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Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen

Jonsson, Magnus LU ; Linse, Sara LU ; Frohm, Birgitta LU ; Lundwall, Åke LU and Malm, Johan LU (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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical Journal
volume
387
issue
Part 2
pages
447 - 453
publisher
Portland Press Limited
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
2007-06-29 11:40:16
date last changed
2017-10-01 04:43:30
@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 Limited},
  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},
  volume       = {387},
  year         = {2005},
}