Temporal relationship between nerve-stump-length-dependent changes in the autophosphorylation of a cyclic AMP-dependent protein kinase and the acetylcholine receptor content in skeletal muscle

The acetylcholine receptor (AChR) content and the autophosphorylation of the regulatory subunit of cyclic AMP-dependent protein kinase type II (R-II) were evaluated in rats soleus muscles at 24, 30 and 66 hr after surgical denervation by cutting the nerve at a short distance (short-nerve-stump) and...

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Bibliographic Details
Published in:Neurochemical research 1988-12, Vol.13 (12), p.1125-1131
Main Authors: Sayers, S T, Yeoh, H C, McLane, J A, Held, I R
Format: Article
Language:English
Subjects:
Animals
Autoradiography
In Vitro Techniques
Male
Muscle Denervation
Muscles - enzymology
Muscles - metabolism
Phosphorylation
Protein Kinases - metabolism
Radioligand Assay
Rats
Receptors, Cholinergic - metabolism
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Summary:The acetylcholine receptor (AChR) content and the autophosphorylation of the regulatory subunit of cyclic AMP-dependent protein kinase type II (R-II) were evaluated in rats soleus muscles at 24, 30 and 66 hr after surgical denervation by cutting the nerve at a short distance (short-nerve-stump) and at a long distance (long-nerve-stump) from the muscle. AChR content was based on the specific binding of [125I]alpha-bungarotoxin (BUTX); changes in the autophosphorylation of R-II were based upon the predominant in vitro 32P-phosphorylation of a 56-Kd soluble protein in cytosolic fractions of solei. The AChR content and the 32P-autophosphorylation of R-II were increased in samples from short-nerve-stump solei, but not from long-nerve-stump solei, after a denervation-time of 30 hr. This nerve-stump-length dependency indicates that the two denervation effects are not related to the immediate halt of impulse-evoked muscle contractility. Furthermore, the results show that alterations in the 32P-autophosphorylation of R-II occurred before, as well as whenever, increases in the AChR content were found. Speculatively, this temporal relationship may be significant with respect to the potential role of R-II in gene expression.
ISSN:0364-3190
1573-6903
DOI:10.1007/BF00971629