Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Truncated semenogelin I binds zinc and is cleaved by prostate-specific antigen

Jonsson, Magnus LU orcid ; Lundwall, Åke LU ; Linse, Sara LU ; Frohm, Birgitta LU and Malm, Johan LU (2006) In Journal of Andrology 27(4). p.542-547
Abstract
Semenogelins I and II are major coagulum-forming proteins in semen, and they are secreted mainly by the seminal vesicles. These proteins bind Zn2+ and act as substrates for prostate-specific antigen and transglutaminase. A variant semenogelin I lacking 60 amino acids has been described that occurs in different populations with an allele frequency of 1%-3%. To better understand the function of the semenogelins in vivo, our aim was to characterize the properties of the variant form and compare with the wild type. Recombinant proteins were synthesized in insect cells, Binding of Zn2+ was studied by titration of metal ions in the presence of a zinc (11) fluorophore chelator. SDS-PAGE was used to visualize the results of cleavage by... (More)
Semenogelins I and II are major coagulum-forming proteins in semen, and they are secreted mainly by the seminal vesicles. These proteins bind Zn2+ and act as substrates for prostate-specific antigen and transglutaminase. A variant semenogelin I lacking 60 amino acids has been described that occurs in different populations with an allele frequency of 1%-3%. To better understand the function of the semenogelins in vivo, our aim was to characterize the properties of the variant form and compare with the wild type. Recombinant proteins were synthesized in insect cells, Binding of Zn2+ was studied by titration of metal ions in the presence of a zinc (11) fluorophore chelator. SDS-PAGE was used to visualize the results of cleavage by prostate-specific antigen and cross-linking with transglutaminase. We found that the truncated and wild-type semenogelin molecules had similar Zn2+-binding properties (ie, a stoichiometry of at least 9-10 mol per mol of protein and an average dissociation constant of 5 mu mol/L per site), and they showed also similar susceptibility for degradation by prostate-specific antigen. Furthermore, like the wild-type form, the truncated semenogelin I was able to serve as a substrate for transglutaminase. These findings imply that the studied characteristics do not depend on a well-defined tertiary structure, or that the deletion has no major effect on the structure responsible for these features. (Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
reproduction, variant, transglutaminase, prostate-specific antigen, semen, fertility
in
Journal of Andrology
volume
27
issue
4
pages
542 - 547
publisher
American Society of Andrology
external identifiers
  • wos:000239401900010
  • scopus:33746414284
ISSN
0196-3635
DOI
10.2164/jandrol.05188
language
English
LU publication?
yes
id
c63ffb00-8f38-44ca-bb70-cfc7f32b9716 (old id 399129)
date added to LUP
2016-04-01 16:18:48
date last changed
2021-02-17 04:04:43
@article{c63ffb00-8f38-44ca-bb70-cfc7f32b9716,
  abstract     = {Semenogelins I and II are major coagulum-forming proteins in semen, and they are secreted mainly by the seminal vesicles. These proteins bind Zn2+ and act as substrates for prostate-specific antigen and transglutaminase. A variant semenogelin I lacking 60 amino acids has been described that occurs in different populations with an allele frequency of 1%-3%. To better understand the function of the semenogelins in vivo, our aim was to characterize the properties of the variant form and compare with the wild type. Recombinant proteins were synthesized in insect cells, Binding of Zn2+ was studied by titration of metal ions in the presence of a zinc (11) fluorophore chelator. SDS-PAGE was used to visualize the results of cleavage by prostate-specific antigen and cross-linking with transglutaminase. We found that the truncated and wild-type semenogelin molecules had similar Zn2+-binding properties (ie, a stoichiometry of at least 9-10 mol per mol of protein and an average dissociation constant of 5 mu mol/L per site), and they showed also similar susceptibility for degradation by prostate-specific antigen. Furthermore, like the wild-type form, the truncated semenogelin I was able to serve as a substrate for transglutaminase. These findings imply that the studied characteristics do not depend on a well-defined tertiary structure, or that the deletion has no major effect on the structure responsible for these features.},
  author       = {Jonsson, Magnus and Lundwall, Åke and Linse, Sara and Frohm, Birgitta and Malm, Johan},
  issn         = {0196-3635},
  language     = {eng},
  number       = {4},
  pages        = {542--547},
  publisher    = {American Society of Andrology},
  series       = {Journal of Andrology},
  title        = {Truncated semenogelin I binds zinc and is cleaved by prostate-specific antigen},
  url          = {http://dx.doi.org/10.2164/jandrol.05188},
  doi          = {10.2164/jandrol.05188},
  volume       = {27},
  year         = {2006},
}