The effect of esterases on 17α-hydroxyprogesterone caproate

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Abstract

Objective: The aim of this investigation is to determine whether 17α-hydroxyprogesterone caproate is hydrolyzed, in vitro, to 17α-hydroxyprogesterone and caproate. Study Design: The in vitro hydrolysis of dual radioactively labeled 17α-hydroxy-[3H] progesterone [14C] caproate by human plasma, hepatic and placental S9 fractions as well as recombinant esterases was investigated. The formation of [3H]-17α-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 17α-hydroxyprogesterone caproate was incubated with the human-derived preparations under identical experimental conditions neither [3H]-17α-hydroxyprogesterone nor [14C]-caproate was detected. Conclusion: 17α-hydroxyprogesterone caproate is not hydrolyzed in vitro by the esterase enzymes present in human plasma, liver, preterm, or term placenta.

Original languageEnglish (US)
Pages (from-to)229.e1-229.e5
JournalAmerican journal of obstetrics and gynecology
Volume198
Issue number2
DOIs
StatePublished - Feb 2008

Keywords

  • 17α-hydroxyprogesterone caproate
  • hydrolysis
  • spontaneous preterm labor

ASJC Scopus subject areas

  • Obstetrics and Gynecology

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