PMID: 6161234Nov 1, 1980Paper

Protease inhibitors reduce effects of denervation on muscle end-plate acetylcholinesterase

Journal of Neurochemistry
H L Fernandez, M J Duell

Abstract

The effects of certain protease inhibitors on end-plate acetylcholinesterase (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 increase in denervated muscle.

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Citations

Nov 1, 1982·Journal of the Neurological Sciences·E Chelmicka-SchorrB G Arnason
Jan 1, 1983·Progress in Neurobiology·J J McArdle
Jul 1, 1993·Progress in Neurobiology·J MassouliéF M Vallette
Oct 1, 1993·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·C Atkins, L Pezzementi
Jul 27, 1999·Chemico-biological Interactions·R GaspersicJ Sketelj
Jul 1, 1989·Circulation Research·C Nyquist-Battie, K Trans-Saltzmann
Feb 4, 1998·Acta Neurologica Scandinavica·D S TewsH M Meinck
Jan 1, 1997·The American Journal of Physiology·C Boudreau-LarivièreB J Jasmin

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