Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina.

نویسندگان

  • Ole E Sørensen
  • Lone Gram
  • Anders H Johnsen
  • Emma Andersson
  • Susanne Bangsbøll
  • G Sandra Tjabringa
  • Pieter S Hiemstra
  • Johan Malm
  • Arne Egesten
  • Niels Borregaard
چکیده

The human cathelicidin, hCAP-18, is expressed both in neutrophils and in epithelial cells. hCAP-18 is processed to the antimicrobial peptide LL-37 by proteinase 3 in neutrophils. hCAP-18 is highly expressed in the epididymis with a subsequent high concentration in seminal plasma where the protein is present in its unprocessed and antimicrobially inactive form. We report here that hCAP-18 in seminal plasma is processed to generate a 38-amino acid antimicrobial peptide ALL-38 by the prostate-derived protease gastricsin when incubated at a pH corresponding to the vaginal pH. In accordance with this, seminal plasma derived hCAP-18 was found in its processed form in the vagina following sexual intercourse. The antimicrobial activity of ALL-38 against a variety of microorganisms tested is equal to that of LL-37. This enzymatic activation of a proantimicrobial substance in seminal plasma following exposure to the vaginal milieu represents a novel mechanism to prevent infection following sexual intercourse.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 278 31  شماره 

صفحات  -

تاریخ انتشار 2003