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(Received for publication, March 26, 1996, and in revised form, May 9, 1996)
From the Departament de Bioquímica i Biologia Molecular,
Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain
Skeletal muscle differentiation involves myoblast
alignment, elongation, and fusion into multinucleate myotubes, together
with the induction of regulatory and structural muscle-specific genes.
Here we show that two phosphatidylinositol 3-kinase inhibitors,
LY294002 and wortmannin, blocked an essential step in the
differentiation of two skeletal muscle cell models. Both inhibitors
abolished the capacity of L6E9 myoblasts to form myotubes, without
affecting myoblast proliferation, elongation, or alignment. Myogenic
events like the induction of myogenin and of glucose carrier GLUT4 were
also blocked and myoblasts could not exit the cell cycle, as measured
by the lack of mRNA induction of p21 cyclin-dependent
kinase inhibitor. Overexpresssion of MyoD in 10T1/2 cells was not
sufficient to bypass the myogenic differentiation blockade by LY294002.
Upon serum withdrawal, 10T1/2-MyoD cells formed myotubes and showed
increased levels of myogenin and p21. In contrast, LY294002-treated
cells exhibited none of these myogenic characteristics and maintained
high levels of Id, a negative regulator of myogenesis. These data
indicate that whereas phosphatidylinositol 3-kinase is not
indispensable for cell proliferation or in the initial events of
myoblast differentiation, i.e. elongation and alignment, it
appears to be essential for terminal differentiation of muscle
cells.
Volume 271, Number 32,
Issue of August 9, 1996
pp. 19146-19151
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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