Angiogenin

Literature References: Single-chain, basic protein of 123 amino acids that induces the in vivo formation of blood vessels. Mol wt ~14,000 Da. First isolated from human adenocarcinoma cells; subsequently found in normal human plasma and shown to be produced by the liver. Angiogenin exhibits a characteristic ribonucleolytic activity toward 28S and 18S ribosomal RNA. Its amino acid sequence is 35% identical with that of human pancreatic ribonuclease. Isoln, characterization, and angiogenic activity: J. W. Fett et al., Biochemistry 24, 5480 (1985). Amino acid sequence: D. J. Strydom et al., ibid. 5486. Cloning and DNA sequence of human angiogenin gene: K. Kurachi et al., ibid. 5494. Structural study: K. A. Palmer et al., Proc. Natl. Acad. Sci. USA 83, 1965 (1986). Ribonucleolytic activity: R. Shapiro et al., Biochemistry 25, 3527 (1986). Isoln from normal human plasma: R. Shapiro et al., ibid. 26, 5141 (1987). Tissue distribution in neonatal and adult rats: H. L. Weiner et al., Science 237, 280 (1987); in human tumor and normal cells: S. M. Rybak et al., Biochem. Biophys. Res. Commun. 146, 1240 (1987). Inhibition of protein synthesis: D. K. St. Clair et al., Proc. Natl. Acad. Sci. USA 84, 8330 (1987). Inhibition of angiogenic and ribonucleolytic activities of angiogenin by placental ribonuclease inhibitor: R. Shapiro, B. L. Vallee, ibid. 2238; F. S. Lee, B. L. Vallee, Biochemistry 28, 3556 (1989). Reviews: J. F. Riordan, B. L. Vallee, Br. J. Cancer 57, 587-590 (1988); B. L. Vallee, J. F. Riordan, Adv. Exp. Med. Biol. 234, 41-53 (1988).