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Phosphorylative neuromodulation of the regulatory subunit of cyclic AMP-dependent protein kinase type II in skeletal muscle

✍ Scribed by J. A. McLane; S. P. Squinto; H. C. Yeoh; I. R. Held

Publisher: John Wiley and Sons
Year: 1985
Tongue: English
Weight: 607 KB
Volume: 14
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.490140208

No coin nor oath required. For personal study only.

✦ Synopsis

The phosphorylative neuromodulation of the regulatory subunit of protein kinase type II (R-II) in cytosolic fractions from denervated and sham-operated, contralateral soleus muscles of the rat was evaluated. The denervation-induced increase in the 32P-phosphorylation of R-II is not related to an increased dephosphorylation by cation-dependent or cation-independent protein phosphatases in the cytosolic fractions. The level of 32P-phosphorylation of an exogenous heptapeptide substrate (Kemptide) by dissociated catalytic subunits of cyclic AMP-dependent protein kinase in cytosolic fractions from denervated and sham-operated solei did not differ. Also, no change in the concentration of cytosolic R-II assessed by competitive enzyme-linked immunosorbent assays (ELISA) was found after denervation. However, the in vitro 32P-phosphorylation of R-II in these samples was increased. Taken together, our results suggest that the increased availability of autophosphorylatable sites reflects an in vivo modulation of R-II phosphorylation rather than a significant change in total R-II content.

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