Premium
Protein phosphorylation in fast and slow chicken skeletal muscles: Effect of denervation
Author(s) -
Wang X.,
Rostas J.A.P.
Publication year - 1998
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/(sici)1097-4598(199804)21:4<504::aid-mus9>3.0.co;2-d
Subject(s) - phosphoprotein , phosphorylation , skeletal muscle , denervation , protein kinase a , biology , glycogen phosphorylase , calmodulin , endocrinology , medicine , phosphorylase kinase , phenotype , cyclic adenosine monophosphate , protein phosphorylation , biochemistry , enzyme , receptor , gene , glycogen
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 3′,5′‐monophosphate (cAMP)‐stimulated, calmodulin‐inhibited 28‐kDa band (markers for fast muscle), a calmodulin‐stimulated 50‐kDa band, and two cAMP‐stimulated bands at 44 and 46 kDa (markers for slow muscle), and the relative concentrations of the regulatory subunits of cAMP‐dependent protein kinase (RI and RII). After denervation the pattern of phosphorylation in fast muscle changed to resemble that of slow muscle: phosphorylation of the fast phenotype markers decreased; the slow phenotype markers, barely detectable in normal fast muscle, appeared as significant phosphoproteins; and the concentration of RII increased with no change in RI. This is consistent with denervation‐induced changes observed using other phenotypic markers and indicates the potential for using these phosphoprotein markers in studies of muscle development and pathophysiology. © 1998 John Wiley & Sons, Inc. Muscle Nerve 21:504–513, 1998.