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An anti-endotoxin peptide that generates from the amino-terminal domain of complement regulatory protein C1 inhibitor.
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2007 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 359, no 2, 285-91 p.Article in journal (Refereed) Published
Abstract [en]

C1 inhibitor (C1INH), a complement regulatory protein, prevents endotoxin shock via a direct interaction of the amino-terminal domain with gram-negative bacterial lipopolysaccharide (LPS). Importantly, the cleaved, inactive C1INH still is an anti-endotoxin effector indicating the anti-endotoxin peptide that generates from the amino-terminal domain of C1INH. In this study, we first identified that a cleaved fragment within the major part of the amino-terminal domain in in vitro proteolytic analysis of C1INH had an ability to bind to LPS. We synthesized several peptides overlapping the C1INH cleaved fragment. Among these synthetic peptides, a 13-mer derivative peptide at position from 18 to 30, named N2((18-30)), exhibited the most powerful anti-endotoxin activity in vitro, enlightening that it was most strong at binding to LPS, inhibiting the interaction of LPS with LPS-binding protein (LBP), blocking LPS binding to CD14(+) cells, and suppressing production of tumor necrosis factor (TNF)-alpha by murine macrophages, RAW 264.7. In the murine endotoxin shock model, the peptide N2((18-30)) protected mice from LPS-induced lethal septic shock by inhibiting macrophage activation. These data indicate that the peptide N2((18-30)) derived from the amino-terminal region of C1INH is anti-endotoxin.

Place, publisher, year, edition, pages
2007. Vol. 359, no 2, 285-91 p.
Identifiers
URN: urn:nbn:se:umu:diva-41172DOI: 10.1016/j.bbrc.2007.05.078PubMedID: 17543887OAI: oai:DiVA.org:umu-41172DiVA: diva2:404841
Available from: 2011-03-18 Created: 2011-03-18 Last updated: 2017-12-11

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  • apa
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  • de-DE
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  • en-US
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  • nn-NO
  • nn-NB
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  • Other locale
More languages
Output format
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  • asciidoc
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