|
|
|
|
|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | ||||
|
Fig. 4. p38-MAPK and PI3K are activated in proliferation and are not controlled
by the differentiation-linked hyperpolarization. (A) Activation of
p38-MAPK pathway was detected by western blot using an antibody directed
against phospho-p38-MAPK (Thr180/Tyr182). Phospho-p38-MAPK is present in
proliferating myoblasts (GM), is maintained in differentiating myoblasts (DM)
and depolarization induced by 10 mM Cs+ (Cs10 mM) does not affect
the level of phosphorylation. By contrast, myogenin expression associated with
differentiation is reduced in presence of Cs+. Protein extracts
were prepared at the indicated time. (B) Phosphorylation of recombinant
ATF2 by immunoprecipitated phospho-p38-MAPK was used to assess p38-MAPK
activity. ATF2 phosphorylation has been detected with an antibody specific for
phospho-ATF2 (Thr71). Phospho-p38-MAPK was immunoprecipitated from
proliferating myoblasts (GM), and from myoblasts differentiated for 4 and 24
hours in presence or absence of 10 mM Cs+. (C) Detection of
phospho-AKT by western blot. Myoblasts were grown in media without exogenous
insulin. Phospho-AKT (Ser473/Thr308) is present in proliferating myoblasts
(GM) and myoblasts differentiated for 24 hours (DM). Phospho-AKT expression is
not affected by 10 mM Cs+ (Cs10) or 15 µM BAPTA-AM (BA).
Myogenic differentiation is confirmed by myogenin expression.
|
