title: The eight human "canonical" ribonucleases: molecular diversity, catalytic properties, and special biological actions of the enzyme proteins.
abstract: Human ribonucleases (RNases) are members of a large superfamily of rapidly evolving homologous proteins. Upon completion of the human genome, eight catalytically active RNases (numbered 1-8) were identified. These structurally distinct RNases, characterized by their various catalytic differences on different RNA substrates, constitute a gene family that appears to be the sole vertebrate-specific enzyme family. Apart from digestion of dietary RNA, a wide variety of biological actions, including neurotoxicity, angiogenesis, immunosuppressivity, and anti-pathogen activity, have been recently reported for almost all members of the family. Recent evolutionary studies suggest that RNases started off in vertebrates as host defence or angiogenic proteins.
authors.affiliation: Department of Structural and Functional Biology, University of Naples Federico II, Naples, Italy. ssorrent@unina.it
authors.forename: Salvatore
authors.initials: S
authors.lastname: Sorrentino
mesh_terms: D000818:Animals; D005075:Biological Evolution; D002384:Catalysis; D006801:Humans; D011506:Proteins / Q000235:genetics*; D012313:RNA / Q000235:genetics / Q000378:metabolism; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014714:Vertebrates / Q000235:genetics / Q000378:metabolism
chemical_list: D011506:Proteins; D012313:RNA; D012260:Ribonucleases