The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
A Biochemical Characterization of the Binding of Osteopontin to Integrins αvβ1 and αvβ5
Open accessAbstract
Osteopontin (OPN) is an extracellular matrix protein that binds to integrin alpha v beta 3. Here we demonstrate that two other integrins, alpha v beta 1 and alpha v beta 5, are also receptors for OPN. Human embryonic kidney 293 cells adhere to human recombinant osteopontin (glutathione S-transferase-osteopontin; GST-OPN) using integrin alpha v beta 1. When the 293 cells are transfected with the beta 5 subunit, they can also adhere to GST-OPN using integrin alpha v beta 5. Divalent cations regulate the binding of GST-OPN to both alpha v beta 1 and alpha v beta 5. Mg2+ and Mn2+ support the binding of GST-OPN to these integrins but Ca2+ does not. The highest affinity is observed in Mn2+. In the presence of this ion, the affinity of GST-OPN for alpha v beta 1 is 18 nM and the affinity for alpha v beta 5 is 48 nM. The antibody 8A2, which is an agonist for beta 1, promotes the adhesion of 293 cells to GST-OPN even when Ca2+ is present. This observation suggests that cellular events could modulate the affinity of alpha v beta 1 for OPN. Collectively, these findings prove that integrins alpha v beta 1, alpha v beta 3, and alpha v beta 5 have similar affinity for OPN. Therefore, all three integrins must be considered when evaluating the biological affects of OPN.
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Metadata
- Authors
- Hu, D. D., Lin, E. C. K., Kovach, N. L., Hoyer, J. R., & Smith, J. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-11
- Volume
- 270
- Issue
- 44
- Pages
- 26232-26238
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1994724799
- Cited by
- 254
- References
- 41
- FWCI
- 7.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hu, D. D., Lin, E. C. K., Kovach, N. L., Hoyer, J. R., & Smith, J. W. (1995). A Biochemical Characterization of the Binding of Osteopontin to Integrins αvβ1 and αvβ5. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.44.26232
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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