Clinical Chemistry
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Clinical Chemistry 23: 2226-2230, 1977;
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Clinical Chemistry, Vol 23, 2226-2230, Copyright © 1977 by American Association for Clinical Chemistry

Mechanisms of cellular enzyme release. II. Inhibition of sarcolemmal enzymes by myopathy-inducing agents

HL Verrill, HD Gruemer and N Baba

A defective membrane mechanism has been suggested [Arch. Neurol. 33, 315 (1976)] for the pathogenesis of Duchenne muscular dystrophy. The characteristic clinical and biological findings, including leakage of cellular enzymes into the serum in the disease, have been duplicated by the imipramine/serotonin rat myopathy model. Sarcolemma was prepared from quadriceps femoris muscles of control and myopathy-affected animals. The activities of sarcolemmal adenosinetriphosphatase and acetylcholinesterase were inhibited in vitro by imipramine and serotonin. The inhibition by imipramine of these sarcolemma-bound enzyme systems decreased the Vmax and increased the Km. This mixed type of inhibition is consistent with an imipramine-induced interference at these enzyme sites and a disruption of lipid-protein interrelations. We hypothesize that such conformational membrane changes might contribute to the leakage of macromolecules such as enzymes from the cell interior.


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M. S. Hudecki, C. M. Pollina, A. K. Bhargava, and R. S. Hudecki
Screening of Antiserotoninergic Drugs With the Genetically Dystrophic Chicken
Arch Neurol, September 1, 1980; 37(9): 545 - 550.
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Copyright © 1977 by the American Association for Clinical Chemistry.