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Increased phosphorylation of nuclear protein in myonuclei isolated from denervated skeletal muscle

โœ Scribed by Dr. Irene R. Held


Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
393 KB
Volume
9
Category
Article
ISSN
0360-4012

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โœฆ Synopsis


The slow-twitch soleus muscle of the rat hindlimb was denervated by cutting the sciatic nerve in the midthigh on one side. A sham operation was performed on the contralateral side to provide a control soleus muscle. At 24, 48, 72, and 120 hours after these surgical procedures, the animals were sacrificed and the nuclei which were isolated from these muscles incubated in a phosphorylating medium containing [y-32P]ATP. At the 48 hour denervation period only, the in vitro phosphorylation of TCA-precipitable nuclear proteins was significantly increased compared to control values. Resolution of the SDS-solubilized nuclear proteins by polyacrylamide gel electrophoresis revealed that the increased phosphorylation was more marked in some phosphoproteins than others. The significance of these early denervation changes are discussed with respect to increases in the activities of the nuclear RNA polymerases and changes in the phosphorylation of cytosolic protein.


๐Ÿ“œ SIMILAR VOLUMES


Protein phosphorylation in fast and slow
โœ X. Wang; J.A.P. Rostas ๐Ÿ“‚ Article ๐Ÿ“… 1998 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 620 KB

We have identified proteins in adult chicken skeletal muscle whose phosphorylation can be used as markers for the mature fast and slow muscle phenotype. These include phosphorylase, phosphorylase kinase, and a cyclic adenosine 3ะˆ,5ะˆ-monophosphate (cAMP)-stimulated, calmodulin-inhibited 28-kDa band (