ISOCITRATE DEHYDROGENASE ACTIVITY AND TYROSINE KINASE INHIBITION IN HYALURONIC ACID AND HEPARIN CAPACITATION OF BULL SPERM

FERNÁNDEZ S; CÓRDOBA M

CABA

Jornada; V Jornadas Internacionales del INITRA; 2017

Facultad de Ciencias Veterinarias-UBA

Isocitrate dehydrogenase enzyme (IDH) catalyzes the conversion of isocitrate to alpha-ketoglutarate, generating NADH or NADPH coenzymes according to intracellular localization. These reduced coenzymes are necessary in metabolic pathways in the spermatozoa, a metabolically active cell. During sperm capacitation, required for the male gamete to acquire fertilizing capacity, intracellular signaling pathways mediated by tyrosine kinase have been identified. The aim of this study was to determine the activity of isocitrate dehydrogenase NAD+ and NADP+ coenzyme dependent in cryopreserved bovine spermatozoa capacitation and in the presence of a tyrosine kinase inhibitor. Hyaluronic acid and heparin were used as capacitation inductors and genistein as a tyrosine kinase inhibitor. IDH activity was determined by spectrophotometry at 340 nm. Capacitation was evaluated by the epifluorescent chlortetracycline technique and viability and membranes integrity by vital staining trypan blue with interferential differential contrast. Data were analyzed by ANOVA and Tukey´s test (P