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The emerging role of progesterone receptor membrane component 1 (PGRMC1) in cancer biology

Cahill, Michael A., Jazayeri, Jalal A., Catalano, Susan M., Toyokuni, Shinya, Kovacevic, Zaklina, Richardson, Des R.·2016·Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

Abstract

Progesterone receptor membrane component 1 (PGRMC1) is a multi-functional protein with a heme-binding moiety related to that of cytochrome b 5 , which is a putative progesterone receptor. The recently solved PGRMC1 structure revealed that heme-binding involves coordination by a tyrosinate ion at Y113, and induces dimerization which is stabilized by hydrophobic stacking of heme on adjacent monomers. Dimerization is required for association with cytochrome P450 (cyP450) enzymes, which mediates chemoresistance to doxorubicin and may be responsible for PGRMC1's anti-apoptotic activity. Here we review the multiple attested involvement of PGRMC1 in diverse functions, including regulation of cytochrome P450, steroidogenesis, vesicle trafficking, progesterone signaling and mitotic spindle and cell cycle regulation. Its wide range of biological functions is attested to particularly by its emerging association with cancer and progesterone-responsive female reproductive tissues. PGRMC1 exhibits all the hallmarks of a higher order nexus signal integration hub protein. It appears capable of acting as a detector that integrates information from kinase/phosphatase pathways with heme and CO levels and probably redox status.

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Research works printed but not linked: 136

  1. Cahill, 2007, Progesterone receptor membrane component 1: an integrative review, J. Steroid Biochem. Mol. Biol., 105, 16, 10.1016/j.jsbmb.2007.02.002 · DOI
  2. Ahmed, 2012, S2R(Pgrmc1): the cytochrome-related sigma-2 receptor that regulates lipid and drug metabolism and hormone signaling, Expert Opin. Drug Metab. Toxicol., 8, 361, 10.1517/17425255.2012.658367 · DOI · Paper page
  3. Losel, 2008, Progesterone receptor membrane component 1–many tasks for a versatile protein, Steroids, 73, 929, 10.1016/j.steroids.2007.12.017 · DOI
  4. Selmin, 1996, Isolation and characterization of a novel gene induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver, Carcinogenesis, 17, 2609, 10.1093/carcin/17.12.2609 · DOI
  5. Meyer, 1996, Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes, Eur. J. Biochem., 239, 726, 10.1111/j.1432-1033.1996.0726u.x · DOI
  6. Gerdes, 1998, Cloning and tissue expression of two putative steroid membrane receptors, Biol. Chem., 379, 907
  7. Kimura, 2012, Functions of MAPR (membrane-associated progesterone receptor) family members as heme/steroid-binding proteins, Curr. Protein Pept. Sci., 13, 687, 10.2174/138920312804142110 · DOI
  8. Mifsud, 2002, Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain, Genome Biol., 3, 10.1186/gb-2002-3-12-research0068 · DOI
  9. Yoshitani, 2005, A structure-based strategy for discovery of small ligands binding to functionally unknown proteins: combination of in silico screening and surface plasmon resonance measurements, Proteomics, 5, 1472, 10.1002/pmic.200401032 · DOI
  10. Ahmed, 2010, Progesterone receptor membrane component 1 (Pgrmc1): a heme-1 domain protein that promotes tumorigenesis and is inhibited by a small molecule, J. Pharmacol. Exp. Ther., 333, 564, 10.1124/jpet.109.164210 · DOI
  11. Ahmed, 2010, Pgrmc1 (progesterone receptor membrane component 1) associates with epidermal growth factor receptor and regulates erlotinib sensitivity, J. Biol. Chem., 285, 24775, 10.1074/jbc.M110.134585 · DOI
  12. Zhang, 2014, Progesterone receptor membrane component 1 is a functional part of the glucagon-like peptide-1 (GLP-1) receptor complex in pancreatic beta cells, Mol. Cell. Proteomics, 13, 3049, 10.1074/mcp.M114.040196 · DOI
  13. Bashour, 2012, Progesterone directly and rapidly inhibits GnRH neuronal activity via progesterone receptor membrane component 1, Endocrinology, 153, 4457, 10.1210/en.2012-1122 · DOI
  14. Mir, 2012, Elevated progesterone receptor membrane component 1/sigma-2 receptor levels in lung tumors and plasma from lung cancer patients, Int. J. Cancer, 131, E1, 10.1002/ijc.26432 · DOI
  15. Wyse Jackson, 2016, Progesterone receptor signalling in retinal photoreceptor neuroprotection, J. Neurochem., 136, 63, 10.1111/jnc.13388 · DOI
  16. Palmerini, 2016, Antagonistic effect of a salivary proline-rich peptide on the cytosolic Ca2+ mobilization induced by progesterone in oral squamous cancer cells, PLoS One, 11, 10.1371/journal.pone.0147925 · DOI
  17. Qin, 2015, Progesterone attenuates Abeta25-35-induced neuronal toxicity via JNK inactivation and progesterone receptor membrane component 1-dependent inhibition of mitochondrial apoptotic pathway, J. Steroid Biochem. Mol. Biol., 154, 302, 10.1016/j.jsbmb.2015.01.002 · DOI
  18. Fan, 2015, Drospirenone enhances GPIb-IX-V-mediated platelet activation, J. Thromb. Haemost., 13, 1918, 10.1111/jth.13109 · DOI
  19. Aizen, 2015, Role of Pgrmc1 in estrogen maintenance of meiotic arrest in zebrafish oocytes through Gper/Egfr, J. Endocrinol., 225, 59, 10.1530/JOE-14-0576 · DOI
  20. Wessel, 2014, New aspects of progesterone interactions with the actin cytoskeleton and neurosteroidogenesis in the cerebellum and the neuronal growth cone, J. Histochem. Cytochem., 62, 835, 10.1369/0022155414550691 · DOI
  21. Rohe, 2009, PGRMC1 (progesterone receptor membrane component 1): a targetable protein with multiple functions in steroid signaling, P450 activation and drug binding, Pharmacol. Ther., 121, 14, 10.1016/j.pharmthera.2008.09.006 · DOI · Paper page
  22. Hughes, 2007, Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes, Cell Metab., 5, 143, 10.1016/j.cmet.2006.12.009 · DOI · Paper page
  23. Oda, 2011, Progesterone receptor membrane component 1 modulates human cytochrome p450 activities in an isoform-dependent manner, Drug Metab. Dispos., 39, 2057, 10.1124/dmd.111.040907 · DOI
  24. Szczesna-Skorupa, 2011, Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductase, Mol. Pharmacol., 79, 340, 10.1124/mol.110.068478 · DOI
  25. Kabe, 2016, Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance, Nat. Commun., 7, 11030, 10.1038/ncomms11030 · DOI · Paper page
  26. Clark, 2016, Progesterone receptor membrane component 1 promotes survival of human breast cancer cells and the growth of xenograft tumors, Cancer Biol. Ther., 17, 262, 10.1080/15384047.2016.1139240 · DOI
  27. Lin, 2015, PGRMC1 contributes to doxorubicin-induced chemoresistance in MES-SA uterine sarcoma, Cell. Mol. Life Sci., 72, 2395, 10.1007/s00018-014-1831-9 · DOI
  28. Friel, 2015, Progesterone receptor membrane component 1 deficiency attenuates growth while promoting chemosensitivity of human endometrial xenograft tumors, Cancer Lett., 356, 434, 10.1016/j.canlet.2014.09.036 · DOI
  29. Lin, 2013, Redox-proteomic analysis of doxorubicin resistance-induced altered thiol activity in uterine carcinoma, J. Pharm. Biomed. Anal., 78-79, 1, 10.1016/j.jpba.2013.01.028 · DOI
  30. Lin, 2012, Proteomic analysis of proteins responsible for the development of doxorubicin resistance in human uterine cancer cells, J. Proteome, 75, 5822, 10.1016/j.jprot.2012.07.047 · DOI
  31. Zhu, 2013, Progesterone protects ovarian cancer cells from cisplatin-induced inhibitory effects through progesterone receptor membrane component 1/2 as well as AKT signaling, Oncol. Rep., 30, 2488, 10.3892/or.2013.2680 · DOI
  32. Peluso, 2009, Progesterone receptor membrane component-1 regulates the development and cisplatin sensitivity of human ovarian tumors in athymic nude mice, Endocrinology, 150, 4846, 10.1210/en.2009-0730 · DOI
  33. Peluso, 2008, Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component-1, J. Clin. Endocrinol. Metab., 93, 1592, 10.1210/jc.2007-2771 · DOI
  34. Liu, 2012, Reversal of paclitaxel resistance in epithelial ovarian carcinoma cells by a MUC1 aptamer-let-7i chimera, Cancer Investig., 30, 577, 10.3109/07357907.2012.707265 · DOI
  35. Dressman, 2006, Gene expression profiles of multiple breast cancer phenotypes and response to neoadjuvant chemotherapy, Clin. Cancer Res., 12, 819, 10.1158/1078-0432.CCR-05-1447 · DOI · Paper page
  36. Wegiel, 2013, Carbon monoxide expedites metabolic exhaustion to inhibit tumor growth, Cancer Res., 73, 7009, 10.1158/0008-5472.CAN-13-1075 · DOI
  37. Neubauer, 2008, Breast cancer proteomics reveals correlation between estrogen receptor status and differential phosphorylation of PGRMC1, Breast Cancer Res., 10, R85, 10.1186/bcr2155 · DOI
  38. Raza, 2001, Identification of the rat adrenal zona fasciculata/reticularis specific protein, inner zone antigen (IZAg), as the putative membrane progesterone receptor, Eur. J. Biochem., 268, 2141, 10.1046/j.1432-1327.2001.02096.x · DOI
  39. Sakamoto, 2008, Cerebellum, 7, 18, 10.1007/s12311-008-0007-2 · DOI
  40. Wessel, 2014, Long-term incubation with mifepristone (MLTI) increases the spine density in developing Purkinje cells: new insights into progesterone receptor mechanisms, Cell. Mol. Life Sci., 71, 1723, 10.1007/s00018-013-1448-4 · DOI
  41. Min, 2005, Molecular identification of adrenal inner zone antigen as a heme-binding protein, FEBS J., 272, 5832, 10.1111/j.1742-4658.2005.04977.x · DOI
  42. Zhang, 2008, Expression of progesterone receptor membrane component 1 and its partner serpine 1 mRNA binding protein in uterine and placental tissues of the mouse and human, Mol. Cell. Endocrinol., 287, 81, 10.1016/j.mce.2008.02.012 · DOI
  43. Peluso, 2013, Progesterone receptor membrane component 1 and its role in ovarian follicle growth, Front. Neurosci., 7, 99, 10.3389/fnins.2013.00099 · DOI
  44. Suchanek, 2005, Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells, Nat. Methods, 2, 261, 10.1038/nmeth752 · DOI
  45. Shao, 2012, Expanding roles for SREBP in metabolism, Cell Metab., 16, 414, 10.1016/j.cmet.2012.09.002 · DOI
  46. Cheng, 2015, Glucose-mediated N-glycosylation of SCAP is essential for SREBP-1 activation and tumor growth, Cancer Cell, 28, 569, 10.1016/j.ccell.2015.09.021 · DOI
  47. Shao, 2015, Sugar makes fat by talking to SCAP, Cancer Cell, 28, 548, 10.1016/j.ccell.2015.10.011 · DOI
  48. Min, 2004, Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis, Mol. Cell. Endocrinol., 215, 143, 10.1016/j.mce.2003.11.025 · DOI
  49. Rozman, 1996, Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes, Genomics, 38, 371, 10.1006/geno.1996.0640 · DOI
  50. Bali, 2013, Pgrmc1: new roles in the microglial mediation of progesterone-antagonism of estradiol-dependent neurite sprouting and in microglial activation, Front. Neurosci., 7, 157, 10.3389/fnins.2013.00157 · DOI
  51. Arimoto, 2013, Age increase of estrogen receptor-alpha (ERalpha) in cortical astrocytes impairs neurotrophic support in male and female rats, Endocrinology, 154, 2101, 10.1210/en.2012-2046 · DOI
  52. Bali, 2013, Progesterone antagonism of neurite outgrowth depends on microglial activation via Pgrmc1/S2R, Endocrinology, 154, 2468, 10.1210/en.2012-2109 · DOI
  53. Peluso, 2012, Progesterone regulation of progesterone receptor membrane component 1 (PGRMC1) sumoylation and transcriptional activity in spontaneously immortalized granulosa cells, Endocrinology, 153, 3929, 10.1210/en.2011-2096 · DOI
  54. Peluso, 2006, Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action, Endocrinology, 147, 3133, 10.1210/en.2006-0114 · DOI
  55. Peluso, 2008, Endocrinology, 149, 534, 10.1210/en.2007-1050 · DOI
  56. Peluso, 2013, Plasminogen activator inhibitor 1 RNA-binding protein interacts with progesterone receptor membrane component 1 to regulate progesterone's ability to maintain the viability of spontaneously immortalized granulosa cells and rat granulosa cells, Biol. Reprod., 88, 20, 10.1095/biolreprod.112.103036 · DOI
  57. Crudden, 2006, Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs, J. Pharmacol. Exp. Ther., 316, 448, 10.1124/jpet.105.094631 · DOI
  58. Sakamoto, 2004, Expression and localization of 25-Dx, a membrane-associated putative progesterone-binding protein, in the developing Purkinje cell, Neuroscience, 126, 325, 10.1016/j.neuroscience.2004.04.003 · DOI
  59. Peluso, 2014, Non-canonical progesterone signaling in granulosa cell function, Reproduction, 147, R169, 10.1530/REP-13-0582 · DOI
  60. Chen, 2011, De novo duplication of Xq22.1→q24 with a disruption of the NXF gene cluster in a mentally retarded woman with short stature and premature ovarian failure, Taiwan J. Obstet. Gynecol., 50, 339, 10.1016/j.tjog.2011.01.018 · DOI
  61. Schuster, 2010, Down-regulation of progesterone receptor membrane component 1 (PGRMC1) in peripheral nucleated blood cells associated with premature ovarian failure (POF) and polycystic ovary syndrome (PCOS), Reprod. Biol. Endocrinol., 8, 58, 10.1186/1477-7827-8-58 · DOI
  62. Wang, 2014, Analysis of progesterone receptor membrane component 1 mutation in Han Chinese women with premature ovarian failure, Reprod. BioMed. Online, 29, 640, 10.1016/j.rbmo.2014.08.001 · DOI
  63. Elassar, 2012, The relationship between follicle development and progesterone receptor membrane component-1 expression in women undergoing in vitro fertilization, Fertil. Steril., 97, 572, 10.1016/j.fertnstert.2011.12.026 · DOI
  64. Qin, 2015, Genetics of primary ovarian insufficiency: new developments and opportunities, Hum. Reprod. Update, 21, 787, 10.1093/humupd/dmv036 · DOI
  65. Kalinowski, 2016, Redox cycling metals: pedaling their roles in metabolism and their use in the development of novel therapeutics, Biochim. Biophys. Acta, 1863, 727, 10.1016/j.bbamcr.2016.01.026 · DOI
  66. Kaluka, 2015, Spectroscopic and mutagenesis studies of human PGRMC1, Biochemistry, 54, 1638, 10.1021/bi501177e · DOI
  67. Hornbeck, 2004, PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation, Proteomics, 4, 1551, 10.1002/pmic.200300772 · DOI
  68. Wagner, 2012, Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues, Mol. Cell. Proteomics, 11, 1578, 10.1074/mcp.M112.017905 · DOI
  69. Wagner, 2011, A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles, Mol. Cell. Proteomics, 10, 10.1074/mcp.M111.013284 · DOI
  70. Zhao, 2014, GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs, Nucleic Acids Res., 42, W325, 10.1093/nar/gku383 · DOI
  71. Moreno-Gonzalo, 2014, Post-translational modifications of exosomal proteins, Front. Immunol., 5, 383, 10.3389/fimmu.2014.00383 · DOI
  72. Penfornis, 2016, Extracellular vesicles as carriers of microRNA, proteins and lipids in tumor microenvironment, Int. J. Cancer, 138, 14, 10.1002/ijc.29417 · DOI
  73. Meehan, 2016, The contribution of tumour-derived exosomes to the hallmarks of cancer, Crit. Rev. Clin. Lab. Sci., 53, 121, 10.3109/10408363.2015.1092496 · DOI
  74. Eifler, 2015, Mapping the SUMOylated landscape, FEBS J., 282, 3669, 10.1111/febs.13378 · DOI
  75. Brown, 2015, Ubiquitylation, neddylation and the DNA damage response, Open Biol., 5, 150018, 10.1098/rsob.150018 · DOI
  76. Ding, 2014, The role of the ubiquitin-proteasome pathway in cancer development and treatment, Front. Biosci., 19, 886, 10.2741/4254 · DOI
  77. Sueldo, 2015, Progestin and adipoQ receptor 7, progesterone membrane receptor component 1 (PGRMC1), and PGRMC2 and their role in regulating progesterone's ability to suppress human granulosa/luteal cells from entering into the cell cycle, Biol. Reprod., 93, 63, 10.1095/biolreprod.115.131508 · DOI
  78. Peluso, 2014, Progesterone receptor membrane component-1 (PGRMC1) and PGRMC-2 interact to suppress entry into the cell cycle in spontaneously immortalized rat granulosa cells, Biol. Reprod., 91, 104, 10.1095/biolreprod.114.122986 · DOI
  79. Runko, 1999, Cloning and expression of VEMA: a novel ventral midline antigen in the rat CNS, Mol. Cell. Neurosci., 14, 428, 10.1006/mcne.1999.0794 · DOI
  80. Runko, 2004, Caenorhabditis elegans VEM-1, a novel membrane protein, regulates the guidance of ventral nerve cord-associated axons, J. Neurosci., 24, 9015, 10.1523/JNEUROSCI.2385-04.2004 · DOI · Paper page
  81. Pandey, 2009, Functional roles of short sequence motifs in the endocytosis of membrane receptors, Front. Biosci., 14, 5339, 10.2741/3599 · DOI
  82. Sunder-Plassmann, 1997, Functional analysis of immunoreceptor tyrosine-based activation motif (ITAM)-mediated signal transduction: the two YxxL segments within a single CD3zeta-ITAM are functionally distinct, Eur. J. Immunol., 27, 2001, 10.1002/eji.1830270826 · DOI
  83. Munton, 2007, Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations, Mol. Cell. Proteomics, 6, 283, 10.1074/mcp.M600046-MCP200 · DOI
  84. Hampton, 2014, Pathways driving the endocytosis of mutant and wild-type EGFR in cancer, Oncoscience, 1, 504, 10.18632/oncoscience.67 · DOI · Paper page
  85. Mir, 2012, Neutrophil gelatinase-associated lipocalin (NGAL) expression is dependent on the tumor-associated sigma-2 receptor S2RPgrmc1, J. Biol. Chem., 287, 14494, 10.1074/jbc.M111.324921 · DOI
  86. Izzo, 2014, Alzheimer's therapeutics targeting amyloid beta 1-42 oligomers II: sigma-2/PGRMC1 receptors mediate Abeta 42 oligomer binding and synaptotoxicity, PLoS One, 9
  87. Kayed, 2013, Molecular mechanisms of amyloid oligomers toxicity, J. Alzheimers Dis., 33, S67
  88. Malenka, 2004, LTP and LTD: an embarrassment of riches, Neuron, 44, 5, 10.1016/j.neuron.2004.09.012 · DOI · Paper page
  89. Huganir, 2013, AMPARs and synaptic plasticity: the last 25 years, Neuron, 80, 704, 10.1016/j.neuron.2013.10.025 · DOI · Paper page
  90. Puzzo, 2005, Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity, J. Neurosci., 25, 6887, 10.1523/JNEUROSCI.5291-04.2005 · DOI
  91. Cahill, 2016, PGRMC1 regulation by phosphorylation: potential new insights in controlling biological activity!, Oncotarget, 10.18632/oncotarget.10691 · DOI
  92. Su, 2012, Progesterone increases the release of brain-derived neurotrophic factor from glia via progesterone receptor membrane component 1 (Pgrmc1)-dependent ERK5 signaling, Endocrinology, 153, 4389, 10.1210/en.2011-2177 · DOI
  93. Sun, 2016, Pgrmc1/BDNF signaling plays a critical role in mediating glia-neuron cross talk, Endocrinology, 157, 2067, 10.1210/en.2015-1610 · DOI
  94. Thomas, 2014, Enhancement of cell surface expression and receptor functions of membrane progestin receptor alpha (mPRalpha) by progesterone receptor membrane component 1 (PGRMC1): evidence for a role of PGRMC1 as an adaptor protein for steroid receptors, Endocrinology, 155, 1107, 10.1210/en.2013-1991 · DOI
  95. Wang, 2014, G protein-coupled receptors: extranuclear mediators for the non-genomic actions of steroids, Int. J. Mol. Sci., 15, 15412, 10.3390/ijms150915412 · DOI
  96. Crudden, 2005, Overexpression of the cytochrome p450 activator hpr6 (heme-1 domain protein/human progesterone receptor) in tumors, Tumour Biol., 26, 142, 10.1159/000086485 · DOI
  97. Peluso, 2007, Non-genomic actions of progesterone in the normal and neoplastic mammalian ovary, Semin. Reprod. Med., 25, 198, 10.1055/s-2007-973432 · DOI
  98. Peluso, 2011, Progesterone signaling mediated through progesterone receptor membrane component-1 in ovarian cells with special emphasis on ovarian cancer, Steroids, 76, 903
  99. Hampton, 2015, PGRMC1 elevation in multiple cancers and essential role in stem cell survival, Adv. Lung Cancer, 4, 37, 10.4236/alc.2015.43006 · DOI
  100. Mir, 2013, Progesterone receptor membrane component 1/Sigma-2 receptor associates with MAP1LC3B and promotes autophagy, Autophagy, 9, 1566, 10.4161/auto.25889 · DOI · Paper page
  101. Zhao, 2015, Hyaluronic acid prevents immunosuppressive drug-induced ovarian damage via up-regulating PGRMC1 expression, Sci. Rep., 5, 7647, 10.1038/srep07647 · DOI
  102. Bruce, 2014, CYB5D2 requires heme-binding to regulate HeLa cell growth and confer survival from chemotherapeutic agents, PLoS One, 9, 10.1371/journal.pone.0086435 · DOI
  103. Neubauer, 2013, Overexpression of progesterone receptor membrane component 1: possible mechanism for increased breast cancer risk with norethisterone in hormone therapy, Menopause, 20, 504, 10.1097/gme.0b013e3182755c97 · DOI
  104. Neubauer, 2009, Membrane-initiated effects of progesterone on proliferation and activation of VEGF in breast cancer cells, Climacteric, 12, 230, 10.1080/13697130802635637 · DOI
  105. Morandell, 2008, Quantitative proteomics and phosphoproteomics reveal novel insights into complexity and dynamics of the EGFR signaling network, Proteomics, 8, 4383, 10.1002/pmic.200800204 · DOI
  106. Schneck, 2013, Membrane-receptor initiated proliferative effects of dienogest in human breast cancer cells, Gynecol. Endocrinol., 29, 160, 10.3109/09513590.2012.730572 · DOI
  107. Liu, 2015, Oestetrol stimulates proliferation and oestrogen receptor expression in breast cancer cell lines: comparison of four oestrogens, Eur. J. Contracept. Reprod. Health Care, 20, 29, 10.3109/13625187.2014.951997 · DOI
  108. Zhang, 2016, May progesterone receptor membrane component 1 (PGRMC1) predict the risk of breast cancer?, Gynecol. Endocrinol., 32, 58, 10.3109/09513590.2015.1078303 · DOI
  109. Ruan, 2012, Progestogens and membrane-initiated effects on the proliferation of human breast cancer cells, Climacteric, 15, 467, 10.3109/13697137.2011.648232 · DOI
  110. Ruan, 2012, Nomegestrol acetate sequentially or continuously combined to estradiol did not negatively affect membrane-receptor associated progestogenic effects in human breast cancer cells, Gynecol. Endocrinol., 28, 863, 10.3109/09513590.2012.671396 · DOI
  111. Neubauer, 2013, Possible role of PGRMC1 in breast cancer development, Climacteric, 16, 509, 10.3109/13697137.2013.800038 · DOI
  112. Zhou, 2013, Medroxyprogesterone acetate-driven increase in breast cancer risk might be mediated via cross-talk with growth factors in the presence of progesterone receptor membrane component-1, Maturitas, 76, 129, 10.1016/j.maturitas.2013.06.013 · DOI
  113. Griffin, 2014, Expression of progesterone receptor membrane component-2 within the immature rat ovary and its role in regulating mitosis and apoptosis of spontaneously immortalized granulosa cells, Biol. Reprod., 91, 36, 10.1095/biolreprod.114.117481 · DOI
  114. Lodde, 2011, A novel role for progesterone and progesterone receptor membrane component 1 in regulating spindle microtubule stability during rat and human ovarian cell mitosis, Biol. Reprod., 84, 715, 10.1095/biolreprod.110.088385 · DOI
  115. Luciano, 2013, Oocytes isolated from dairy cows with reduced ovarian reserve have a high frequency of aneuploidy and alterations in the localization of progesterone receptor membrane component 1 and aurora kinase B, Biol. Reprod., 88, 58, 10.1095/biolreprod.112.106856 · DOI
  116. Terzaghi, 2016, PGRMC1 participates in late events of bovine granulosa cells mitosis and oocyte meiosis, Cell Cycle, 10.1080/15384101.2016.1192731 · DOI
  117. Albrecht, 2012, In vitro inhibition of SKOV-3 cell migration as a distinctive feature of progesterone receptor membrane component type 2 versus type 1, Steroids, 77, 1543, 10.1016/j.steroids.2012.09.006 · DOI
  118. Mach, 2013, The sigma receptor: a novel protein for the imaging and treatment of cancer, J. Med. Chem., 56, 7137, 10.1021/jm301545c · DOI
  119. Hornick, 2012, Therapeutic targeting of pancreatic cancer utilizing sigma-2 ligands, Surgery, 152, S152, 10.1016/j.surg.2012.05.014 · DOI
  120. Matsumoto, 2014, Chapter Nine - Sigma (σ) receptors as potential therapeutic targets to mitigate psychostimulant effects, vol. 69, 323
  121. Garg, 2014, Conjugation to a SMAC mimetic potentiates sigma-2 ligand induced tumor cell death in ovarian cancer, Mol. Cancer, 13, 50, 10.1186/1476-4598-13-50 · DOI
  122. Makvandi, 2015, The sigma-2 receptor as a therapeutic target for drug delivery in triple negative breast cancer, Biochem. Biophys. Res. Commun., 467, 1070, 10.1016/j.bbrc.2015.09.157 · DOI
  123. Zeng, 2013, Sigma-2 receptor ligand as a novel method for delivering a SMAC mimetic drug for treating ovarian cancer, Br. J. Cancer, 109, 2368, 10.1038/bjc.2013.593 · DOI
  124. Hashim, 2014, Targeted pancreatic cancer therapy with the small molecule drug conjugate SW IV-134, Mol. Oncol., 8, 956, 10.1016/j.molonc.2014.03.005 · DOI
  125. Xu, 2011, Identification of the PGRMC1 protein complex as the putative sigma-2 receptor binding site, Nat. Commun., 2, 380, 10.1038/ncomms1386 · DOI · Paper page
  126. Zeng, 2016, The PGRMC1 protein level correlates with the binding activity of a sigma-2 fluorescent probe (SW120) in rat brain cells, Mol. Imaging Biol., 18, 172, 10.1007/s11307-015-0891-z · DOI · Paper page
  127. Chu, 2015, The sigma-2 receptor and progesterone receptor membrane component 1 are different binding sites derived from independent genes, EBioMedicine, 2, 1806, 10.1016/j.ebiom.2015.10.017 · DOI · Paper page
  128. Abate, 2015, Elements in support of the ‘non-identity’ of the PGRMC1 protein with the sigma receptor, Eur. J. Pharmacol., 758, 16, 10.1016/j.ejphar.2015.03.067 · DOI · Paper page
  129. Wendler, 2013, PGRMC2, a yet uncharacterized protein with potential as tumor suppressor, migration inhibitor, and regulator of cytochrome P450 enzyme activity, Steroids, 78, 555, 10.1016/j.steroids.2012.12.002 · DOI
  130. Hellewell, 1994, Rat liver and kidney contain high densities of sigma 1 and sigma 2 receptors: characterization by ligand binding and photoaffinity labeling, Eur. J. Pharmacol., 268, 9, 10.1016/0922-4106(94)90115-5 · DOI · Paper page
  131. Rodriguez, 2014, Interplay between nuclear transport and ubiquitin/SUMO modifications in the regulation of cancer-related proteins, Semin. Cancer Biol., 27, 11, 10.1016/j.semcancer.2014.03.005 · DOI
  132. Ponten, 2008, The Human Protein Atlas–a tool for pathology, J. Pathol., 216, 387, 10.1002/path.2440 · DOI
  133. Goh, 2007, The human disease network, Proc. Natl. Acad. Sci. U. S. A., 104, 8685, 10.1073/pnas.0701361104 · DOI · Paper page
  134. Price, 2013, Progesterone receptor membrane component 1: is metabolism integral to its function and what other steroids are involved?, Menopause, 20, 486, 10.1097/GME.0b013e318287f30e · DOI
  135. Feng, 2012, PGRMC1 involved in the regulation of cell proliferation of breast cancer and experimental chemotherapy sensitivity, Cancer Res. Prev. Treat., 39, 123
  136. Ji, 2012, Expression of progesterone receptor membrane component-1 is associated with the malignant phenotypes of breast cancer, Nan Fang Yi Ke Da Xue Xue Bao, 32, 635

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Metadata

Authors
Cahill, M. A., Jazayeri, J. A., Catalano, S. M., Toyokuni, S., Kovacevic, Z., & Richardson, D. R.
Venue
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer
Publisher
Elsevier BV
Published
2016-12
Volume
1866
Issue
2
Pages
339-349
ISSN
0304-419X
Cited by
40
References
4
Language
en
Funders
  • Charles Sturt University (A541-900-xxx-40513, A534-900-xxx-41066, A102-900-xxx-40002)
  • NHMRC (APP1062607, APP1037323)
  • Cancer Institute NSW (12ECF2-17)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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