The effect of esterases on 17α-hydroxyprogesterone caproate

Research output: Contribution to journalArticle

13 Citations (Scopus)

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)
JournalAmerican Journal of Obstetrics and Gynecology
Volume198
Issue number2
DOIs
StatePublished - Feb 2008

Fingerprint

Acetylesterase
17-alpha-Hydroxyprogesterone
Butyrylthiocholine
Esterases
Hydrolysis
Butyrylcholinesterase
Carboxylesterase
Liver
Radioactivity
Placenta
Progesterone
17-alpha-hydroxy-progesterone caproate
High Pressure Liquid Chromatography
Enzymes
In Vitro Techniques

Keywords

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

ASJC Scopus subject areas

  • Medicine(all)
  • Obstetrics and Gynecology

Cite this

The effect of esterases on 17α-hydroxyprogesterone caproate. / Yan, Ru; Fokina, Valentina; Hankins, Gary; Ahmed, Mahmoud; Nanovskaya, Tatiana.

In: American Journal of Obstetrics and Gynecology, Vol. 198, No. 2, 02.2008.

Research output: Contribution to journalArticle

@article{b21876b397544ae99b38ac3d68c0121b,
title = "The effect of esterases on 17α-hydroxyprogesterone caproate",
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.",
keywords = "17α-hydroxyprogesterone caproate, hydrolysis, spontaneous preterm labor",
author = "Ru Yan and Valentina Fokina and Gary Hankins and Mahmoud Ahmed and Tatiana Nanovskaya",
year = "2008",
month = "2",
doi = "10.1016/j.ajog.2007.07.038",
language = "English (US)",
volume = "198",
journal = "American Journal of Obstetrics and Gynecology",
issn = "0002-9378",
publisher = "Mosby Inc.",
number = "2",

}

TY - JOUR

T1 - The effect of esterases on 17α-hydroxyprogesterone caproate

AU - Yan, Ru

AU - Fokina, Valentina

AU - Hankins, Gary

AU - Ahmed, Mahmoud

AU - Nanovskaya, Tatiana

PY - 2008/2

Y1 - 2008/2

N2 - 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.

AB - 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.

KW - 17α-hydroxyprogesterone caproate

KW - hydrolysis

KW - spontaneous preterm labor

UR - http://www.scopus.com/inward/record.url?scp=38349136867&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=38349136867&partnerID=8YFLogxK

U2 - 10.1016/j.ajog.2007.07.038

DO - 10.1016/j.ajog.2007.07.038

M3 - Article

VL - 198

JO - American Journal of Obstetrics and Gynecology

JF - American Journal of Obstetrics and Gynecology

SN - 0002-9378

IS - 2

ER -