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Protease Inhibitors Reduce Effects of Denervation on Muscle End‐Plate Acetylcholinesterase
Author(s) -
Fernandez Hugo L.,
Duell Myron J.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb07872.x
Subject(s) - leupeptin , pepstatin , denervation , aprotinin , acetylcholinesterase , chemistry , aché , medicine , endocrinology , cholinesterase , protease , in vivo , biochemistry , enzyme , biology , microbiology and biotechnology
The effects of certain protease inhibitors on end‐plate acetyl‐cholinesterase (AChE) activity, as well as on wet weight and total protein, were studied in vivo in intact and denervated anterior gracilis muscles from the rat. A combination of leupeptin, pepstatin, and aprotinin, administered intraarterially, partly prevented the early (24 h) denervation‐induced decrease in muscle weight and protein content. In turn, leupeptin and aprotinin, either alone or in combination, markedly reduced the decay of AChE activity in the denervated muscles, whereas pepstatin alone was ineffective. Such effects were additive in that the inhibitors in combination were more effective than when they were used separately. Additional experiments indicated that none of the inhibitors, at the concentrations used, affected AChE activity directly, nor did they have a significant effect during processing of the muscle samples. These findings indicate that the initial decay of AChE activity with denervation was effectively reduced by the inhibitors, probably through inactivation of proteolytic enzymes which, otherwise, would be increased in denervated muscle.