24(9) 1557-1563. 

Adverse reactions occurring in patients may include abdominal pain, asthenia, diarrhea, dyspepsia, flatulence, headache, nausea. Laboratory abnormalities may include the following hematuria, increased ALT or AST, increased amylase, increased creatine kinase, increased serum creatinine greater than or equal to 0.3 mg/dL from baseline 4%. 

The patient, a 63-year-old Caucasian female, was hospitalized on 4 April 2002 though 10 April 2002 for a non-ST segment elevation myocardial infarction (non-Q-wave MI per chart documentation). She had a negative adenosine stress test after the initial event. Her serum cardiac-specific troponin I (cTnl) concentration 24 hours after her onset of chest pain was 1.4 pg/L (upper limit of normal is 0.3 ng/mL), and her creatine kinase (CK) MB level was 12.5 pg/L (upper limit of normal 6.0 ng/mL). Three days post-event her cTnl level was 0.5 pg/L and her CK-MB level was 4.5 pg/L (Fig. 5-1). MB refers to one of the isoenzyme forms of CK found in serum. The form of the enzyme that occurs in brain (BB) does not usually get past the blood-brain barrier and therefore is not normally present in the serum. The MM and MB forms account for almost all of the CK in serum. Skeletal muscle contains mainly MM, with less than 2% of its CK in the MB form. MM is also the predominant myocardial creatine kinase and MB accounts for 10%-20% of creatine kinase in heart muscle. 

It was soon noted, however, that serum creatine kinase as well as aldolase may be elevated in carriers (S12, S33), that here creatine kinase is far more sensitive, and that by its assay not only might the carrier state be confirmed in almost every female known to harbor the gene (Al, H8), but the expected proportion of mutant cases could be found by a family absence of both clinical and biochemical evidence of heredity (R12). These results have been confirmed for creatine kinase in a very large series of relatives of Duchenne-type dystrophic patients (R4), although... 

K6. Kemey, L. P., and Pennington, R. J., Changes in serum creatine kinase in myocardial infarction, Proc. Assoc. Clin. Biochem. 2, 62 (1962). 

There were no differences in the activities of serum transaminases, lactate dehydrogenase, or creatine kinase in patients with myocardial infarction who received an 18-hour infusion of urokinase compared with patients who received glucose alone (38), but subacute alterations of liver function tests have been described with streptokinase and anistreplase (39). Unexplained increases in transaminase activities have been reported in almost 25% of patients treated with streptokinase (40). In view of the greater prominence of liver dysfunction with streptokinase than with alteplase it could be wiser to choose alteplase rather than streptokinase in patients with previous impaired hepatic function (41). 

RN13 Ng, R.H., Sparks, K.M. and Statland, B.E. (1991). Measurement of creatine kinase in plasma, serum, and whole blood with the Reflotron system. Clin. Chem. 37, 917, Abstr. 38. 

The selection of which enzyme to measure in serum for diagnostic or prognostic purposes depends on a number of factors. An important factor is the distribution of enzymes among the various tissues, shown, for example, for aspartate aminotransferase, alanine aminotransferase, and creatine kinase in Figure 8-14. The main enzymes of established clinical value, together with their tissues of origin and their major clinical applications, are listed in Table 8-3 (see also Chapter 21). 

Bll. Brody, I. A., and Hatcher, M. A., Origin of increased serum creatine kinase in tetanus. Arch. Neurol. 16, 89-93 (1967). 

The diagnosis of organ disease is aided by measurement of a number of enzymes characteristic of that tissue or organ. Most tissues have characteristic enzyme patterns (Table 8-2) that may be reflected in the relative serum concentrations of the respective enzymes in disease. The diseased tissue can be further identified by determination of the isoenzyme pattern of one of these enzymes (e.g., lactate dehydrogenase, creatine kinase) in the serum, since many tissues have characteristic isoenzyme distribution patterns for a given enzyme. For example, creatine kinase (CK) is a dimer composed of two subunits, M (for muscle) and B (for brain), that occur in three isoenzyme forms, BB(CKi), MB(CK2) and MM(CK3), which catalyze the reversible phosphorylation of creatine with adenosine triphosphate (ATP) as the phosphate donor ... 

D. Hendriks, J. Soons, S. Scharp6, R. Wevers, M. van Sande, and B. Holmquist. Identification of the carboxypeptidase responsible for the post-synthetic modification of creatine kinase in human serum. Clin. Chim. Acta 772 253-260 (1988). 

Shibata, S., and B. Kobayashi. 1978. Blood platelets as a possible source of creatine kinase in rat plasma and serum. Thrombosis and Hemostasis (Stuttgart) 39 701-706. 

Chronic, heavy, daily alcohol consumption is associated with decreased muscle strength, even when adjusted for other factors such as age, nicotine use, and chronic illness. Heavy doses of alcohol also can cause irreversible damage to muscle, reflected by a marked increase in the activity of creatine kinase in plasma. Muscle biopsies from heavy drinkers also reveal decreased glycogen stores and reduced pyruvate kinase activity. Approximately 50% of chronic heavy drinkers have evidence of type 11 fiber atrophy. These changes correlate with reductions in muscle protein synthesis and serum camosinase activities. Most patients with chronic alcoholism show electromyographical changes, and many show evidence of a skeletal myopathy similar to alcoholic cardiomyopathy. 

A further practical consideration in the application of serum creatine kinase measurements is the possible effect of physical exercise upon the levels of this enzyme. Exercise of sufficient intensity and duration can substantially increase serum creatine kinase in normal individuals, and it is particularly important that this should be avoided in suspected carriers before testing (since the expected elevations may be small). 

In vivo, patients treated with AZT develop a mitochondrial myopathy with mitochondrial DNA depletion, deficiency of cytochrome c oxidase (complex IV), intracellular fat accumulation, high lactate production and marked phosphocreatine depletion (Lewis and Dalakas 1995 Dalakas 2001). Clinically, the patient presents with fatigue, myalgia, muscle weakness, wasting and elevated serum creatine kinase. Muscle biopsy shows ragged red fibers , the characteristic histopathologic changes of mitochondrial myopathy, cansed by subsarcolemmal accumulation of mitochondria (Lewis and Dalakas 1995). 

A 33-year-old female patient treated with haloperidol for a history of schizophrenia is seen in the ED because of complaints of fever, stiffness, and tremor. Her temperature is 104°F, and her serum creatine kinase (CK) level is elevated. What has occurred ... 

Constipation occurs in fewer than 10% of patients taking statins. Other adverse effects include elevated serum aminotransferase levels (primarily alanine aminotransferase), elevated creatine kinase levels, myopathy, and rarely rhabdomyolysis. 

Swanson, J. R., and Wilkinson, J. H., Measurement of creatine kinase activity in serum. Stand. Methods Clin. Chem. 7, 33-42 (1972). 

T6. Tummistor, T., and Airaksinen, M. N., Increase of creatine kinase activity in serum caused by intermittently administered suxamethonium. Brit. J. Anaesth. 38, 510 (1966). 

Myopathy and neuropathy Colchicine myoneuropathy appears to be a common cause of weakness in patients on standard therapy who have elevated plasma levels caused by altered renal function. It is often unrecognized and misdiagnosed as polymyositis or uremic neuropathy. Proximal weakness and elevated serum creatine kinase are generally present, and resolve in 3 to 4 weeks following drug withdrawal. Maiabsorption of vitamin B-f2- Colchicine induces reversible malabsorption of vitamin B-12, apparently by altering the function of ileal mucosa. 

The most common adverse effects of lamivudine seen at doses used to treat HBV are mild they include headache, malaise, fatigue, fever, insomnia, diarrhea, and upper respiratory infections. Elevated alanine aminotransferase (ALT), serum lipase, and creatine kinase may also occur. The safety and efficacy of lamivudine in patients with decompensated liver disease have not been established. Dosage adjustment is required in individuals with renal impairment. Coadministration of trimethoprim-sulfamethoxazole decreases the renal clearance of lamivudine. 

Correct answer = D. The CK isoenzyme pattern at admission showed elevated MB isozyme, indicating that the patient had experienced a myocardial infarction in the previous 12 to 24 hours. [Note 48 to 64 hours after an infarction, the MB isozyme would have returned to normal values.] On day 2, 12 hours after the cardioconversions, the MB isozyme had decreased, indicating no further damage to the heart. However, the patient showed an increased MM isozyme after cardo-conversion. This suggests damage to muscle, probably a result of the convulsive muscle contractions caused by repeated cardioconversion. Angina is typically the result of transient spasms in the vasculature of the heart, and would not be expected to lead to tissue death that results in elevation in serum creatine kinase. 

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