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Laboratory of Cell Biology, the
Laboratory of Pathology, and the || Laboratory of Experimental Carcinogenesis, National Cancer Institute, Bethesda, Maryland 20892
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.
Key Words: endothelial cells angiogenesis cell growth cancer antitumor agent
S.E. Pike and L. Yao contributed equally to this work.
Abbreviations used: aa, amino acids; bFGF, basic fibroblast growth factor; FBHE, fetal bovine heart endothelial cells; HUVEC, human umbilical vein endothelial cells; IP-10, IFN-
inducible protein-10; MBP, maltose-binding protein; Mig, monokine induced by IFN-
; VEGF, vascular endothelial growth factor.
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