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The eight human canonical ribonucleases: Molecular diversity, catalytic properties, and special biological actions of the enzyme proteins

Journal

FEBS LETTERS
Volume 584, Issue 11, Pages 2194-2200

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.04.018

Keywords

Human RNase; Vertebrate RNase superfamily; Eosinophil neurotoxin; Human angiogenin; Host-defence protein

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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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