| Autor: |
Pike, Sandra E., Yao, Lei, Jones, Karen D., Cherney, Barry, Appella, Ettore, Sakaguchi, Kazuyasu, Nakhasi, Hira, Teruya-Feldstein, Julie, Wirth, Peter, Gupta, Ghanshyam, Tosato, Giovanna |
| Zdroj: |
The Journal of Experimental Medicine; December 1998, Vol. 188 Issue: 12 p2349-2356, 8p |
| Abstrakt: |
An endothelial cell inhibitor was purified from supernatant of an Epstein-Barr virus–immortalized cell line and identified as fragments of calreticulin. The purified recombinant NH2-terminal domain of calreticulin (amino acids 1–180) inhibited the proliferation of endothelial cells, but not cells of other lineages, and suppressed angiogenesis in vivo. We have named this NH2-terminal domain of calreticulin vasostatin. When inoculated into athymic mice, vasostatin significantly reduced growth of human Burkitt lymphoma and human colon carcinoma. Compared with other inhibitors of angiogenesis, vasostatin is a small, soluble, and stable molecule that is easy to produce and deliver. As an angiogenesis inhibitor that specifically targets proliferating endothelial cells, vasostatin has a unique potential for cancer treatment. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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