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Lysosomal and Nonlysosomal Hydrolases of Skeletal Muscle in Neuromuscular Diseases
Timo E. S. Takala, MD, PhD;
Vilho V. Myllylä, MD, PhD;
Antero Salminen, MSc;
Uolevi Tolonen, MD, PhD;
Ilmo E. Hassinen, MD, PhD;
Veikko Vihko, PhD
Arch Neurol. 1983;40(9):541-544.
Abstract
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• The activities of four lysosomal and two nonlysosomal hydrolases were studied in skeletal muscle biopsy samples from patients with neuromuscular diseases and from controls. β-Glucosaminidase activity was increased in polymyositis. β-Glucuronidase and alkaline protease activities were elevated in muscular dystrophy in adults, whereas cathepsin D activity was increased in amyotrophic lateral sclerosis. There were significant correlations between the activities of lysosomal and nonlysosomal hydrolases. The activity of β-glucuronidase, β-glucosaminidase, alkaline protease, and dipeptidyl aminopeptidase IV showed a positive correlation with the severity of muscular atrophy. The activities of these hydrolases and the activity of dipeptidyl aminopeptidase I correlated positively with the activities of muscular galactosylhydroxylysyl glucosyltransferase and with the serum concentration of type III procollagen aminoterminal propeptide. The results suggest that in neuromuscular diseases the lysosomal and nonlysosomal pathways for muscle degradation are affected concomitantly with collagen biosynthesis.
Author Affiliations
From the Departments of Clinical Chemistry (Dr Takala), Neurology (Drs Myllylä and Tolonen), and Medical Biochemistry (Dr Hassinen), University of Oulu (Finland), and the Department of Cell Biology (Mr Salminen and Dr Vihko), University of Jyväskylä (Finland).
Footnotes
Accepted for publication Dec 29, 1982.
Reprint requests to the Department of Neurology, University of Oulu, SF-90220 Oulu 22, Finland (Dr Myllylä).
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