Lack of effect of ouabain on creatine phosphokinase efflux from skeletal muscle

TY - JOUR

T1 - Lack of effect of ouabain on creatine phosphokinase efflux from skeletal muscle

AU - Meltzer, Herbert Y.

N1 - Funding Information: Plasma creatine phosphokinase (CPK) (EC 2.7.3.2) activity is elevated in a variety of human and animal skeletal and cardiac muscle diseases, among them Duchenne muscular dystrophy [I]. hamster muscular dystrophy [Z], myocardial infarction [3], malignant hyperpyrexia [4], hypothyroidism [S] and alcoholic myopathy L6]. Since CPK activity is confined almost exclusively to skeletal muscle, cardiac muscle and brain, only these tissues need be considered as sources of serum CPK [7]. Since brain-type CPK is rarely present in serum, only skeletal and cardiac muscle need be considered as sources of CPK activity in serum under most circumstances. There are probably a variety of mechanisms for the exit of CPK from muscle and its entry into serum. Release from necrotic cells, though important in such diseases as rhabdomyolysis [S] and myocardial infarction [9], may not be the major one in most conditions with increased serum CPK activity. It has been suggested that proteins such as CPK can passively diffuse through the cell membrane [IO] or can be transported across the cell membrane [I I]. It has also been proposed that diminished activity 01 Na+,K’-adenosine triphosphatase (Na+.K+-ATPase), which is part of the sarcolemma [IZ], and which mediates Na’-K+ ion flux. is causally related to the efflux of CPK from skeletal muscle and its subsequent entry into plasma in malignant hyperpyrexia [13]. This was based on the finding of decreased erythrocyte Na’,K’-ATPase activity in 8 of 13 people at high risk for malignant hyperpyrexia [13]. It was proposed that in malignant hyperpyrcxia a decrease in Na+,K+-ATPase activity and anesthetic agents might interact to produce uncoupling of oxidative phosphorylation. which would lead to muscle breakdown. Further evidence for this theory is the observation that massive, prolonged increases in serum CPK activity occur in volunteers given small doses of digoxin [14]. This led to the proposal that digoxin. an inhibitor of Na+.K+-ATPase, had a direct effect * Supported by USPHS 25,116 and 16.127 and by State of Illinois 431-13-RD. Dr. Meltzer is recipient of USPHS Career Development Award MH 47,808. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1975/2/1

Y1 - 1975/2/1

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U2 - 10.1016/0006-2952(75)90228-2

DO - 10.1016/0006-2952(75)90228-2

M3 - Article

C2 - 1125051

AN - SCOPUS:0016466288

SN - 0006-2952

VL - 24

SP - 419

EP - 421

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

IS - 3

ER -