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Updated: Nov 22, 2025

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
Published on: May 17, 2016
Control of the Proliferation/Differentiation Balance in Skeletal Myoblasts by Integrin and Syndecan Targeting
Varvara Gribova1,2,3,4,5, Isabelle Pignot-Paintrand1,2, Laure Fourel6
1LMGP, Université Grenoble Alpes, F-38016 Grenoble, France.
Abstract:
Controlling the different steps of cell differentiation in vitro using bioactive surfaces may be useful in view of future cell therapies. Substrates presenting peptides, which are minimal fragments of extracellular matrix (ECM) proteins may be used for this purpose. In this work, we used polyelectrolyte multilayer films presenting two peptides derived from different muscle ECM proteins to target syndecan or/and integrin receptors. We showed that the presence of laminin-derived peptide to target syndecan-1 promotes lamellipodia formation, increases migration speed, directionality, and cell proliferation but impaired myotube formation. The cellular effects of L2synd are under the control of Rac1 and Cdc42 activities and involved β1 integrin in contrast to RGD-containing peptide, which enabled adhesion via β3 integrins and muscle cell differentiation. Our results show that peptides grafted onto multilayered films can guide the proliferation/differentiation balance and reveal crosstalk between different adhesion receptors.
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