Characteristic ribonucleolytic activity of human angiogenin
Citations Over TimeTop 10% of 1986 papers
Abstract
Angiogenin, a blood vessel inducing protein isolated from a human tumor cell line, has been found to exhibit ribonucleolytic activity. It catalyzes the cleavage of both 28S and 18S ribosomal RNA as determined by agarose gel electrophoresis. The major products formed with these substrates are 100-500 nucleotides in length. In contrast, angiogenin is inactive toward all of the more conventional substrates of the homologous pancreatic ribonucleases. In particular, it does not produce detectable amounts of acid-soluble fragments from high molecular weight wheat germ RNA, poly(C), or poly(U), nor does it hydrolyze cytidine or uridine cyclic 2',3'-phosphate. The high degree of sequence homology between angiogenin and the pancreatic ribonucleases, which includes all three catalytic residues, His-12, Lys-41, and His-119, has thus identified the chemical nature of a potential angiogenin substrate. These results may bear importantly on the physiological function of angiogenin.
Related Papers
- → Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease.(1994)154 cited
- → Structure and Action of Mammalian Ribonuclease (Angiogenin) Inhibitor(1993)101 cited
- → Immunosuppressive activity of angiogenin in comparison with bovine seminal ribonuclease and pancreatic ribonuclease(1995)56 cited
- → Structure and Function of Angiogenin(1997)54 cited
- → Crystallization and Crystal Structure Determination of Ribonuclease A-Ribonuclease Inhibitor Protein Complex(2003)6 cited