Abstract
ATF3 stimulated promoter activity of EphA1 by 3.4-fold in ATF3-dependent angiogenesis in vitro. Although tyrosine kinase activation of EphA1 was dispensable, binding of EphA1 to fibronectin through its type I repeat played an essential role in the angiogenesis. Recombinant proteins containing fibronectin 10th to 12th type I repeat (I 10-12) but not I 12 could inhibit the angiogenesis in vitro by competitively targeting EphA1 with the full-length fibronectin. However, I 12 acquired a higher affinity toward EphA2 with K d 18 nM and inhibited vascular endothelial growth factor-dependent angiogenic invasion in a Matrigel plug assay.
| Original language | English |
|---|---|
| Pages (from-to) | 13148-13155 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 283 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - May 9 2008 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Masuda, J., Usui, R., & Maru, Y. (2008). Fibronectin type I repeat is a nonactivating ligand for EphA1 and inhibits ATF3-dependent angiogenesis. Journal of Biological Chemistry, 283(19), 13148-13155. https://doi.org/10.1074/jbc.M702164200