Evidence map›Paper›PMID 27599036›Full record

ArticleBiochemistry2016

A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.

Robert B Piel, Mesafint T Shiferaw, Ajay A Vashisht, Jason R Marcero, Jeremy L Praissman, John D Phillips, James A Wohlschlegel, Amy E Medlock

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 132 citations in OpenAlex.

  1. Review
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  10. Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025
    Review
  11. Update on heme biosynthesis, tissue-specific regulation, heme transport, relation to iron metabolism and cellular energy.Liver international : official journal of the International Association for the Study of the Liver · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Sigma Receptors: Novel Regulators of Iron/Heme Homeostasis and Ferroptosis.International journal of molecular sciences · 2023
    Review
  16. Inhibition ofVaccines · 2023
    Article
  17. Article
  18. Review
  19. Review
  20. Article

11 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Robert B PielDepartment of Biochemistry and Molecular Biology, Biomedical and Health Sciences Institute, AU/UGA Medical Partnership, University of Georgia , Athens, Georgia 30602, United States.
Mesafint T ShiferawDepartment of Biochemistry and Molecular Biology, Biomedical and Health Sciences Institute, AU/UGA Medical Partnership, University of Georgia , Athens, Georgia 30602, United States.
Ajay A VashishtDepartment of Biological Chemistry, University of California , Los Angeles, California 90095-1737, United States.
Jason R MarceroDepartment of Biochemistry and Molecular Biology, Biomedical and Health Sciences Institute, AU/UGA Medical Partnership, University of Georgia , Athens, Georgia 30602, United States.
Jeremy L PraissmanDepartment of Biochemistry and Molecular Biology, Biomedical and Health Sciences Institute, AU/UGA Medical Partnership, University of Georgia , Athens, Georgia 30602, United States.
John D PhillipsHematology Division, University of Utah School of Medicine , Salt Lake City, Utah 84132, United States.
James A WohlschlegelDepartment of Biological Chemistry, University of California , Los Angeles, California 90095-1737, United States.
Amy E MedlockDepartment of Biochemistry and Molecular Biology, Biomedical and Health Sciences Institute, AU/UGA Medical Partnership, University of Georgia , Athens, Georgia 30602, United States.
University of Georgia · USUniversity of California, Los Angeles · USUniversity of Utah · US

Funding

Porphyrias Consortium: SupplementU54DK083909 · NIDDK · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI DESNICK, ROBERT J · 2009 to 2023
$18.5M
TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Proteomics CoreU54DK110858 · NIDDK · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Anna E Beaudin, JAMES Eric COX · 2016 to 2026
$8.6M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
PORPHYRIN BIOSYNTHESIS IN NORMAL AND DISEASE STATESR01DK020503 · NIDDK · UNIVERSITY OF UTAH · PI PARKER, CHARLES J, PHILLIPS, JOHN DEARBORN · 1986 to 2012
$3.3M
PORPHYRIN BIOSYNTHESIS IN NORMAL AND DISEASE STATESR37DK020503 · NIDDK · UNIVERSITY OF UTAH · PI KUSHNER, JAMES P · 1993 to 2001
$463k
Porphyrin Biosynthesis in Normal and Disease StatesR56DK020503 · NIDDK · UNIVERSITY OF UTAH · PI PHILLIPS, JOHN DEARBORN · 2013 to 2013
$149k
NIDDK NIH HHS R01 DK020503NIDDK NIH HHS R37 DK020503NIDDK NIH HHS R56 DK020503NIDDK NIH HHS U54 DK083909NIDDK NIH HHS U54 DK110858NIGMS NIH HHS P41 GM103490NIGMS NIH HHS R01 GM089778
6 · The paper itself

Abstract

Heme is an iron-containing cofactor essential for multiple cellular processes and fundamental activities such as oxygen transport. To better understand the means by which heme synthesis is regulated during erythropoiesis, affinity purification coupled with mass spectrometry (MS) was performed to identify putative protein partners interacting with ferrochelatase (FECH), the terminal enzyme in the heme biosynthetic pathway. Both progesterone receptor membrane component 1 (PGRMC1) and progesterone receptor membrane component 2 (PGRMC2) were identified in these experiments. These interactions were validated by reciprocal affinity purification followed by MS analysis and immunoblotting. The interaction between PGRMC1 and FECH was confirmed in vitro and in HEK 293T cells, a non-erythroid cell line. When cells that are recognized models for erythroid differentiation were treated with a small molecule inhibitor of PGRMC1, AG-205, there was an observed decrease in the level of hemoglobinization relative to that of untreated cells. In vitro heme transfer experiments showed that purified PGRMC1 was able to donate heme to apo-cytochrome b5. In the presence of PGRMC1, in vitro measured FECH activity decreased in a dose-dependent manner. Interactions between FECH and PGRMC1 were strongest for the conformation of FECH associated with product release, suggesting that PGRMC1 may regulate FECH activity by controlling heme release. Overall, the data illustrate a role for PGRMC1 in regulating heme synthesis via interactions with FECH and suggest that PGRMC1 may be a heme chaperone or sensor.

Indexed as

AnimalsCell LineFerrochelataseHumansMembrane ProteinsMiceReceptors, ProgesteroneFerrochelataseMembrane ProteinsPGRMC1 protein, humanReceptors, Progesterone

Identifiers

PMID27599036
PMCPMC5278647
OpenAlexW2512794557

What OpenQuestion holds

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Registered trials

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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.