ArticleReproductive sciences (Thousand Oaks, Calif.)2012
Metabolism of 17-alpha-hydroxyprogesterone caproate by human placental mitochondria.
Article in Reproductive sciences (Thousand Oaks, Calif.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
5 citing papers in PubMed.
- Pharmacology and placental transport of 17-hydroxyprogesterone caproate in singleton gestation.American journal of obstetrics and gynecology · 2012Trial
- In utero exposure to 17α-hydroxyprogesterone caproate and risk of cancer in offspring.American journal of obstetrics and gynecology · 2022Article
- Basic obstetric pharmacology.Seminars in perinatology · 2014Review
- Bioanalysis of eukaryotic organelles.Chemical reviews · 2013Review
- Liquid chromatography-tandem mass spectrometry analysis of human adrenal vein 19-carbon steroids before and after ACTH stimulation.The Journal of clinical endocrinology and metabolism · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Perfusion of 17-alpha-hydroxyprogesterone caproate (17HPC) via the maternal circuit of a dually perfused human placental lobule resulted in the extensive formation of 2 metabolites. On the other hand, human placental microsomes biotransformed 17HPC into 5 monohydroxylated metabolites, which did not correspond to those formed during perfusion. The goal of this investigation was to determine the subcellular localization of the enzymes responsible for the biotransformation of 17HPC during its perfusion in human placenta. Crude subcellular fractions of the human placental tissue were utilized. Six 17HPC metabolites were formed by the placental mitochondrial fraction, of which 4 were identical to those formed by the microsomes; whereas the other 2, namely MM and M₁₉, were formed by the mitochondrial fraction only. The latter metabolites were identical to those formed during 17HPC perfusion, as determined by liquid chromatography-mass spectrometry (LC-MS) analysis. Therefore, these data strongly suggest that the enzymes responsible for the biotransformation of 17HPC during its perfusion are predominantly localized in human placental mitochondria.
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Registered trials
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