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Involvement of the ERK/MAP kinase signalling pathway in milli-calpain activation and myogenic cell migration

Ludovic Leloup1, Laetitia Daury, Germain Mazères

  • 1Université Bordeaux 1, Unité Protéolyse, Croissance et Développement Musculaire, INRA USC-2009, ISTAB, avenue des Facultés, 33405 Talence Cedex, France. ludovic.leloup@etu.u-bordeaux1.fr

The International Journal of Biochemistry & Cell Biology
|April 17, 2007
PubMed

Insights

Insulin-like growth factor-1 (IGF-1), transforming growth factor-beta1 (TGF-beta1), and insulin stimulate myoblast migration via the ERK/MAP kinase pathway, increasing milli-calpain activity.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Insulin-like growth factor-1 (IGF-1), transforming growth factor-beta1 (TGF-beta1), and insulin stimulate myoblast migration.
  • This stimulation involves increased milli-calpain expression and activity.
  • The specific signaling pathways mediating these effects are currently unknown.

Purpose of the Study:

  • To identify the signaling pathway(s) responsible for IGF-1, TGF-beta1, and insulin-induced myoblast migration.
  • To elucidate the role of these pathways in regulating milli-calpain expression and activity.

Main Methods:

  • Wound healing assays were performed using myoblasts treated with growth factors.
  • Specific inhibitors for ERK/MAP kinase and PI3K/Akt pathways were employed.
  • Milli-calpain expression and activity were assessed via Western blotting and enzyme assays.

Main Results:

  • Inhibition of the ERK/MAP kinase pathway abolished the migratory effects of the growth factors.
  • The ERK/MAP kinase pathway was identified as the mediator for the up-regulation of milli-calpain expression and activity.
  • The PI3K/Akt pathway, MyoD, and myogenin were found not to be involved.

Conclusions:

  • The ERK/MAP kinase signaling pathway is the primary mediator of IGF-1, TGF-beta1, and insulin-induced myoblast migration.
  • This pathway also regulates milli-calpain expression and activity, crucial for myoblast migration.

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