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

Summary, in English

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 LL37. 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.

• Author: OE Sorensen; L Gram; AH Johnsen; E Andersson; S Bangsboll; GS Tjabringa; PS Hiemstra; Johan Malm; A Egesten; N Borregaard
• Department/s: Clinical Chemistry, Malmö
• Publishing year: 2003
• Language: English
• Pages: 28540-28546
• Publication/Series: Journal of Biological Chemistry
• Volume: 278
• Issue: 31
• Links: http://dx.doi.org/10.1074/jbc.M301608200
• Document type: Journal article
• Publisher: American Society for Biochemistry and Molecular Biology
• Topic: Medicinal Chemistry
• Status: Published
• Research group: Clinical Chemistry, Malmö
• ISBN/ISSN/Other: ISSN: 1083-351X