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J Biol Chem, Vol. 274, Issue 25, 17437-17444, June 18, 1999
B and Inducible Nitric-oxide Synthase Define a
Common Myogenic Signaling Pathway
From the Departament de Bioquímica i Biologia Molecular,
Facultat de Biologia, Universitat de Barcelona, Avinguda Diagonal
645, 08028 Barcelona, Spain
Insulin-like growth factors (IGFs) are potent
inducers of skeletal muscle differentiation and phosphatidylinositol
(PI) 3-kinase activity is essential for this process. Here we show that
IGF-II induces nuclear factor-
B (NF-B) and nitric-oxide synthase
(NOS) activities downstream from PI 3-kinase and that these events are critical for myogenesis. Differentiation of rat L6E9 myoblasts with
IGF-II transiently induced NF-B DNA binding activity, inducible nitric-oxide synthase (iNOS) expression, and nitric oxide (NO) production. IGF-II-induced iNOS expression and NO production were blocked by NF-B inhibition. Both NF-B and NOS activities were essential for IGF-II-induced terminal differentiation (myotube formation and expression of skeletal muscle proteins: myosin heavy chain, GLUT 4, and caveolin 3), which was totally blocked by NF-B or
NOS inhibitors in rat and human myoblasts. Moreover, the NOS substrate
L-Arg induced myogenesis in the absence of IGFs in
both rat and human myoblasts, and this effect was blocked by NOS
inhibition. Regarding the mechanisms involved in IGF-II activation of
NF-B, PI 3-kinase inhibition prevented NF-B activation, iNOS
expression, and NO production. Moreover, IGF-II induced, through a PI
3-kinase-dependent pathway, a decrease in IB-
protein
content that correlated with a decrease in the amount of IB-
associated with p65 NF-B.
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