Abstract
The four collagen-binding αI domain integrins form their own subgroup among cell adhesion receptors. The signaling functions of α1β1 and α2β1 integrins have been analyzed in many experimental models, whereas less studies are available about the more recently found α10β1 and α11β1 heterodimers. Interestingly, collagen binding by α1β1 and α2β1 often generates opposite cellular responses. For example α1β1 has often been reported to promote cell proliferation and to suppress collagen synthesis, whereas α2β1 can in many model systems inhibit growth and promote collagen synthesis. There are obviously cell type dependent factors modifying the signaling. Additionally the structure and the organization of collagenous matrix play a critic role. Many recent studies have also stressed the importance of the crosstalk between the integrins and other cell surface receptors.
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Acknowledgments
Original integrin-related studies in the author’s research group have been supported by the Academy of Finland, the Sigrid Jusélius Foundation, the Finnish Cancer Association and the European Union (Metafight and CAFFEIN in the 7th Framework Programme).
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Heino, J. (2014). Cellular Signaling by Collagen-Binding Integrins. In: Gullberg, D. (eds) I Domain Integrins. Advances in Experimental Medicine and Biology, vol 819. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9153-3_10
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