Journal of Andrology
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Published-Ahead-of-Print April 1, 2006, DOI:10.2164/jandrol.05188

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

Magnus Jonsson , Ake Lundwall , Sara Linse , Birgitta Frohm , and Johan Malm

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 (II) 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 (i.e. a stoichiometry of at least 9-10 mol per mol of protein and an average dissociation constant of 5 µM 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.






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Copyright © 2006 by The American Society of Andrology.