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Histochemical localization of carbonic anhydrase in normal and diseased human muscle
Author(s) -
Peyronnard JeanMarie,
Charron Louise F.,
Messier JeanPierre,
Lavoie Jeanne,
FaracoCantin Féliciana,
Dubreuil Martin
Publication year - 1988
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880110204
Subject(s) - carbonic anhydrase , atrophy , muscle biopsy , enzyme , succinate dehydrogenase , adenosine triphosphatase , dihydrolipoamide dehydrogenase , anatomy , biopsy , biology , pathology , biochemistry , dehydrogenase , atpase , chemistry , endocrinology , medicine
A method is described for histological localization of carbonic anhydrase (CA) in sections of frozen human muscle using the rapid and inexpensive histochemical technique of Hansson. Results obtained in normal subjects indicate clearly that CA reactive fibers are of type 1. Similarly, abnormalities seen with CA in the muscle biopsy of a patient presenting with type 1 fiber hypotrophy and preponderance duplicated almost exactly those observed with the actinomyosine adenosine triphosphatase and the reduced nicotin‐amide adenine dinucleotide dehydrogenase reactions. Observations of grouped CA‐positive muscle fibers in a case of chronic neurogenic atrophy suggest that, like other enzymes, CA expression in muscle is under neurogenic control.