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  Fibronectins containing extradomain A or B enhance osteoblast differentiation via distinct integrins

Sens, C., Huck, K., Pettera, S., Uebel, S., Wabnitz, G., Moser, M., et al. (2017). Fibronectins containing extradomain A or B enhance osteoblast differentiation via distinct integrins. Journal of Biological Chemistry, 292(19), 7745-7760. doi:10.1074/jbc.M116.739987.

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 Creators:
Sens, Carla1, Author              
Huck, Katrin1, Author              
Pettera, Stefan2, Author              
Uebel, Stephan2, Author              
Wabnitz, Guido3, Author
Moser, Markus4, Author              
Nakchbandi, Inaam1, Author              
Affiliations:
1Nakchbandi, Inaam / Translational Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565162              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              
3external, ou_persistent22              
4Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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Free keywords: SPLICED EDA SEGMENT; CELL-ADHESION; IN-VITRO; BONE-FORMATION; MICE LACKING; MATRIX; ALPHA-V-BETA-3; EXPRESSION; BINDING; OSTEOCLASTSBiochemistry & Molecular Biology;
 Abstract: Fibronectin is a multidomain protein secreted by various cell types. It forms a network of fibers within the extracellular matrix and impacts intracellular processes by binding to various molecules, primarily integrin receptors on the cells. Both the presence of several isoforms and the ability of the various domains and isoforms to bind to a variety of integrins result in a wide range of effects. In vivo findings suggest that fibronectin isoforms produced by the osteoblasts enhance their differentiation. Here we report that the isoform characterized by the presence of extradomain A activates alpha 4 beta 1 integrin and augments osteoblast differentiation. In addition, the isoform containing extradomain B enhances the binding of fibronectin through the RGD sequence to beta 3-containing integrin, resulting in increased mineralization by and differentiation of osteoblasts. Our study thus reveals novel functions for two fibronectin isoforms and the mediating receptors in osteoblast differentiation.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000401154100006
DOI: 10.1074/jbc.M116.739987
 Degree: -

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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 292 (19) Sequence Number: - Start / End Page: 7745 - 7760 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826