Isoenzyme distribution of creatine kinase and lactate dehydrogenase in serum and skeletal muscle in Duchenne muscular dystrophy, collagen disease, and other muscular disorders.

Abstract

We determined the total activity and isoenzyme distribution of lactate dehydrogenase and creatine kinase in serum and biopsy specimens from skeletal muscle of nine normal individuals and nine patients with Duchenne muscular dystrophy (I), five with collagen disease (II), and four with non-progressive unclassified myopathy (III). Mean total serum creatine kinase in patients with Duchenne muscular dystrophy (867 U/liter, SD = 197) was 31-fold that in the control group (28 U/liter, SD = 14). There was also a small (3.3-fold) increase in the mean total serum creatine kinase of patients with III, but none in the serum from patients with II. Changes in the creatine kinase isoenzyme distribution of skeletal muscle were primarily in the MB isoenzyme. The mean percentage of creatine kinase-MB activity in muscle from patients with I (2.81, SD = 1.15) and patients with III (1.69, SD = 1.07) significantly (P less than 0.005) exceeded that of the control group (0.43, SD = 0.18). Muscle from patients with II showed little change. The most striking changes in lactate dehydrogenase were also observed in patients with I, in whom the mean total serum activity (356 U/liter, SD = 115) was 3.4-fold that of serum from the control group (105 U/liter, SD = 19). Skeletal muscle from these patients also showed a significant decrease in mean percent isoenzyme 5 activity (from 50 to 23) and an increase in that of isoenzymes 1 and 2 (from 1 to 9 and 8 to 20, respectively). These changes in the distribution of these two sets of isoenzymes in muscle were reflected in the serum.

Geographic distribution of xanthine oxidase, free radical scavengers, creatine kinase, and lactate dehydrogenase enzyme systems in rat heart and skeletal muscle

“…4) supports the theory that the muscle type LD (LD4, LD5) is especially geared to serve as a pyruvate reductase in anaerobically metabolizing tissues, whereas the heart type (LD 1, 2 ) is better suited to serve as a n LD in aerobically metabolizing tissues (Everse and Kaplan, 1975). The distribution of LD isoenzymes in the rat found in our study is similar to that previously described in humans and other animal species (Yasmineh et al, 1978). However, our study examined a larger cross section of different muscle types.…”

Muscular sufficiency, serum protein, enzymes and bioenergetic studies (31‐phosphorus magnetic resonance spectroscopy) in chronic malnutrition

“…The serum enzyme activities of LDH, ALP, AST, ALT, CK, CK-MB and CK-MM were significantly increased suggesting the release and leakage of enzymes into the circulation due to muscle degradation. Serum enzymes, electromyography and muscle biopsy form the complete work-up for the diagnosis of various myopathies (6,16,17). The increased levels of serum enzymes are suggestive of myopathies but are not specific for any type of myopathy.…”

Serum CK‐MB activity in progressive muscular dystrophy: Is it of nosologic value?

“…In the last few years, creatine-kinase (CK) isoenzyme activity has been studied widely in serum and muscle of patients with progressive muscular dystrophies. This enzyme has three isoenzyme forms: MM, predominant in cardiac and skeletal muscle; BB, present in the brain; and MB, which is the hybrid form present in minor quantity in cardiac and skeletal muscle [Dawson and Fine, 19671. An increase in CK-MB in dystrophic muscle has been reported by most authors working in the field [Miyazaki et al, 1966;Goto et al, 1969;Tzvetanova, 1971;Somer et al, 1976;Tzvetanova, 1978;Yasmineh et al, 1978;Ionasescu et al, 19811, but a normal distribution of CK isoenzymes has been found by others [Kar and Pearson, 1965;Cao et al, 1968;Laudahn, 19741. The first investigation on serum activity in dystrophic patients reported the presence of only the CK-MM form [Rosalki, 1965;Miyazalu et al, 19661. More recently, with the improvement of electrophoresis and techniques of enzymatic assays, the presence of CK-MB in myopathic serum has been reported more frequently [Goto and Kabuki, 1970;Cao et al, 1971;Somer et al, 1973;Goto, 1974;Somer et al, 1976;Goedde et al, 1977;Tzvetanova, 1978;Goedde et al, 19781.…”