Truncated semenogelin I binds zinc and is cleaved by prostate-specific antigen
Jonsson, Magnus LU
; 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:
https://lup.lub.lu.se/record/399129
- author
- Jonsson, Magnus
LU
; Lundwall, Åke
LU
; Linse, Sara
LU
; Frohm, Birgitta
LU
and Malm, Johan
LU
- organization
- publishing date
- 2006
- 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
- 2022-01-28 18:50:24
@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}},
keywords = {{reproduction; variant; transglutaminase; prostate-specific antigen; semen; fertility}},
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}},
}