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PGRMC1

Progesterone receptor membrane component 1 (abbreviated PGRMC1) is a protein which co-purifies with progesterone binding proteins in the liver and ovary.[5][6] In humans, the PGRMC1 protein is encoded by the PGRMC1 gene.[7]

PGRMC1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPGRMC1, HPR6.6, MPR, progesterone receptor membrane component 1, Dap1, IZA
External IDsOMIM: 300435 MGI: 1858305 HomoloGene: 48457 GeneCards: PGRMC1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006667
NM_001282621

NM_016783

RefSeq (protein)

NP_001269550
NP_006658
NP_006658.1

NP_058063

Location (UCSC)Chr X: 119.24 – 119.24 MbChr X: 35.86 – 35.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The sole biochemical function of PGRMC1 is heme-binding.[8][9] PGRMC1 shares key structural motifs with cytochrome b5.[10] PGRMC1 binds and activates P450 proteins,[11][12][13] which are important in drug, hormone and lipid metabolism. PGRMC1 also binds to PAIR-BP1 (plasminogen activator inhibitor RNA-binding protein-1).[6] However, its expression outside of the reproductive tract and in males suggests multiple functions for the protein. These may include binding to Insig (insulin-induced gene),[14] which regulates cholesterol synthesis.[15]

Expression edit

PGRMC1 is highly expressed in the liver and kidney in humans[7] with lower expression in the brain, lung, heart, skeletal muscle and pancreas.[7][16][17] In rodents, PGRMC1 is found in the liver, lung, kidney and brain.[16][17] PGRMC1 is over-expressed in breast tumors and in cancer cell lines from the colon, thyroid, ovary, lung, and cervix.[18][19] Microarray analyses have detected PGRMC1 expression in colon, lung and breast tumors.[20][21][22]

PGRMC1 expression is induced by the non-genotoxic carcinogen 2,3,7,8-tetrachlorodibenzo-p-dioxin in the rat liver,[17] but this induction is specific to males.[23] PGRMC1 is expressed in the ovary and corpus luteum, where its expression is induced by progesterone[24] and during pregnancy,[25] respectively. PGRMC1/25-Dx is expressed in various regions of the brain [hypothalamic area, circumventricular organs, ependymal cells of the lateral ventricles, meninges,[16][26] including regions known to facilitate lordosis.[16]

Binding to heme and cytochrome P450s edit

The PGRMC1 yeast homologue, Dap1 (damage associated protein 1), binds heme[9][27] through a penta-coordinate mechanism.[9][28] Yeast cells lacking the DAP1 gene are sensitive to DNA damage,[29] and heme-binding is essential for damage resistance.[27] Dap1 is also required for a critical step in cholesterol synthesis in which the P450 protein Erg11/Cyp51 removes a methyl group from lanosterol.[11][27][29][30] Erg11/Cyp51 is the target of the azole antifungal drugs. As a result, yeast cells lacking the DAP1 gene are highly sensitive to antifungal drugs[11][27][29] This function is conserved between the unrelated fungi S. cerevisiae and S. pombe. Dap1 also regulates the metabolism of iron in yeast.[30]

In yeast and humans, PGRMC1 binds directly to P450 proteins, including CYP51A1, CYP3A4, CYP7A1 and CYP21A2.[11] PGRMC1 also activates Cyp21 when the two proteins are co-expressed,[12][13] indicating that PGRMC1 promotes progesterone turnover. Just as Dap1 is required for the action of Erg11 in the synthesis of ergosterol in yeast, PGRMC1 regulates the Cyp51-catalyzed demethylation step in human cholesterol synthesis.[11] Thus, PGRMC1 and its homologues bind and regulate P450 proteins, and it has been likened to “a helping hand for P450 proteins”.[31]

Roles in signaling and apoptosis edit

The yeast PGRMC1 homologue is required for resistance to damage.[29] PGRMC1 also promotes survival in human cancer cells after treatment with chemotherapy.[6][8] In contrast, PGRMC1 promotes cell death in cancer cells after oxidative damage.[32] PGRMC1 alters several known survival signaling proteins, including the Akt protein kinase and the cell death-associated protein IκB.[32] Progesterone inhibits apoptosis in immortalized granulosa cells, and this activity requires PGRMC1 and its binding partner, PAIR-BP1 (plasminogen activator inhibitor RNA-binding protein-1).[6] However, PAIR-BP1 is not a progesterone binding protein, and the component of the PGRMC1 complex that binds to progesterone is unknown.

PGRMC1 was originally thought to represent a progesterone receptor of some sort and to bind to progesterone, but subsequently thought has moved towards PGRMC1 acting as a downstream mediator of some other progesterone-binding protein.[33]

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101856 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006373 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Meyer C, Schmid R, Scriba PC, Wehling M (Aug 1996). "Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes". European Journal of Biochemistry. 239 (3): 726–31. doi:10.1111/j.1432-1033.1996.0726u.x. PMID 8774719.
  6. ^ a b c d Peluso JJ, Romak J, Liu X (Feb 2008). "Progesterone receptor membrane component-1 (PGRMC1) is the mediator of progesterone's antiapoptotic action in spontaneously immortalized granulosa cells as revealed by PGRMC1 small interfering ribonucleic acid treatment and functional analysis of PGRMC1 mutations". Endocrinology. 149 (2): 534–43. doi:10.1210/en.2007-1050. PMC 2219306. PMID 17991724.
  7. ^ a b c Gerdes D, Wehling M, Leube B, Falkenstein E (Jul 1998). "Cloning and tissue expression of two putative steroid membrane receptors". Biological Chemistry. 379 (7): 907–11. doi:10.1515/bchm.1998.379.7.907. PMID 9705155.
  8. ^ a b Crudden G, Chitti RE, Craven RJ (Jan 2006). "Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs". The Journal of Pharmacology and Experimental Therapeutics. 316 (1): 448–55. doi:10.1124/jpet.105.094631. PMID 16234411. S2CID 18928996.
  9. ^ a b c Ghosh K, Thompson AM, Goldbeck RA, Shi X, Whitman S, Oh E, Zhiwu Z, Vulpe C, Holman TR (Dec 2005). "Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p". Biochemistry. 44 (50): 16729–36. doi:10.1021/bi0511585. PMC 2577039. PMID 16342963.
  10. ^ Mifsud W, Bateman A (2002). "Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain". Genome Biology. 3 (12): RESEARCH0068. doi:10.1186/gb-2002-3-12-research0068. PMC 151170. PMID 12537557.
  11. ^ a b c d e Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ (Feb 2007). "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes". Cell Metabolism. 5 (2): 143–9. doi:10.1016/j.cmet.2006.12.009. PMID 17276356.
  12. ^ a b Min L, Strushkevich NV, Harnastai IN, Iwamoto H, Gilep AA, Takemori H, Usanov SA, Nonaka Y, Hori H, Vinson GP, Okamoto M (Nov 2005). "Molecular identification of adrenal inner zone antigen as a heme-binding protein". The FEBS Journal. 272 (22): 5832–43. doi:10.1111/j.1742-4658.2005.04977.x. PMID 16279947.
  13. ^ a b Min L, Takemori H, Nonaka Y, Katoh Y, Doi J, Horike N, Osamu H, Raza FS, Vinson GP, Okamoto M (Feb 2004). "Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis". Molecular and Cellular Endocrinology. 215 (1–2): 143–8. doi:10.1016/j.mce.2003.11.025. PMID 15026187. S2CID 20640748.
  14. ^ Suchanek M, Radzikowska A, Thiele C (Apr 2005). "Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells". Nature Methods. 2 (4): 261–7. doi:10.1038/nmeth752. PMID 15782218.
  15. ^ Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS (Aug 2002). "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER". Cell. 110 (4): 489–500. doi:10.1016/S0092-8674(02)00872-3. PMID 12202038.
  16. ^ a b c d Krebs CJ, Jarvis ED, Chan J, Lydon JP, Ogawa S, Pfaff DW (Nov 2000). "A membrane-associated progesterone-binding protein, 25-Dx, is regulated by progesterone in brain regions involved in female reproductive behaviors". Proceedings of the National Academy of Sciences of the United States of America. 97 (23): 12816–21. Bibcode:2000PNAS...9712816K. doi:10.1073/pnas.97.23.12816. PMC 18847. PMID 11070092.
  17. ^ a b c Selmin O, Lucier GW, Clark GC, Tritscher AM, Vanden Heuvel JP, Gastel JA, Walker NJ, Sutter TR, Bell DA (Dec 1996). "Isolation and characterization of a novel gene induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver". Carcinogenesis. 17 (12): 2609–15. doi:10.1093/carcin/17.12.2609. PMID 9006096.
  18. ^ Crudden G, Loesel R, Craven RJ (2005). "Overexpression of the cytochrome p450 activator hpr6 (heme-1 domain protein/human progesterone receptor) in tumors". Tumour Biology. 26 (3): 142–6. doi:10.1159/000086485. PMID 15970648. S2CID 2555270.
  19. ^ Peluso JJ, Liu X, Saunders MM, Claffey KP, Phoenix K (May 2008). "Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component-1". The Journal of Clinical Endocrinology and Metabolism. 93 (5): 1592–9. doi:10.1210/jc.2007-2771. PMID 18319313.
  20. ^ Difilippantonio S, Chen Y, Pietas A, Schlüns K, Pacyna-Gengelbach M, Deutschmann N, Padilla-Nash HM, Ried T, Petersen I (Sep 2003). "Gene expression profiles in human non-small and small-cell lung cancers". European Journal of Cancer. 39 (13): 1936–47. doi:10.1016/S0959-8049(03)00419-2. PMID 12932674.
  21. ^ Dressman HK, Hans C, Bild A, Olson JA, Rosen E, Marcom PK, Liotcheva VB, Jones EL, Vujaskovic Z, Marks J, Dewhirst MW, West M, Nevins JR, Blackwell K (Feb 2006). "Gene expression profiles of multiple breast cancer phenotypes and response to neoadjuvant chemotherapy". Clinical Cancer Research. 12 (3 Pt 1): 819–26. doi:10.1158/1078-0432.CCR-05-1447. PMID 16467094.
  22. ^ Irby RB, Malek RL, Bloom G, Tsai J, Letwin N, Frank BC, Verratti K, Yeatman TJ, Lee NH (Mar 2005). "Iterative microarray and RNA interference-based interrogation of the SRC-induced invasive phenotype". Cancer Research. 65 (5): 1814–21. doi:10.1158/0008-5472.CAN-04-3609. PMID 15753379.
  23. ^ Selmin O, Thorne PA, Blachere FM, Johnson PD, Romagnolo DF (Feb 2005). "Transcriptional activation of the membrane-bound progesterone receptor (mPR) by dioxin, in endocrine-responsive tissues". Molecular Reproduction and Development. 70 (2): 166–74. doi:10.1002/mrd.20090. PMID 15570619. S2CID 20023746.
  24. ^ Nilsson EE, Stanfield J, Skinner MK (Dec 2006). "Interactions between progesterone and tumor necrosis factor-alpha in the regulation of primordial follicle assembly". Reproduction. 132 (6): 877–86. doi:10.1530/REP-06-0045. PMC 8260010. PMID 17127748.
  25. ^ Cai Z, Stocco C (Dec 2005). "Expression and regulation of progestin membrane receptors in the rat corpus luteum". Endocrinology. 146 (12): 5522–32. doi:10.1210/en.2005-0759. PMID 16123161.
  26. ^ Meffre D, Delespierre B, Gouézou M, Leclerc P, Vinson GP, Schumacher M, Stein DG, Guennoun R (Jun 2005). "The membrane-associated progesterone-binding protein 25-Dx is expressed in brain regions involved in water homeostasis and is up-regulated after traumatic brain injury". Journal of Neurochemistry. 93 (5): 1314–26. doi:10.1111/j.1471-4159.2005.03127.x. PMID 15934950. S2CID 10107122.
  27. ^ a b c d Mallory JC, Crudden G, Johnson BL, Mo C, Pierson CA, Bard M, Craven RJ (Mar 2005). "Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae". Molecular and Cellular Biology. 25 (5): 1669–79. doi:10.1128/MCB.25.5.1669-1679.2005. PMC 549369. PMID 15713626.
  28. ^ Thompson AM, Reddi AR, Shi X, Goldbeck RA, Moënne-Loccoz P, Gibney BR, Holman TR (Dec 2007). "Measurement of the heme affinity for yeast dap1p, and its importance in cellular function". Biochemistry. 46 (50): 14629–37. doi:10.1021/bi7013739. PMC 2669782. PMID 18031064.
  29. ^ a b c d Hand RA, Jia N, Bard M, Craven RJ (Apr 2003). "Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor". Eukaryotic Cell. 2 (2): 306–17. doi:10.1128/EC.2.2.306-317.2003. PMC 154842. PMID 12684380.
  30. ^ a b Craven RJ, Mallory JC, Hand RA (Dec 2007). "Regulation of iron homeostasis mediated by the heme-binding protein Dap1 (damage resistance protein 1) via the P450 protein Erg11/Cyp51". The Journal of Biological Chemistry. 282 (50): 36543–51. doi:10.1074/jbc.M706770200. PMID 17954932.
  31. ^ Debose-Boyd RA (Feb 2007). "A helping hand for cytochrome p450 enzymes". Cell Metabolism. 5 (2): 81–3. doi:10.1016/j.cmet.2007.01.007. PMID 17276348.
  32. ^ a b Hand RA, Craven RJ (Oct 2003). "Hpr6.6 protein mediates cell death from oxidative damage in MCF-7 human breast cancer cells". Journal of Cellular Biochemistry. 90 (3): 534–47. doi:10.1002/jcb.10648. PMID 14523988. S2CID 24471996.
  33. ^ Cahill MA, Jazayeri JA, Catalano SM, Toyokuni S, Kovacevic Z, Richardson DR (December 2016). "The emerging role of progesterone receptor membrane component 1 (PGRMC1) in cancer biology". Biochim. Biophys. Acta. 1866 (2): 339–349. doi:10.1016/j.bbcan.2016.07.004. PMID 27452206.

pgrmc1, progesterone, receptor, membrane, component, abbreviated, protein, which, purifies, with, progesterone, binding, proteins, liver, ovary, humans, protein, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes4x8yidentifiersalias. Progesterone receptor membrane component 1 abbreviated PGRMC1 is a protein which co purifies with progesterone binding proteins in the liver and ovary 5 6 In humans the PGRMC1 protein is encoded by the PGRMC1 gene 7 PGRMC1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes4X8YIdentifiersAliasesPGRMC1 HPR6 6 MPR progesterone receptor membrane component 1 Dap1 IZAExternal IDsOMIM 300435 MGI 1858305 HomoloGene 48457 GeneCards PGRMC1Gene location Human Chr X chromosome human 1 BandXq24Start119 236 245 bp 1 End119 244 466 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX X A3 3Start35 861 859 bp 2 End35 869 732 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inseminal vesiculacaput epididymiscorpus epididymisbronchial epithelial cellponsendometriummiddle temporal gyruskidney tubulejejunal mucosagerminal epitheliumTop expressed inolfactory epitheliumparaventricular nucleus of hypothalamusarcuate nucleusventromedial nucleussuprachiasmatic nucleusleft lobe of liverdorsomedial hypothalamic nucleuslateral hypothalamusmedian eminencemammillary bodyMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionsteroid binding protein binding heme binding lipid binding amyloid beta bindingCellular componentorganelle membrane integral component of membrane extracellular exosome endoplasmic reticulum membrane endomembrane system membrane intracellular membrane bounded organelle endoplasmic reticulum plasma membrane specific granule membrane integral component of plasma membrane smooth endoplasmic reticulum membrane neuron projection neuronal cell body cell body synapseBiological processneutrophil degranulationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez1085753328EnsemblENSG00000101856ENSMUSG00000006373UniProtO00264Q6IB11O55022RefSeq mRNA NM 006667NM 001282621NM 016783RefSeq protein NP 001269550NP 006658NP 006658 1NP 058063Location UCSC Chr X 119 24 119 24 MbChr X 35 86 35 87 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse The sole biochemical function of PGRMC1 is heme binding 8 9 PGRMC1 shares key structural motifs with cytochrome b5 10 PGRMC1 binds and activates P450 proteins 11 12 13 which are important in drug hormone and lipid metabolism PGRMC1 also binds to PAIR BP1 plasminogen activator inhibitor RNA binding protein 1 6 However its expression outside of the reproductive tract and in males suggests multiple functions for the protein These may include binding to Insig insulin induced gene 14 which regulates cholesterol synthesis 15 Contents 1 Expression 2 Binding to heme and cytochrome P450s 3 Roles in signaling and apoptosis 4 See also 5 ReferencesExpression editPGRMC1 is highly expressed in the liver and kidney in humans 7 with lower expression in the brain lung heart skeletal muscle and pancreas 7 16 17 In rodents PGRMC1 is found in the liver lung kidney and brain 16 17 PGRMC1 is over expressed in breast tumors and in cancer cell lines from the colon thyroid ovary lung and cervix 18 19 Microarray analyses have detected PGRMC1 expression in colon lung and breast tumors 20 21 22 PGRMC1 expression is induced by the non genotoxic carcinogen 2 3 7 8 tetrachlorodibenzo p dioxin in the rat liver 17 but this induction is specific to males 23 PGRMC1 is expressed in the ovary and corpus luteum where its expression is induced by progesterone 24 and during pregnancy 25 respectively PGRMC1 25 Dx is expressed in various regions of the brain hypothalamic area circumventricular organs ependymal cells of the lateral ventricles meninges 16 26 including regions known to facilitate lordosis 16 Binding to heme and cytochrome P450s editThe PGRMC1 yeast homologue Dap1 damage associated protein 1 binds heme 9 27 through a penta coordinate mechanism 9 28 Yeast cells lacking the DAP1 gene are sensitive to DNA damage 29 and heme binding is essential for damage resistance 27 Dap1 is also required for a critical step in cholesterol synthesis in which the P450 protein Erg11 Cyp51 removes a methyl group from lanosterol 11 27 29 30 Erg11 Cyp51 is the target of the azole antifungal drugs As a result yeast cells lacking the DAP1 gene are highly sensitive to antifungal drugs 11 27 29 This function is conserved between the unrelated fungi S cerevisiae and S pombe Dap1 also regulates the metabolism of iron in yeast 30 In yeast and humans PGRMC1 binds directly to P450 proteins including CYP51A1 CYP3A4 CYP7A1 and CYP21A2 11 PGRMC1 also activates Cyp21 when the two proteins are co expressed 12 13 indicating that PGRMC1 promotes progesterone turnover Just as Dap1 is required for the action of Erg11 in the synthesis of ergosterol in yeast PGRMC1 regulates the Cyp51 catalyzed demethylation step in human cholesterol synthesis 11 Thus PGRMC1 and its homologues bind and regulate P450 proteins and it has been likened to a helping hand for P450 proteins 31 Roles in signaling and apoptosis editThe yeast PGRMC1 homologue is required for resistance to damage 29 PGRMC1 also promotes survival in human cancer cells after treatment with chemotherapy 6 8 In contrast PGRMC1 promotes cell death in cancer cells after oxidative damage 32 PGRMC1 alters several known survival signaling proteins including the Akt protein kinase and the cell death associated protein IkB 32 Progesterone inhibits apoptosis in immortalized granulosa cells and this activity requires PGRMC1 and its binding partner PAIR BP1 plasminogen activator inhibitor RNA binding protein 1 6 However PAIR BP1 is not a progesterone binding protein and the component of the PGRMC1 complex that binds to progesterone is unknown PGRMC1 was originally thought to represent a progesterone receptor of some sort and to bind to progesterone but subsequently thought has moved towards PGRMC1 acting as a downstream mediator of some other progesterone binding protein 33 See also editPGRMC PGRMC2 Membrane progesterone receptorReferences edit a b c GRCh38 Ensembl release 89 ENSG00000101856 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000006373 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Meyer C Schmid R Scriba PC Wehling M Aug 1996 Purification and partial sequencing of high affinity progesterone binding site s from porcine liver membranes European Journal of Biochemistry 239 3 726 31 doi 10 1111 j 1432 1033 1996 0726u x PMID 8774719 a b c d Peluso JJ Romak J Liu X Feb 2008 Progesterone receptor membrane component 1 PGRMC1 is the mediator of progesterone s antiapoptotic action in spontaneously immortalized granulosa cells as revealed by PGRMC1 small interfering ribonucleic acid treatment and functional analysis of PGRMC1 mutations Endocrinology 149 2 534 43 doi 10 1210 en 2007 1050 PMC 2219306 PMID 17991724 a b c Gerdes D Wehling M Leube B Falkenstein E Jul 1998 Cloning and tissue expression of two putative steroid membrane receptors Biological Chemistry 379 7 907 11 doi 10 1515 bchm 1998 379 7 907 PMID 9705155 a b Crudden G Chitti RE Craven RJ Jan 2006 Hpr6 heme 1 domain protein regulates the susceptibility of cancer cells to chemotherapeutic drugs The Journal of Pharmacology and Experimental Therapeutics 316 1 448 55 doi 10 1124 jpet 105 094631 PMID 16234411 S2CID 18928996 a b c Ghosh K Thompson AM Goldbeck RA Shi X Whitman S Oh E Zhiwu Z Vulpe C Holman TR Dec 2005 Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p Biochemistry 44 50 16729 36 doi 10 1021 bi0511585 PMC 2577039 PMID 16342963 Mifsud W Bateman A 2002 Membrane bound progesterone receptors contain a cytochrome b5 like ligand binding domain Genome Biology 3 12 RESEARCH0068 doi 10 1186 gb 2002 3 12 research0068 PMC 151170 PMID 12537557 a b c d e Hughes AL Powell DW Bard M Eckstein J Barbuch R Link AJ Espenshade PJ Feb 2007 Dap1 PGRMC1 binds and regulates cytochrome P450 enzymes Cell Metabolism 5 2 143 9 doi 10 1016 j cmet 2006 12 009 PMID 17276356 a b Min L Strushkevich NV Harnastai IN Iwamoto H Gilep AA Takemori H Usanov SA Nonaka Y Hori H Vinson GP Okamoto M Nov 2005 Molecular identification of adrenal inner zone antigen as a heme binding protein The FEBS Journal 272 22 5832 43 doi 10 1111 j 1742 4658 2005 04977 x PMID 16279947 a b Min L Takemori H Nonaka Y Katoh Y Doi J Horike N Osamu H Raza FS Vinson GP Okamoto M Feb 2004 Characterization of the adrenal specific antigen IZA inner zone antigen and its role in the steroidogenesis Molecular and Cellular Endocrinology 215 1 2 143 8 doi 10 1016 j mce 2003 11 025 PMID 15026187 S2CID 20640748 Suchanek M Radzikowska A Thiele C Apr 2005 Photo leucine and photo methionine allow identification of protein protein interactions in living cells Nature Methods 2 4 261 7 doi 10 1038 nmeth752 PMID 15782218 Yang T Espenshade PJ Wright ME Yabe D Gong Y Aebersold R Goldstein JL Brown MS Aug 2002 Crucial step in cholesterol homeostasis sterols promote binding of SCAP to INSIG 1 a membrane protein that facilitates retention of SREBPs in ER Cell 110 4 489 500 doi 10 1016 S0092 8674 02 00872 3 PMID 12202038 a b c d Krebs CJ Jarvis ED Chan J Lydon JP Ogawa S Pfaff DW Nov 2000 A membrane associated progesterone binding protein 25 Dx is regulated by progesterone in brain regions involved in female reproductive behaviors Proceedings of the National Academy of Sciences of the United States of America 97 23 12816 21 Bibcode 2000PNAS 9712816K doi 10 1073 pnas 97 23 12816 PMC 18847 PMID 11070092 a b c Selmin O Lucier GW Clark GC Tritscher AM Vanden Heuvel JP Gastel JA Walker NJ Sutter TR Bell DA Dec 1996 Isolation and characterization of a novel gene induced by 2 3 7 8 tetrachlorodibenzo p dioxin in rat liver Carcinogenesis 17 12 2609 15 doi 10 1093 carcin 17 12 2609 PMID 9006096 Crudden G Loesel R Craven RJ 2005 Overexpression of the cytochrome p450 activator hpr6 heme 1 domain protein human progesterone receptor in tumors Tumour Biology 26 3 142 6 doi 10 1159 000086485 PMID 15970648 S2CID 2555270 Peluso JJ Liu X Saunders MM Claffey KP Phoenix K May 2008 Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component 1 The Journal of Clinical Endocrinology and Metabolism 93 5 1592 9 doi 10 1210 jc 2007 2771 PMID 18319313 Difilippantonio S Chen Y Pietas A Schluns K Pacyna Gengelbach M Deutschmann N Padilla Nash HM Ried T Petersen I Sep 2003 Gene expression profiles in human non small and small cell lung cancers European Journal of Cancer 39 13 1936 47 doi 10 1016 S0959 8049 03 00419 2 PMID 12932674 Dressman HK Hans C Bild A Olson JA Rosen E Marcom PK Liotcheva VB Jones EL Vujaskovic Z Marks J Dewhirst MW West M Nevins JR Blackwell K Feb 2006 Gene expression profiles of multiple breast cancer phenotypes and response to neoadjuvant chemotherapy Clinical Cancer Research 12 3 Pt 1 819 26 doi 10 1158 1078 0432 CCR 05 1447 PMID 16467094 Irby RB Malek RL Bloom G Tsai J Letwin N Frank BC Verratti K Yeatman TJ Lee NH Mar 2005 Iterative microarray and RNA interference based interrogation of the SRC induced invasive phenotype Cancer Research 65 5 1814 21 doi 10 1158 0008 5472 CAN 04 3609 PMID 15753379 Selmin O Thorne PA Blachere FM Johnson PD Romagnolo DF Feb 2005 Transcriptional activation of the membrane bound progesterone receptor mPR by dioxin in endocrine responsive tissues Molecular Reproduction and Development 70 2 166 74 doi 10 1002 mrd 20090 PMID 15570619 S2CID 20023746 Nilsson EE Stanfield J Skinner MK Dec 2006 Interactions between progesterone and tumor necrosis factor alpha in the regulation of primordial follicle assembly Reproduction 132 6 877 86 doi 10 1530 REP 06 0045 PMC 8260010 PMID 17127748 Cai Z Stocco C Dec 2005 Expression and regulation of progestin membrane receptors in the rat corpus luteum Endocrinology 146 12 5522 32 doi 10 1210 en 2005 0759 PMID 16123161 Meffre D Delespierre B Gouezou M Leclerc P Vinson GP Schumacher M Stein DG Guennoun R Jun 2005 The membrane associated progesterone binding protein 25 Dx is expressed in brain regions involved in water homeostasis and is up regulated after traumatic brain injury Journal of Neurochemistry 93 5 1314 26 doi 10 1111 j 1471 4159 2005 03127 x PMID 15934950 S2CID 10107122 a b c d Mallory JC Crudden G Johnson BL Mo C Pierson CA Bard M Craven RJ Mar 2005 Dap1p a heme binding protein that regulates the cytochrome P450 protein Erg11p Cyp51p in Saccharomyces cerevisiae Molecular and Cellular Biology 25 5 1669 79 doi 10 1128 MCB 25 5 1669 1679 2005 PMC 549369 PMID 15713626 Thompson AM Reddi AR Shi X Goldbeck RA Moenne Loccoz P Gibney BR Holman TR Dec 2007 Measurement of the heme affinity for yeast dap1p and its importance in cellular function Biochemistry 46 50 14629 37 doi 10 1021 bi7013739 PMC 2669782 PMID 18031064 a b c d Hand RA Jia N Bard M Craven RJ Apr 2003 Saccharomyces cerevisiae Dap1p a novel DNA damage response protein related to the mammalian membrane associated progesterone receptor Eukaryotic Cell 2 2 306 17 doi 10 1128 EC 2 2 306 317 2003 PMC 154842 PMID 12684380 a b Craven RJ Mallory JC Hand RA Dec 2007 Regulation of iron homeostasis mediated by the heme binding protein Dap1 damage resistance protein 1 via the P450 protein Erg11 Cyp51 The Journal of Biological Chemistry 282 50 36543 51 doi 10 1074 jbc M706770200 PMID 17954932 Debose Boyd RA Feb 2007 A helping hand for cytochrome p450 enzymes Cell Metabolism 5 2 81 3 doi 10 1016 j cmet 2007 01 007 PMID 17276348 a b Hand RA Craven RJ Oct 2003 Hpr6 6 protein mediates cell death from oxidative damage in MCF 7 human breast cancer cells Journal of Cellular Biochemistry 90 3 534 47 doi 10 1002 jcb 10648 PMID 14523988 S2CID 24471996 Cahill MA Jazayeri JA Catalano SM Toyokuni S Kovacevic Z Richardson DR December 2016 The emerging role of progesterone receptor membrane component 1 PGRMC1 in cancer biology Biochim Biophys Acta 1866 2 339 349 doi 10 1016 j bbcan 2016 07 004 PMID 27452206 Retrieved from https en wikipedia org w index php title PGRMC1 amp oldid 1188053199, wikipedia, wiki, book, books, library,

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