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Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo.

Abstract
The anthrax toxin protective antigen precursor is activated by proteolytic cleavage by furin or a furin-like protease. We present here data demonstrating that the small stable furin inhibitor hexa-D-arginine amide delays anthrax toxin-induced toxemia both in cells and in live animals, suggesting that furin inhibition may represent a reasonable avenue for therapeutic intervention in anthrax.
AuthorsMiroslav S Sarac, Juan R Peinado, Stephen H Leppla, Iris Lindberg
JournalInfection and immunity (Infect Immun) Vol. 72 Issue 1 Pg. 602-5 (Jan 2004) ISSN: 0019-9567 [Print] United States
PMID14688144 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Antigens, Bacterial
  • Bacterial Toxins
  • Enzyme Inhibitors
  • Peptides
  • anthrax toxin
  • polyarginine
  • Furin
Topics
  • Animals
  • Anthrax (prevention & control)
  • Antigens, Bacterial
  • Bacterial Toxins (toxicity)
  • Cell Line
  • Enzyme Inhibitors (administration & dosage)
  • Furin (antagonists & inhibitors)
  • Macrophages, Alveolar (pathology)
  • Male
  • Peptides (administration & dosage)
  • Rats
  • Rats, Inbred F344
  • Toxemia (prevention & control)

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