Eyster K M, McFarland D C
Department of Physiology and Pharmacology, University of South Dakota, Vermillion 57069, USA.
Comp Biochem Physiol B Biochem Mol Biol. 1995 Nov;112(3):549-55. doi: 10.1016/0305-0491(95)00107-7.
The current studies were undertaken to determine whether embryonic myoblasts or myogenic satellite cells undergoing differentiation and fusion contained endogenous modulators of protein kinase C (PKC). Clonal-derived turkey embryonic myoblast and satellite cell cultures were harvested at confluency and at approximately 40% fusion (embryonic myoblasts) or 75% fusion (satellite cells). PKC activity in cystosolic preparations of the cells and myotubes was undetectable. Cytosolic extracts (0.065 mg protein) of confluent and fused satellite cell cultures and confluent embryonic myoblasts had no effect on control PKC activity (control: 14.9 pmol/min, control + cytosols: 15.2, 13.9 and 13.5 pmol/min, respectively). Cytosolic preparations (0.065 mg protein) of embryonic myoblast-derived myotubes inhibited control PKC activity (4.0 pmol/min). In a time-course study, PKC-inhibitory activity was present in embryonic myoblasts at the earliest time point examined (30% fusion). Additionally, protein phosphatase activity correlated with PKC inhibitory activity. Thus, PKC-inhibitory activity appears as embryonic myoblasts begin to undergo fusion to form myotubes, but is not present in differentiating satellite cells.
