Proteome analysis of testis from infertile protein C inhibitor‐deficient mice reveals novel changes in serpin processing and prostaglandin metabolism. Issue 21 (20th October 2015)

• Record Type: Journal Article
• Authors: Yang, Hanjiang; Wahlmüller, Felix Christof; Uhrin, Pavel; Baumgartner, Roland; Mitulovic, Goran; Sarg, Bettina; Geiger, Margarethe; Zellner, Maria
• Is Part Of: Electrophoresis. Volume 36:Issue 21/22(2015)
• Page Start: 2837
• Page End: 2840
• Publication Date: 2015-10-20
• Subjects: 2D differential gel electrophoresis -- Drug‐target validation -- Infertility -- Prostag‐landin reductase 1 -- Serpin; Electrophoresis -- Periodicals; Electrophoresis -- Periodicals; 541.372
• DOI: 10.1002/elps.201500218
• Languages: English
• ISSNs: 0173-0835

Abstract

Abstract : Serine protease inhibitors (serpin) have therapeutic potential in a variety of pathogenic processes, ranging from thrombosis and altered immune response to liver cirrhosis. To investigate the physiological effects of protein C inhibitor (PCI, serpinA5), its gene was inactivated in a mouse model, resulting in male infertility. In the present report, 2D differential gel electrophoresis was utilized to investigate the molecular mechanisms for PCI involvement in male reproduction. Comparing the testes proteomes of three PCI‐knockout mice with three wild types demonstrated similar patterns with the exception of a massive upregulation of prostaglandin reductase 1 (tenfold; p < 0.002) and the complete shifts in the molecular weights of serpinA1C and serpinA3K. All these PCI‐dependent proteome changes were immunologically verified. Unbiased proteome analysis indicated that inactivation of serpinA5 strongly influenced both the protein species pattern of other A‐clade serpins as well as prostaglandin metabolism in the testes.