Participation of succinate dehydrogenase in capacitation and acrosome reaction in cryopreserved porcine spermatozoa

RODRIGUEZ PC; BREININGER E; PEREZ COLMAN M

Congreso; XVIII Jornadas Anuales Multidisciplinarias de la Sociedad Argentina de Biología; 2016

The aim of this study was to determine the activity of succinate dehydrogenase (SDH; 1.3.5.1) and evaluate its participation in capacitation and acrosome reaction (AR) in cryopreserved porcine spermatozoa. This enzyme is involved in the production of the energy required for these sperm metabolic processes and its activity was previously determined in fresh porcine sperm. The activity of SDH was determined spectrophotometrically at 600 nm, during 2 minutes, at 37°C. Enzyme unit (U) was defined as the amount of SDH that catalyzes the reduction of 1 μmol of DCPIP/min. Capacitation and AR were determined, in the presenceor absence of sodium malonate (competitive inhibitor of SDH; 1, 5 and 10 mM), by CTC technique and trypan blue combined with DIC, respectively. Sperm viability was evaluated by the eosin-nigrosin technique and motility was evaluated by optic microscopy, with a thermal stage. The results are expressed as means±SEM and were analysed by ANOVA and Bonferroni test. The activity of SDH was 0,7±0,1 U/1010 spermatozoa. The addition of the enzyme inhibitor (1mM) significantly (p