OBJECTIVE: The aim of this investigation is to determine whether 17alpha-hydroxyprogesterone caproate is hydrolyzed, in vitro, to 17alpha-hydroxyprogesterone and caproate. STUDY DESIGN: The in vitro hydrolysis of dual radioactively labeled 17alpha-hydroxy-[3H] progesterone [14C] caproate by human plasma, hepatic and placental S9 fractions as well as recombinant esterases was investigated. The formation of [3H]-17alpha-hydroxyprogesterone and [14C]-caproate were determined with the use of high-performance liquid chromatography equipped with an online radioactivity detector. The presence and activity of carboxylesterase and butyrylcholinesterase in the human-derived preparations was confirmed by the hydrolysis of their prototypic substrates p-nitrophenyl acetate, p-nitrophenyl butyrate, and butyrylthiocholine, respectively. RESULTS: The aforementioned human-derived preparations hydrolyzed p-nitrophenyl acetate, p-nitrophenyl butyrate, and butyrylthiocholine. However, when 17alpha-hydroxyprogesterone caproate was incubated with the human-derived preparations under identical experimental conditions neither [3H]-17alpha-hydroxyprogesterone nor [14C]-caproate was detected. CONCLUSION: 17Alpha-hydroxyprogesterone caproate is not hydrolyzed in vitro by the esterase enzymes present in human plasma, liver, preterm, or term placenta.
OBJECTIVE: The aim of this investigation is to determine whether 17alpha-hydroxyprogesterone caproate is hydrolyzed, in vitro, to 17alpha-hydroxyprogesterone and caproate. STUDY DESIGN: The in vitro hydrolysis of dual radioactively labeled 17alpha-hydroxy-[3H] progesterone [14C] caproate by human plasma, hepatic and placental S9 fractions as well as recombinant esterases was investigated. The formation of [3H]-17alpha-hydroxyprogesterone and [14C]-caproate were determined with the use of high-performance liquid chromatography equipped with an online radioactivity detector. The presence and activity of carboxylesterase and butyrylcholinesterase in the human-derived preparations was confirmed by the hydrolysis of their prototypic substrates p-nitrophenyl acetate, p-nitrophenyl butyrate, and butyrylthiocholine, respectively. RESULTS: The aforementioned human-derived preparations hydrolyzed p-nitrophenyl acetate, p-nitrophenyl butyrate, and butyrylthiocholine. However, when 17alpha-hydroxyprogesterone caproate was incubated with the human-derived preparations under identical experimental conditions neither [3H]-17alpha-hydroxyprogesterone nor [14C]-caproate was detected. CONCLUSION:17Alpha-hydroxyprogesterone caproate is not hydrolyzed in vitro by the esterase enzymes present in human plasma, liver, preterm, or term placenta.
Authors: Paul J Meis; Mark Klebanoff; Elizabeth Thom; Mitchell P Dombrowski; Baha Sibai; Atef H Moawad; Catherine Y Spong; John C Hauth; Menachem Miodovnik; Michael W Varner; Kenneth J Leveno; Steve N Caritis; Jay D Iams; Ronald J Wapner; Deborah Conway; Mary J O'Sullivan; Marshall Carpenter; Brian Mercer; Susan M Ramin; John M Thorp; Alan M Peaceman; Steven Gabbe Journal: N Engl J Med Date: 2003-06-12 Impact factor: 91.245
Authors: Valentina M Fokina; Olga L Zharikova; Gary D V Hankins; Mahmoud S Ahmed; Tatiana N Nanovskaya Journal: Reprod Sci Date: 2011-12-02 Impact factor: 3.060
Authors: Sarah J Hemauer; Ru Yan; Svetlana L Patrikeeva; Donald R Mattison; Gary D V Hankins; Mahmoud S Ahmed; Tatiana N Nanovskaya Journal: Am J Obstet Gynecol Date: 2008-08 Impact factor: 8.661
Authors: Ru Yan; Tatiana N Nanovskaya; Olga L Zharikova; Donald R Mattison; Gary D V Hankins; Mahmoud S Ahmed Journal: Biochem Pharmacol Date: 2008-02-07 Impact factor: 5.858