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

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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; Egesten, A; Borregaard, N.

In: Journal of Biological Chemistry, Vol. 278, No. 31, 2003, p. 28540-28546.

Research output: Contribution to journalArticle

Harvard

Sorensen, OE, Gram, L, Johnsen, AH, Andersson, E, Bangsboll, S, Tjabringa, GS, Hiemstra, PS, Malm, J, Egesten, A & Borregaard, N 2003, 'Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina', Journal of Biological Chemistry, vol. 278, no. 31, pp. 28540-28546. https://doi.org/10.1074/jbc.M301608200

APA

Sorensen, OE., Gram, L., Johnsen, AH., Andersson, E., Bangsboll, S., Tjabringa, GS., Hiemstra, PS., Malm, J., Egesten, A., & Borregaard, N. (2003). Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina. Journal of Biological Chemistry, 278(31), 28540-28546. https://doi.org/10.1074/jbc.M301608200

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MLA

Vancouver

Author

Sorensen, OE ; Gram, L ; Johnsen, AH ; Andersson, E ; Bangsboll, S ; Tjabringa, GS ; Hiemstra, PS ; Malm, Johan ; Egesten, A ; Borregaard, N. / Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 31. pp. 28540-28546.

RIS

TY - JOUR

T1 - Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina

AU - Sorensen, OE

AU - Gram, L

AU - Johnsen, AH

AU - Andersson, E

AU - Bangsboll, S

AU - Tjabringa, GS

AU - Hiemstra, PS

AU - Malm, Johan

AU - Egesten, A

AU - Borregaard, N

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

UR - http://www.jbc.org/content/281/18/12999.short

U2 - 10.1074/jbc.M301608200

DO - 10.1074/jbc.M301608200

M3 - Article

C2 - 12759353

VL - 278

SP - 28540

EP - 28546

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 31

ER -