期刊
BLOOD
卷 115, 期 20, 页码 4138-4147出版社
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2009-05-223057
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资金
- Japanese Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for the Promotion of Science
- University of Tsukuba
- AstraZeneca [2004]
- Kowa Life Science Foundation
- Kato Memorial Bioscience Foundation
- [17390073]
- [20012007]
- [21590328]
- Grants-in-Aid for Scientific Research [21590328] Funding Source: KAKEN
E2-2 belongs to the basic helix-loop-helix (bHLH) family of transcription factors. E2-2 associates with inhibitor of DNA binding (Id) 1, which is involved in angiogenesis. In this paper, we demonstrate that E2-2 interacts with Id1 and provide evidence that this interaction potentiates angiogenesis. Mutational analysis revealed that the HLH domain of E2-2 is required for the interaction with Id1 and vice versa. In addition, Id1 interfered with E2-2-mediated effects on luciferase reporter activities. Interestingly, injection of E2-2-expressing adenoviruses into Matrigel plugs implanted under the skin blocked in vivo angiogenesis. In contrast, the injection of Id1-expressing adenoviruses rescued E2-2-mediated inhibition of in vivo angiogenic reaction. Consistent with the results of the Matrigel plug assay, E2-2 could inhibit endothelial cell (EC) migration, network formation, and proliferation. On the other hand, knockdown of E2-2 in ECs increased EC migration. The blockade of EC migration by E2-2 was relieved by exogenous expression of Id1. We also demonstrated that E2-2 can perturb VEGFR2 expression via inhibition of VEGFR2 promoter activity. This study suggests that E2-2 can maintain EC quiescence and that Id1 can counter this effect. (Blood. 2010; 115(20): 4138-4147)
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