Document 0800
 DOCN  M9470800
 TI    RNase inhibition of human immunodeficiency virus infection of H9 cells.
 DT    9409
 AU    Youle RJ; Wu YN; Mikulski SM; Shogen K; Hamilton RS; Newton D; D'Alessio
       G; Gravell M; Biochemistry Section, Surgical Neurology Branch, National;
       Institute of Neurological Disorders and Stroke, National; Institutes of
       Health, Bethesda, MD 20892.
 SO    Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):6012-6. Unique Identifier :
       AIDSLINE MED/94286568
 AB    Onconase and bovine seminal RNase, two members of the RNase A
       superfamily, inhibit human immunodeficiency virus type 1 replication in
       H9 leukemia cells 90-99.9% over a 4-day incubation at concentrations not
       toxic to uninfected H9 cells. Two other members of the same protein
       family, bovine pancreatic RNase A and human eosinophil-derived
       neurotoxin, have no detectable antiviral activity, demonstrating a
       strikingly selective antiviral activity among homologous ribonucleases.
       The antiviral RNases do not appear to affect viral particles directly
       but inhibit replication in host cell cultures. Onconase, already in
       clinical trials for cancer therapy, and bovine seminal RNase have
       potential as antiviral therapeutics.
 DE    Animal  Antineoplastic Agents/TOXICITY  Antiviral Agents/*TOXICITY
       Cattle  Cell Line  Cell Survival/DRUG EFFECTS  Dose-Response
       Relationship, Drug  Egg Proteins/*TOXICITY  Human  HIV-1/DRUG
       EFFECTS/*PHYSIOLOGY  Kinetics  Leukemia  Male  Ribonuclease,
       Pancreatic/*TOXICITY  Ribonucleases/*TOXICITY  Semen/ENZYMOLOGY  Time
       Factors  Tumor Cells, Cultured  Virus Replication/*DRUG EFFECTS  JOURNAL
       ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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