Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/900077
- author
- Sorensen, OE LU ; Gram, L ; Johnsen, AH ; Andersson, E ; Bangsboll, S ; Tjabringa, GS ; Hiemstra, PS ; Malm, Johan LU ; Egesten, A and Borregaard, N
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 278
- issue
- 31
- pages
- 28540 - 28546
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000184421100026
- scopus:0042208088
- pmid:12759353
- 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
- 2016-04-01 11:40:10
- date last changed
- 2022-04-12 23:24:29
@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 = {{American Society for Biochemistry and Molecular Biology}}, 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}}, doi = {{10.1074/jbc.M301608200}}, volume = {{278}}, year = {{2003}}, }