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

Författare

Summary, in English

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.

Publiceringsår

2005

Språk

Engelska

Sidor

447-453

Publikation/Tidskrift/Serie

Biochemical Journal

Volym

387

Issue

Part 2

Dokumenttyp

Artikel i tidskrift

Förlag

Portland Press

Ämne

  • Biochemistry and Molecular Biology

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 0264-6021