Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965287
- author
- Peter, A. ; Lilja, Hans LU ; Lundwall, Åke LU and Malm, Johan LU
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- 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)
- alternative location
- 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}}, }