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Secretory Leucocyte Protease Inhibitor in the Male Genital Tract : PSA‐Induced Proteolytic Processing in Human Semen and Tissue Localization

OHLSSON, KJELL ; BJARTELL, ANDERS LU and LILJA, HANS LU orcid (1995) In Journal of Andrology 16(1). p.64-74
Abstract

ABSTRACT: Secretory leucocyte protease inhibitor, SLPI, is a low‐molecular‐weight, acid‐stable protein present in the liquid part of fresh human ejaculate but not demonstrable in the gel structure. No fragmentation of SLPI occurred during gel dissolution, but a slow proteolytic cleavage of SLPI was seen on incubation of the liquified semen at 37°C. The same pattern of degradation products was seen after incubation of SLPI with prostatic secretion and also with purified prostate‐specific antigen, PSA. We could identify Arg 20‐Tyr 21 and Met 73‐Leu 74 to be the primary cleavage sites upon proteolytic modification of SLPI by purified PSA. However, we did not find any inhibition of the enzymatic activity of PSA by SLPI, even at a 100‐fold... (More)

ABSTRACT: Secretory leucocyte protease inhibitor, SLPI, is a low‐molecular‐weight, acid‐stable protein present in the liquid part of fresh human ejaculate but not demonstrable in the gel structure. No fragmentation of SLPI occurred during gel dissolution, but a slow proteolytic cleavage of SLPI was seen on incubation of the liquified semen at 37°C. The same pattern of degradation products was seen after incubation of SLPI with prostatic secretion and also with purified prostate‐specific antigen, PSA. We could identify Arg 20‐Tyr 21 and Met 73‐Leu 74 to be the primary cleavage sites upon proteolytic modification of SLPI by purified PSA. However, we did not find any inhibition of the enzymatic activity of PSA by SLPI, even at a 100‐fold molar excess of the inhibitor. The slow degradation of SLPI facilitated sampling and the reliable determination of the normal level of SLPI in seminal plasma, which was about 20 mg/L. We investigated the glandular origion of SLPI in the genital tract by immunocytochemistry. A strong immunostaining for SLPI was demonstrated in epithelial cells within the glandular lumina of the prostate gland, seminal vesicles, and epididymis but not in the stromal parts of these glands. In addition the immunostaining was also detected in the deferent ducts and the germinal epithelium of the testes. Taking into account that SLPI is a strong inhibitor of several proteases, including leukocyte elastase and cathepsin G, the results suggest that SLPI has a local protective function against proteolytic degradation of the male reproductive tract tissues during inflammation. 1995 American Society of Andrology

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
prostate, Protease inhibitors, proteolytic enzymes, semen, seminal vesicles
in
Journal of Andrology
volume
16
issue
1
pages
64 - 74
publisher
American Society of Andrology
external identifiers
  • pmid:7539415
  • scopus:0028914791
ISSN
0196-3635
language
English
LU publication?
yes
id
aaf481f5-f81a-445b-a1ce-9762b2d64ef7
alternative location
https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.1939-4640.1995.tb01733.x
date added to LUP
2022-12-06 17:09:41
date last changed
2024-01-03 19:32:28
@article{aaf481f5-f81a-445b-a1ce-9762b2d64ef7,
  abstract     = {{<p>ABSTRACT:  Secretory leucocyte protease inhibitor, SLPI, is a low‐molecular‐weight, acid‐stable protein present in the liquid part of fresh human ejaculate but not demonstrable in the gel structure. No fragmentation of SLPI occurred during gel dissolution, but a slow proteolytic cleavage of SLPI was seen on incubation of the liquified semen at 37°C. The same pattern of degradation products was seen after incubation of SLPI with prostatic secretion and also with purified prostate‐specific antigen, PSA. We could identify Arg 20‐Tyr 21 and Met 73‐Leu 74 to be the primary cleavage sites upon proteolytic modification of SLPI by purified PSA. However, we did not find any inhibition of the enzymatic activity of PSA by SLPI, even at a 100‐fold molar excess of the inhibitor. The slow degradation of SLPI facilitated sampling and the reliable determination of the normal level of SLPI in seminal plasma, which was about 20 mg/L. We investigated the glandular origion of SLPI in the genital tract by immunocytochemistry. A strong immunostaining for SLPI was demonstrated in epithelial cells within the glandular lumina of the prostate gland, seminal vesicles, and epididymis but not in the stromal parts of these glands. In addition the immunostaining was also detected in the deferent ducts and the germinal epithelium of the testes. Taking into account that SLPI is a strong inhibitor of several proteases, including leukocyte elastase and cathepsin G, the results suggest that SLPI has a local protective function against proteolytic degradation of the male reproductive tract tissues during inflammation. 1995 American Society of Andrology</p>}},
  author       = {{OHLSSON, KJELL and BJARTELL, ANDERS and LILJA, HANS}},
  issn         = {{0196-3635}},
  keywords     = {{prostate; Protease inhibitors; proteolytic enzymes; semen; seminal vesicles}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{64--74}},
  publisher    = {{American Society of Andrology}},
  series       = {{Journal of Andrology}},
  title        = {{Secretory Leucocyte Protease Inhibitor in the Male Genital Tract : PSA‐Induced Proteolytic Processing in Human Semen and Tissue Localization}},
  url          = {{https://onlinelibrary.wiley.com/doi/pdf/10.1002/j.1939-4640.1995.tb01733.x}},
  volume       = {{16}},
  year         = {{1995}},
}