Interplay between integrins and cadherins to control bone differentiation upon BMP-2 stimulation

authors

• Valat Anne
• Fourel Laure
• Sales Adria
• Machillot Paul
• Bouin Anne-Pascale
• Fournier Carole
• Bosc Lauriane
• Arboléas Mélanie
• Bourrin-Reynard Ingrid
• Wagoner Johnson Amy J
• Bruckert Franz
• Albigès-Rizo Corinne
• Picart Catherine

keywords

• Osteoblast differentation
• BMP-2 bone morphogenetic protein-2
• Adhesion receptors
• Integrins
• Cadherins
• Extracellular matrix ECM

abstract

BMP-2 enable the revelation of specific roles of the adhesive receptors depending on the transcription factor. Discussion: While β3 integrin and cadherin-11 work in concert to control early pSMAD1,5,9 signaling, β1 integrin and Cadherin-11 control RunX2, ALP activity and fibronectin organization around the cells. In contrast, while β1 integrin is also important for osterix transcriptional activity, Cadherin-11 and β5 integrin act as negative osterix regulators. In addition, β5 integrin negatively regulates RunX2. Our results show that biomimetic films can be used to delinate the specific events associated with BMP-2-mediated muscle to bone transdifferentiation. Our study reveals how integrins and cadherins work together, while exerting distinct functions to drive osteogenic programming. Different sets of integrins and cadherins have complementary mechanical roles during the time window of this transdifferentiation.

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