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

FERNÁNDEZ SILVINA; CÓRDOBA M

ANIMAL REPRODUCTION SCIENCE

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2015 vol. 164 p. 90 - 96

0378-4320

Progesterone causes metabolic changes involvingaminotransferases and creatine kinase in cryopreserved bovine spermatozoaSilvina Fernández, Mariana Córdoba∗Cátedra de Química Biológica, Instituto de Investigación y Tecnología en Reproducción Animal, Facultad de Ciencias Veterinarias,Universidad de Buenos Aires, Av. Chorroarín 280 1427 Ciudad Autónoma de Buenos Aires, Argentina.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 340nm 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