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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 ; 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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@misc{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},
  keyword      = {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},
  series       = {Eur J Biochem},
  title        = {Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase},
  volume       = {252},
  year         = {1998},
}