Progesterone causes metabolic changes involving aminotransferases and creatine kinase in cryopreserved bovine spermatozoa.

Progesterone (P4) is capable of inducing acrosome reaction in many species. The objective of this study was to determine the activity of enzymes involved in metabolism that contribute to the redox state and supply energy for acrosome reaction in cryopreserved bull spermatozoa. To accomplish this aim, acrosome reaction was induced by P4 in capacitated and non-capacitated samples. Alanine and aspartate aminotransferases (ALT, AST) and creatine kinase (CK) activities were measured spectrophotometrically at 340 nm after acrosome reaction with P4. Oxygen consumption was measured polarographically. ALT and AST activities increased by the addition of P4 capacitated and non-capacitated samples. P4 addition provoked an increase in CK activity in non-capacitated spermatozoa compared to heparin capacitated spermatozoa with or without P4 addition. P4 increased oxygen consumption, the percentage of acrosome reacted spermatozoa as well as the absence of acrosome integrity in both capacitated and non-capacitated bovine spermatozoa, but oxygen consumption in P4 samples was significantly lower than in heparin capacitated spermatozoa (P<0.05). Acrosome reaction induction by P4 required different creatine kinase activity with the same oxygen consumption and transaminases level to maintain oxidative metabolism and redox state through reducing equivalents transfer between cytosolic and mitochondrial compartment. In conclusion, P4 induces a lower oxidative metabolism during acrosome reaction in bovine cryopreserved spermatozoa, compared to heparin induced capacitation process.