International journal of fertility and menopausal studies · 1994
Arrest of rat embryonic development by the inhibition of gamma-glutamyl transpeptidase. I. Intrauterine administration of L-serine-borate complex.
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Díaz-Flores M, Duran-Reyes G, Hicks J J
Аннотация
OBJECTIVE: The purpose of this study was to investigate the activity of gamma-glutamyl transpeptidase (gamma-GTP, E.C. 2.3.2.2) in rat endometrium (day 5 of pregnancy). Since gamma-GTP is an enzyme involved in the translocation of amino acids from fluids toward tissues, these substrates are necessary for anabolic processes.
METHODS AND RESULTS: The presence of statistically higher activity of gamma-GTP in rat (Sprague-Dawley) implantation sites (1.06 nmol/mg protein/min) than in nondecidualized (0.87 nmol/mg protein/min) tissues was demonstrated. The intrauterine administration of L-serine-borate complex (5 mM) during day 5 of pregnancy arrested 91.6% of rat embryonic development (day 18). This inhibitory effect was not present when borate or L-serine was administered separately. The L-serine-borate complex also inhibited (by 88%) the gamma-GTP in vitro.
CONCLUSION: The inhibition of gamma-GTP by L-serine-borate complex might be considered as a new approach to the arrest of biological processes in differentiation or development.
METHODS AND RESULTS: The presence of statistically higher activity of gamma-GTP in rat (Sprague-Dawley) implantation sites (1.06 nmol/mg protein/min) than in nondecidualized (0.87 nmol/mg protein/min) tissues was demonstrated. The intrauterine administration of L-serine-borate complex (5 mM) during day 5 of pregnancy arrested 91.6% of rat embryonic development (day 18). This inhibitory effect was not present when borate or L-serine was administered separately. The L-serine-borate complex also inhibited (by 88%) the gamma-GTP in vitro.
CONCLUSION: The inhibition of gamma-GTP by L-serine-borate complex might be considered as a new approach to the arrest of biological processes in differentiation or development.