ArticleBiochemistry2015
Spectroscopic and mutagenesis studies of human PGRMC1.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 58 citations in OpenAlex.
- Sorghum bicolor membrane steroid binding protein 1 can bind heme and remodel ER membranes.Plant & cell physiology · 2026Article
- Sex differences in innate immune cell responses: Impact on cancer immunity and response to therapy.Frontiers in immunology · 2026Review
- Luteal insufficiency in canines: Assessment of progesterone dynamics and efficacy of combined hormonal treatment.Open veterinary journal · 2025Article
- Excessive progesterone impairs mouse decidualization via the Kyn-AhR pathway.Frontiers in cell and developmental biology · 2025Article
- Pleiotropy of Progesterone Receptor Membrane Component 1 in Modulation of Cytochrome P450 Activity.Journal of xenobiotics · 2024Review
- Reevaluating the Role of Progesterone in Ovarian Cancer: Is Progesterone Always Protective?Endocrine reviews · 2023Article
- Function and regulation of a steroidogenic CYP450 enzyme in the mitochondrion of Toxoplasma gondii.PLoS pathogens · 2023Article
- Reproductive Functions of the Mitochondrial Progesterone Receptor (PR-M).Reproductive sciences (Thousand Oaks, Calif.) · 2023Review
- PGRMC1: An enigmatic heme-binding protein.Pharmacology & therapeutics · 2023Review
- Review
- Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei.Metallomics : integrated biometal science · 2022Article
- A Recap of Heme Metabolism towards Understanding Protoporphyrin IX Selectivity in Cancer Cells.International journal of molecular sciences · 2022Review
- Pleiotropic Actions of PGRMC Proteins in Cancer.Endocrinology · 2022Review
- Review
- Progesterone Receptor Membrane Component (PGRMC)1 and PGRMC2 and Their Roles in Ovarian and Endometrial Cancer.Cancers · 2021Review
- Progesterone receptor membrane component 1 (PGRMC1) binds and stabilizes cytochromes P450 through a heme-independent mechanism.The Journal of biological chemistry · 2021Article
- PAQR6 Upregulation Is Associated with AR Signaling and Unfavorite Prognosis in Prostate Cancers.Biomolecules · 2021Article
- An Analysis of the Multifaceted Roles of Heme in the Pathogenesis of Cancer and Related Diseases.Cancers · 2021Review
- The Interface of Nuclear and Membrane Steroid Signaling.Endocrinology · 2021Review
- Crosstalk between progesterone receptor membrane component 1 and estrogen receptor α promotes breast cancer cell proliferation.Laboratory investigation; a journal of technical methods and pathology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Progesterone receptor membrane component 1 (PGRMC1) is a 25 kDa protein with an N-terminal transmembrane domain and a putative C-terminal cytochrome b5 domain. Heme-binding activity of PGRMC1 has been shown in various homologues of PGRMC1. Although the general definition of PGRMC1 is as a progesterone receptor, progesterone-binding activity has not been directly demonstrated in any of the purified PGRMC1 proteins fully loaded with heme. Here, we show that the human homologue of PGRMC1 (hPGRMC1) binds heme in a five-coordinate (5C) high-spin (HS) configuration, with an axial tyrosinate ligand, likely Y95. The negatively charged tyrosinate ligand leads to a relatively low redox potential of approximately -331 mV. The Y95C or Y95F mutation dramatically reduces the ability of the protein to bind heme, supporting the assignment of the axial heme ligand to Y95. On the other hand, the Y95H mutation retains ∼90% of the heme-binding activity. The heme in Y95H is also 5CHS, but it has a hydroxide axial ligand, conceivably stabilized by the engineered-in H95 via an H-bond; CO binding to the distal ligand-binding site leads to an exchange of the axial ligand to a histidine, possibly H95. We show that progesterone binds to hPGRMC1 and introduces spectral changes that manifest conformational changes to the heme. Our data offer the first direct evidence supporting progesterone-binding activity of PGRMC1.
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Registered trials
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.