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  • Title: Histochemical features of ragged-red fibres in diseased skeletal muscles.
    Author: Meijer AE.
    Journal: J Neurol Sci; 1990 Dec; 100(1-2):57-62. PubMed ID: 2089141.
    Abstract:
    In the present communication, the activity of 24 oxidoreductases, transferases, isomerases and hydrolases was examined histochemically in ragged-red fibres of human skeletal muscle specimens. The biopsy material was obtained from patients with neuromuscular diseases caused by an abnormally metabolic functioning of the muscle mitochondria. The granular accumulations of the ragged-red fibres were characterized by an impressive activity of all mitochondrial and most non-mitochondrial enzymes examined, whether participating in the aerobic or in the anaerobic pathways. With the exception of mitochondrial Mg2(+)-stimulated ATPase, acid phosphatase and AMP-aminohydrolase, there was no activity of the other hydrolytic enzymes studied in these regions. The strong activity of mitochondrial ATPase points to the presence of loosely coupled and/or uncoupled mitochondria. Ragged-red fibres that exhibited a diffuse and corpuscular activity of acid phosphatase, were always undergoing necrotic changes. Adsorption studies with diluted enzyme solutions demonstrated that the granular accumulations display a specific, moderate affinity for glycolytic enzymes.
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