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 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
Fibronectin type I repeat is a nonactivating ligand for EphA1 and inhibits ATF3-dependent angiogenesis. / Masuda, Junko; Usui, Ryosuke; Maru, Yoshiro.
In: Journal of Biological Chemistry, Vol. 283, No. 19, 09.05.2008, p. 13148-13155.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fibronectin type I repeat is a nonactivating ligand for EphA1 and inhibits ATF3-dependent angiogenesis
AU - Masuda, Junko
AU - Usui, Ryosuke
AU - Maru, Yoshiro
PY - 2008/5/9
Y1 - 2008/5/9
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=45149128636&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=45149128636&partnerID=8YFLogxK
U2 - 10.1074/jbc.M702164200
DO - 10.1074/jbc.M702164200
M3 - Article
C2 - 18308734
AN - SCOPUS:45149128636
VL - 283
SP - 13148
EP - 13155
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 19
ER -