Evidence map›Paper›PMID 23518922›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2013

A truncated progesterone receptor (PR-M) localizes to the mitochondrion and controls cellular respiration.

Qunsheng Dai, Anish A Shah, Rachana V Garde, Bryan A Yonish, Li Zhang, Neil A Medvitz, Sara E Miller, Elizabeth L Hansen, Carrie N Dunn, Thomas M Price

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Reproductive Functions of the Mitochondrial Progesterone Receptor (PR-M).Reproductive sciences (Thousand Oaks, Calif.) · 2023
    Review
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  11. Review
  12. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Qunsheng DaiDepartments of Obstetrics and Gynecology, Duke University, Durham, NC 27710, USA.
Anish A Shah
Rachana V Garde
Bryan A Yonish
Li Zhang
Neil A Medvitz
Sara E Miller
Elizabeth L Hansen
Carrie N Dunn
Thomas M Price
Duke University · USShenzhen Maternity and Child Healthcare Hospital · CN

Funding

Modulation of mitochondrial calcium by a novel progesterone receptorR03HD052770 · NICHD · DUKE UNIVERSITY · PI PRICE, THOMAS M · 2006 to 2007
$152k
NICHD NIH HHS 1R03HD052770-01NICHD NIH HHS R03 HD052770
6 · The paper itself

Abstract

The cDNA for a novel truncated progesterone receptor (PR-M) was previously cloned from human adipose and aortic cDNA libraries. The predicted protein sequence contains 16 unique N-terminal amino acids, encoded by a sequence in the distal third intron of the progesterone receptor PR gene, followed by the same amino acid sequence encoded by exons 4 through 8 of the nuclear PR. Thus, PR-M lacks the N terminus A/B domains and the C domain for DNA binding, whereas containing the hinge and hormone-binding domains. In this report, we have localized PR-M to mitochondria using immunofluorescent localization of a PR-M-green fluorescent protein (GFP) fusion protein and in Western blot analyses of purified human heart mitochondrial protein. Removal of the putative N-terminal mitochondrial localization signal obviated association of PR-M with mitochondria, whereas addition of the mitochondrial localization signal to green fluorescent protein resulted in mitochondrial localization. Immunoelectron microscopy and Western blot analysis after mitochondrial fractionation identified PR-M in the outer mitochondrial membrane. Antibody specificity was shown by mass spectrometry identification of a PR peptide in a mitochondrial membrane protein isolation. Cell models of overexpression and gene silencing of PR-M demonstrated a progestin-induced increase in mitochondrial membrane potential and an increase in oxygen consumption consistent with an increase in cellular respiration. This is the first example of a truncated steroid receptor, lacking a DNA-binding domain that localizes to the mitochondrion and initiates direct non-nuclear progesterone action. We hypothesize that progesterone may directly affect cellular energy production to meet the increased metabolic demands of pregnancy.

Indexed as

Base PairingBlotting, NorthernCell Line, TumorCell RespirationFemaleHumansMass SpectrometryMembrane Potential, MitochondrialMitochondria, HeartMitochondrial MembranesMitochondrial ProteinsOxygenPeptidesProgestinsProtein TransportReceptors, ProgesteroneMitochondrial ProteinsOxygenPeptidesPR-M protein, humanProgestinsReceptors, ProgesteroneRNA, Messenger

Identifiers

PMID23518922
PMCPMC3634113
OpenAlexW2108405868

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.