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  • Open Access

    ARTICLE

    A 66-kDa protein of bovine hypophyseal Pars tuberalis induces luteinizing hormone release from rat Pars distalis

    MARTHA LAFARQUE, LILIANA OLIVEROS

    BIOCELL, Vol.32, No.3, pp. 211-218, 2008, DOI:10.32604/biocell.2008.32.211

    Abstract In this study, evidence for a factor secreted by bovine hypophyseal pars tuberalis that stimulates luteinizing hormone (LH) release from rat pars distalis cells is shown. The secretion products of bovine pars tuberalis cells into the culture medium were assayed on dispersed rat pars distalis cells in 30 min incubations and superfusion experiments. The culture medium from pars tuberalis total cell populations, added at a dose of 6 μg per tube, induced the greater LH release from pars distalis cells, without effect on follicle stimulating hormone (FSH) release. After pars tuberalis cells separation on a discontinuos Percoll gradient, only the culture medium… More >

  • Open Access

    ARTICLE

    Brief Note: Reactive oxygen species in bovine embryo in vitro production

    G.C. DALVIT, P.D. CETICA, L.N. PINTOS, M.T. BECONI

    BIOCELL, Vol.29, No.2, pp. 209-212, 2005, DOI:10.32604/biocell.2005.29.209

    Abstract Oxidative modifications of cell components due to the action of reactive oxygen species (ROS) is one of the most potentially damaging processes for proper cell function. However, in the last few years it has been observed that ROS participate in physiological processes. The aim of this work was to determine ROS generation during in vitro production of bovine embryos. Cumulus-oocyte complexes were recovered by aspiration of antral follicles from ovaries obtained from slaughtered cows and cultured in medium 199 for 22 h at 39ºC in 5% CO2: 95% humidified air. In vitro fertilization was carried out in… More >

  • Open Access

    ARTICLE

    Brief Note : Proacrosin-acrosin activity in capacitated and acrosome reacted sperm from cryopreserved bovine semen

    M. I. ROSATTI, M. T. BECONI, M. CÓRDOBA

    BIOCELL, Vol.28, No.3, pp. 311-316, 2004, DOI:10.32604/biocell.2004.28.311

    Abstract Acrosin activity is associated with normal fertility in human and bovine spermatozoa. The aim of the study was to determine the variation of the enzyme activity in the proacrosin-acrosin system in capacitated and acrosome reacted cryopreserved bovine sperm. Enzyme activity was assessed spectrophotometrically using N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) as specific substrate for acrosin at pH 8. Capacitation with heparin and quercitin failed to induce conversion of proacrosin to acrosin. An increase in acrosin activity produced by the presence of progesterone, in a dose-dependent manner, was related with the induction of true acrosome reaction. The total level More >

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