This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Turner, T. T. Articles by Bazemore-Walker, C. R. Search for Related Content PubMed PubMed Citation Articles by Turner, T. T. Articles by Bazemore-Walker, C. R.

Testicular Torsion Alters the Presence of Specific Proteins in the Mouse Testis as Well as the Phosphorylation Status of Specific Proteins

TERRY T. TURNER^*,

JOHN D. SHANNON

CARTHENE R. BAZEMORE-WALKER

From the Departments of ^* Urology, Cell Biology, Microbiology, and Chemistry, University of Virginia, Charlottesville, Virginia.

Correspondence to: Dr Terry T. Turner, Department of Urology, University of Virginia School of Medicine, Charlottesville, VA 22908 (e-mail: ttt{at}virginia.edu).

Testicular torsion followed by torsion repair induces an ischemia-reperfusion injury to the testis that can render the testis aspermatogenic. Previous results have demonstrated this loss of spermatogenesis to be the result of germ cell apoptosis induced by oxidative stress. The present work reports protein changes occurring in the mouse testis 24 hours after repair of a testicular torsion known to induce germ cell apoptosis and severe seminiferous impairment. Total proteins were extracted from sham-operated testes and testes having had 2-hour 720° torsion 24 hours previously. Testicular proteins were separated by 2-dimensional electrophoresis and the resulting gel images were analyzed with image analysis software. Of the over 1100 proteins detected on the average gel, over 700 were consistently appearing in multiple gels, and those protein spot intensities were averaged within sham and torsion groups and compared between the 2 groups. Twenty-three proteins were consistently increased after torsion repair and 48 were decreased. Six proteins, 3 of which increased and 3 of which decreased after torsion repair, were identified by mass spectrometry. The 3 proteins that increased after torsion repair, ß2-tubulin and 2 isoforms of serum albumin, as well as the 3 proteins that decreased after torsion repair, vimentin, phosphoglycerate kinase, and t-complex protein 1ß, were for the most part associated with various aspects of cell stress responses. The number of proteins phosphorylated on tyrosine residues exceeded the number of proteins phosphorylated on serine/threonine residues, but among 6 stress-related proteins specifically examined for phosphorylation in sham testes and those examined after torsion repair, increases in threonine phosphorylation of c-Jun NH₂ terminal kinase and activating transcription factor 2 were the most prominent. Knowing these proteins and the pathways to which they point will aid in the search for new therapies of oxidative stress in the testis.

     Key words: Oxidative stress, testicular proteins