The Synthetic Antimicrobial Peptide 19-2.5 Interacts With Heparanase and Heparan Sulfate in Murine Sepsis In Vivo and in Human Sepsis Ex Vivo

نویسندگان

  • L Martin
  • S Doemming
  • A Humbs
  • L Heinbockel
  • K Brandenburg
  • G Marx
  • T Schürholz
چکیده

Introduction Heparanase is an endo-b-glucuronidase that cleaves highly potent heparan sulfate (HS) from its proteoglycan, thereby triggering the inflammatory response in [1]. Thus, new anti-infective agents that interact with heparanase may be promising tools for sepsis therapy. As a novel anti-infective agent, peptide 19-2.5 (pep2.5) belongs to the class of synthetic anti-lipopolysaccharide peptides, however its activity is not restricted to Gramnegative bacterial infection [2,3].

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The Synthetic Antimicrobial Peptide 19-2.5 Interacts with Heparanase and Heparan Sulfate in Murine and Human Sepsis.

Heparanase is an endo-β-glucuronidase that cleaves heparan sulfate side chains from their proteoglycans. Thereby, heparanase liberates highly potent circulating heparan sulfate-fragments (HS-fragments) and triggers the fatal and excessive inflammatory response in sepsis. As a potential anti-inflammatory agent for sepsis therapy, peptide 19-2.5 belongs to the class of synthetic anti-lipopolysacc...

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عنوان ژورنال:

دوره 3  شماره 

صفحات  -

تاریخ انتشار 2015