Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen
(2005) In Biochemical Journal 387(Part 2). p.447-453- Abstract
- In semen. the gel proteins SgI and SgII (semenogelins I and II) are digested by PSA (prostate-specific antigen), resulting in liquefaction and release of motile spermatozoa. Semen contains a high concentration of Zn2+, which is known to inhibit the protease activity of PSA. We characterized the binding of Zn2+ to SgI and SgII and found evidence that these proteins are involved in regulating the activity of PSA. Intact SgI and SgII and synthetic semenogelin peptides were used in the experiments. Binding of Zn2+ was studied by radioligand blotting, titration with a zinc (II) fluorophore chelator and NMR analysis. A chromogenic substrate was used to measure the enzymatic activity of PSA. SgI and SgII bound Zn2+ with a stoichiometry of at... (More)
- In semen. the gel proteins SgI and SgII (semenogelins I and II) are digested by PSA (prostate-specific antigen), resulting in liquefaction and release of motile spermatozoa. Semen contains a high concentration of Zn2+, which is known to inhibit the protease activity of PSA. We characterized the binding of Zn2+ to SgI and SgII and found evidence that these proteins are involved in regulating the activity of PSA. Intact SgI and SgII and synthetic semenogelin peptides were used in the experiments. Binding of Zn2+ was studied by radioligand blotting, titration with a zinc (II) fluorophore chelator and NMR analysis. A chromogenic substrate was used to measure the enzymatic activity of PSA. SgI and SgII bound Zn2+ with a stoichiometry of at least 10 cool (mol of protein)(-1) and with an average dissociation constant of approx. 5 mu M per site. Moreover, Zn2+-inhibited PSA was activated by exposure to SgI or SgII. Since both proteins have high affinity for Zn2+ and are the dominating proteins in semen, they probably represent the major Zn2+ binders in semen, one function of which may be to regulate the activity of PSA. The system is self-regulating, and PSA is maintained in an active state by its substrate. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/151515
- author
- Jonsson, Magnus LU ; Linse, Sara LU ; Frohm, Birgitta LU ; Lundwall, Åke LU and Malm, Johan LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical Journal
- volume
- 387
- issue
- Part 2
- pages
- 447 - 453
- publisher
- Portland Press
- external identifiers
-
- wos:000228699200018
- pmid:15563730
- scopus:17644419655
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20041424
- language
- English
- LU publication?
- yes
- id
- cef50128-7d98-49c0-99f1-959ba3588ba9 (old id 151515)
- date added to LUP
- 2016-04-01 16:18:18
- date last changed
- 2022-01-28 18:44:54
@article{cef50128-7d98-49c0-99f1-959ba3588ba9, abstract = {{In semen. the gel proteins SgI and SgII (semenogelins I and II) are digested by PSA (prostate-specific antigen), resulting in liquefaction and release of motile spermatozoa. Semen contains a high concentration of Zn2+, which is known to inhibit the protease activity of PSA. We characterized the binding of Zn2+ to SgI and SgII and found evidence that these proteins are involved in regulating the activity of PSA. Intact SgI and SgII and synthetic semenogelin peptides were used in the experiments. Binding of Zn2+ was studied by radioligand blotting, titration with a zinc (II) fluorophore chelator and NMR analysis. A chromogenic substrate was used to measure the enzymatic activity of PSA. SgI and SgII bound Zn2+ with a stoichiometry of at least 10 cool (mol of protein)(-1) and with an average dissociation constant of approx. 5 mu M per site. Moreover, Zn2+-inhibited PSA was activated by exposure to SgI or SgII. Since both proteins have high affinity for Zn2+ and are the dominating proteins in semen, they probably represent the major Zn2+ binders in semen, one function of which may be to regulate the activity of PSA. The system is self-regulating, and PSA is maintained in an active state by its substrate.}}, author = {{Jonsson, Magnus and Linse, Sara and Frohm, Birgitta and Lundwall, Åke and Malm, Johan}}, issn = {{0264-6021}}, language = {{eng}}, number = {{Part 2}}, pages = {{447--453}}, publisher = {{Portland Press}}, series = {{Biochemical Journal}}, title = {{Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen}}, url = {{http://dx.doi.org/10.1042/BJ20041424}}, doi = {{10.1042/BJ20041424}}, volume = {{387}}, year = {{2005}}, }