J. Vodiskar et al., Combined effects of glucocorticoids and electromechanical activity on the acetylcholinesterase expression in the fast rat muscle, CHEM-BIO IN, 120, 1999, pp. 333-339
Protein synthesis is impaired in the glucocorticoid (GC)-treated fast mamma
lian muscle. Electromechanical activity was reported to alleviate this effe
ct. Acetylcholinesterase (AChE; EC 3.1.1.7) synthesis in the skeletal muscl
e is regulated by both, GCs and electromechanical activity. In light of the
above reports, one would expect that electrical stimulation will prevent G
C-mediated fall of AChE synthesis in the muscle. On the other hand, a subst
antial body of evidence suggests that electromechanical activity exerts its
effect at the AChE mRNA level, while GCs most probably act at the translat
ional or early posttranslational level. Different levels of action would be
more consistent with the independent and therefore additive influences of
the two regulatory factors. In order to ascertain whether glucocorticoid an
d electromechanical effects interact in the control of AChE activity, we co
mpared the effects of GCs on normal, nonstimulated fast rat skeletal muscle
, with those of GC-treated and simultaneously electrically stimulated (toni
c pattern, 10 Hz) muscle. Untreated and stimulated-only muscles were used a
s respective controls. The effects on the fast extensor digitorum longus mu
scle and slow soleus muscle, treated similarly were compared. As expected,
chronic GC treatment and electrical stimulation of fast rat muscles with sl
ow activity patterns both downregulated AChE activity. However, no addition
al decrease in AChE activity was observed, if stimulated fast muscle was si
multaneously treated with GCs, suggesting that slow pattern of electromecha
nical activity prevents GC-mediated downregulation of AChE. The most plausi
ble explanation of this observation is, that muscle activity blocks express
ion of some generally acting factors, which are induced by GCs and are resp
onsible for the impaired synthesis of several proteins including AChE. (C)
1999 Elsevier Science Ireland Ltd. All rights reserved.