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Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase

Peter, A. ; Lilja, Hans LU orcid ; Lundwall, Åke LU and Malm, Johan LU (1998) In Eur J Biochem 252(2). p.21-216
Abstract
The major seminal vesicle secreted proteins in human semen, semenogelin I and semenogelin II, interact non-covalently and via disulphide bridges to instantly form a coagulum upon ejaculation. The coagulum is liquefied after a few minutes due to the action of a prostatic serine protease, prostate-specific antigen (PSA). In contrast to rat semen, which forms an insoluble plug within minutes of expulsion, no transglutaminase-mediated cross-linking has been demonstrated in ejaculated human semen. However, we here show that semenogelin I and semenogelin II, both in seminal vesicle fluid and purified from semen, are substrates for factor XIIIa, the fibrin cross-linking transglutaminase. The cross-linking of the semenogelins, which was... (More)
The major seminal vesicle secreted proteins in human semen, semenogelin I and semenogelin II, interact non-covalently and via disulphide bridges to instantly form a coagulum upon ejaculation. The coagulum is liquefied after a few minutes due to the action of a prostatic serine protease, prostate-specific antigen (PSA). In contrast to rat semen, which forms an insoluble plug within minutes of expulsion, no transglutaminase-mediated cross-linking has been demonstrated in ejaculated human semen. However, we here show that semenogelin I and semenogelin II, both in seminal vesicle fluid and purified from semen, are substrates for factor XIIIa, the fibrin cross-linking transglutaminase. The cross-linking of the semenogelins, which was conformation-dependent, and the incorporation of a fluorescence-labelled amine, were visualised by SDS/PAGE and Western blot. Purified semenogelin I and semenogelin II could be cross-linked separately into complexes. Moreover, digestion of semenogelin with PSA produced fragments, some of which were cross-linked into complexes by factor XIIIa. We also found that PSA was unable to release any semenogelin fragments during exposure of the high molecular-mass complexes of cross-linked semenogelin to active PSA. (Less)
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author
; ; and
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publishing date
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Contribution to journal
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published
subject
keywords
Non-U.S. Gov't, Research Support, Recombinant Proteins/metabolism, Prostate-Specific Antigen/metabolism, Peptide Fragments/metabolism, Male, Humans, Gonadal Steroid Hormones/*metabolism, Fluorescent Dyes/metabolism, Dithiothreitol/pharmacology, Disulfides/metabolism, Cross-Linking Reagents/metabolism, Cadaverine/analogs & derivatives/metabolism, Calcium/pharmacology, Semen/*chemistry, *Seminal Vesicle Secretory Proteins, Solubility, Substrate Specificity, Transglutaminases/*metabolism, Urea/pharmacology
in
Eur J Biochem
volume
252
issue
2
pages
21 - 216
publisher
Wiley-Blackwell
external identifiers
  • scopus:0032031582
language
English
LU publication?
yes
additional info
2
id
4289eee9-6ed0-4b81-8601-13fdc7152389 (old id 3965287)
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http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9523691
date added to LUP
2016-04-04 14:10:43
date last changed
2022-01-30 01:34:11
@article{4289eee9-6ed0-4b81-8601-13fdc7152389,
  abstract     = {{The major seminal vesicle secreted proteins in human semen, semenogelin I and semenogelin II, interact non-covalently and via disulphide bridges to instantly form a coagulum upon ejaculation. The coagulum is liquefied after a few minutes due to the action of a prostatic serine protease, prostate-specific antigen (PSA). In contrast to rat semen, which forms an insoluble plug within minutes of expulsion, no transglutaminase-mediated cross-linking has been demonstrated in ejaculated human semen. However, we here show that semenogelin I and semenogelin II, both in seminal vesicle fluid and purified from semen, are substrates for factor XIIIa, the fibrin cross-linking transglutaminase. The cross-linking of the semenogelins, which was conformation-dependent, and the incorporation of a fluorescence-labelled amine, were visualised by SDS/PAGE and Western blot. Purified semenogelin I and semenogelin II could be cross-linked separately into complexes. Moreover, digestion of semenogelin with PSA produced fragments, some of which were cross-linked into complexes by factor XIIIa. We also found that PSA was unable to release any semenogelin fragments during exposure of the high molecular-mass complexes of cross-linked semenogelin to active PSA.}},
  author       = {{Peter, A. and Lilja, Hans and Lundwall, Åke and Malm, Johan}},
  keywords     = {{Non-U.S. Gov't; Research Support; Recombinant Proteins/metabolism; Prostate-Specific Antigen/metabolism; Peptide Fragments/metabolism; Male; Humans; Gonadal Steroid Hormones/*metabolism; Fluorescent Dyes/metabolism; Dithiothreitol/pharmacology; Disulfides/metabolism; Cross-Linking Reagents/metabolism; Cadaverine/analogs & derivatives/metabolism; Calcium/pharmacology; Semen/*chemistry; *Seminal Vesicle Secretory Proteins; Solubility; Substrate Specificity; Transglutaminases/*metabolism; Urea/pharmacology}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{21--216}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Eur J Biochem}},
  title        = {{Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase}},
  url          = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9523691}},
  volume       = {{252}},
  year         = {{1998}},
}