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

Sorensen, OE; Gram, L; Johnsen, AH; Andersson, E; Bangsboll, S; Tjabringa, GS; Hiemstra, PS; Malm, Johan LU ; Egesten, A and Borregaard, N (2003) In Journal of Biological Chemistry 278(31). p.28540-28546
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
278
issue
31
pages
28540 - 28546
publisher
ASBMB
external identifiers
  • wos:000184421100026
  • scopus:0042208088
ISSN
1083-351X
DOI
10.1074/jbc.M301608200
language
English
LU publication?
yes
id
7b6c5083-ae00-4d19-863b-e493a5c92669 (old id 900077)
date added to LUP
2008-01-16 08:32:25
date last changed
2017-06-18 03:31:33
@article{7b6c5083-ae00-4d19-863b-e493a5c92669,
  abstract     = {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       = {Sorensen, OE and Gram, L and Johnsen, AH and Andersson, E and Bangsboll, S and Tjabringa, GS and Hiemstra, PS and Malm, Johan and Egesten, A and Borregaard, N},
  issn         = {1083-351X},
  language     = {eng},
  number       = {31},
  pages        = {28540--28546},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina},
  url          = {http://dx.doi.org/10.1074/jbc.M301608200},
  volume       = {278},
  year         = {2003},
}