NDLI: A small-molecule inhibitor of the ribonucleolytic activity of human angiogenin that possesses antitumor activity.

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A small-molecule inhibitor of the ribonucleolytic activity of human angiogenin that possesses antitumor activity.

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A small-molecule inhibitor of the ribonucleolytic activity of human angiogenin that possesses antitumor activity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kao, Richard Y. T. Jenkins, Jeremy L. Olson, Karen A. Shapiro, Robert Fett, James W. Key, Marc E.
Description	Author Affiliation: Kao RY ( Center for Biochemical and Biophysical Sciences, Harvard Medical School, Cambridge, MA 02139, USA.);
Abstract	The results of previous preclinical and clinical studies have identified angiogenin (ANG) as a potentially important target for anticancer therapy. Here we report the design and implementation of a high-throughput screening assay to identify small molecules that bind to the ribonucleolytic active site of ANG, which is critically involved in the induction of angiogenesis by this protein. Screening of 18,310 compounds from the National Cancer Institute (NCI) Diversity Set and ChemBridge DIVERSet yielded 15 hits that inhibit the enzymatic activity of ANG with K(i) values <100 microM. One of these, NCI compound 65828 [8-amino-5-(4'-hydroxybiphenyl-4-ylazo)naphthalene-2-sulfonate; K(i) = 81 microM], was selected for more detailed studies. Minor changes in ANG or ligand structure markedly reduced potency, demonstrating that inhibition reflects active-site rather than nonspecific binding; these observations are consistent with a computationally generated model of the ANG.65828 complex. Local treatment with modest doses of 65828 significantly delayed the formation of s.c. tumors from two distinct human cancer cell types in athymic mice. ANG is the likely target involved because (i) a 65828 analogue with much lower potency against the enzymatic activity of ANG failed to exert any antitumor effect, (ii) tumors from 65828-treated mice had fewer interior blood vessels than those from control mice, and (iii) 65828 appears to have no direct effect on the tumor cells. Our findings provide considerable support for the targeting of the enzymatic active site of ANG as a strategy for developing new anticancer drugs.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Anticarcinogenic Agents Pharmacology Naphthalenesulfonates Neoplasms Prevention & Control Neovascularization, Pathologic Ribonuclease, Pancreatic Antagonists & Inhibitors Amino Acid Substitution Animals Cell Line Drug Evaluation, Preclinical Genetic Variation Kinetics Mice Mice, Nude Molecular Structure Blood Recombinant Proteins Reproducibility Of Results Structure-Activity Relationship Transplantation, Heterologous Tumor Cells, Cultured Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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