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{{PBB|geneid=10857}}
{{PBB|geneid=10857}}
'''Progesterone receptor membrane component 1''' (abbreviated '''PGRMC1''') is a [[protein]] which co-purifies with progesterone binding proteins in the liver and ovary.<ref>Meyer, C, Schmid, R, Scriba, PC, Wehling, M (1996) Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes. Eur J Biochem 239(3): 726-731.</ref><ref name="peluso2008b">Peluso, JJ, Romak, J, Liu, X (2008b) 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): 534-543.>> </ref> The sole biochemical function of PGRMC1 is [[heme]]-binding,<ref name="crudden2006">Crudden, G, Chitti, RE, Craven, RJ (2006) Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs. J Pharmacol Exp Ther 316(1): 448-455</ref><ref name="ghosh2005">Ghosh, K, Thompson, AM, Goldbeck, RA, Shi, X, Whitman, S, Oh, E, Zhiwu, Z, Vulpe, C, Holman, TR (2005) Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p. Biochemistry 44(50): 16729-16736.</ref>and PGRMC1 shares key structural motifs with [[cytochrome b<sub>5</sub>]]<ref>Mifsud, W, Bateman, A (2002) Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain. Genome Biol 3(12): RESEARCH0068.</ref> a heme binding protein that activates [[cytochrome P450]] proteins.<ref>Schenkman, JB, Jansson, I (2003) The many roles of cytochrome b5. Pharmacology & therapeutics 97(2): 139-152.</ref> PGRMC1 binds and activates P450 proteins<ref name="hughes2007">Hughes, AL, Powell, DW, Bard, M, Eckstein, J, Barbuch, R, Link, AJ, Espenshade, PJ (2007) Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes. Cell Metab 5(2): 143-149.</ref><ref>Min, L, Strushkevich, NV, Harnastai, IN, Iwamoto, H, Gilep, AA, Takemori, H, Usanov, SA, Nonaka, Y, Hori, H, Vinson, GP, Okamoto, M (2005) Molecular identification of adrenal inner zone antigen as a heme-binding protein. Febs J 272(22): 5832-5843.</ref><ref name="min2004">Min, L, Takemori, H, Nonaka, Y, Katoh, Y, Doi, J, Horike, N, Osamu, H, Raza, FS, Vinson, GP, Okamoto, M (2004) Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis. Mol Cell Endocrinol 215(1-2): 143-148.</ref>, which are important in drug, hormone and lipid metabolism. PGRMC1 also binds to PAIRBP1 [plasminogen activator inhibitor 1 [[mRNA]] binding protein<ref name="peluso2008b" /> 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 <ref>Suchanek, M, Radzikowska, A, Thiele, C (2005) Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat Methods 2(4): 261-267.</ref>], which regulates cholesterol synthesis <ref>Yang, T, Espenshade, PJ, Wright, ME, Yabe, D, Gong, Y, Aebersold, R, Goldstein, JL, Brown, MS (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.</ref>.
'''Progesterone receptor membrane component 1''' (abbreviated '''PGRMC1''') is a [[protein]] which co-purifies with progesterone binding proteins in the liver and ovary.<ref name="pmid8774719">{{cite journal | author = Meyer C, Schmid R, Scriba PC, Wehling M | title = Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes | journal = Eur. J. Biochem. | volume = 239 | issue = 3 | pages = 726–31 | year = 1996 | month = August | pmid = 8774719 | url = http://www.blackwell-synergy.com/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1996&volume=239&issue=3&spage=726 | issn = }}</ref><ref name="peluso2008b">{{cite journal | author = Peluso JJ, Romak J, Liu X | title = 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 | journal = Endocrinology | volume = 149 | issue = 2 | pages = 534–43 | year = 2008 | month = February | pmid = 17991724 | doi = 10.1210/en.2007-1050 | url = | issn = }}</ref> 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.<ref name="peluso2008b"/>

The sole biochemical function of PGRMC1 is [[heme]]-binding.<ref name="crudden2006">{{cite journal | author = Crudden G, Chitti RE, Craven RJ | title = Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs | journal = J. Pharmacol. Exp. Ther. | volume = 316 | issue = 1 | pages = 448–55 | year = 2006 | month = January | pmid = 16234411 | doi = 10.1124/jpet.105.094631 | url = | issn = }}</ref><ref name="ghosh2005">{{cite journal | author = Ghosh K, Thompson AM, Goldbeck RA, Shi X, Whitman S, Oh E, Zhiwu Z, Vulpe C, Holman TR | title = Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p | journal = Biochemistry | volume = 44 | issue = 50 | pages = 16729–36 | year = 2005 | month = December | pmid = 16342963 | doi = 10.1021/bi0511585 | url = | issn = }}</ref> PGRMC1 shares key structural motifs with [[cytochrome b5|cytochrome b<sub>5</sub>]].<ref name="pmid12537557">{{cite journal | author = Mifsud W, Bateman A | title = Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain | journal = Genome Biol. | volume = 3 | issue = 12 | pages = RESEARCH0068 | year = 2002 | pmid = 12537557 | pmc = 151170 | url = http://genomebiology.com/1465-6906/3/RESEARCH0068 | issn = }}</ref> PGRMC1 binds and activates P450 proteins,<ref name="hughes2007">{{cite journal | author = Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ | title = Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes | journal = Cell Metab. | volume = 5 | issue = 2 | pages = 143–9 | year = 2007 | month = February | pmid = 17276356 | doi = 10.1016/j.cmet.2006.12.009 | url = | issn = }}</ref><ref name="pmid16279947">{{cite journal | author = Min L, Strushkevich NV, Harnastai IN, Iwamoto H, Gilep AA, Takemori H, Usanov SA, Nonaka Y, Hori H, Vinson GP, Okamoto M | title = Molecular identification of adrenal inner zone antigen as a heme-binding protein | journal = FEBS J. | volume = 272 | issue = 22 | pages = 5832–43 | year = 2005 | month = November | pmid = 16279947 | doi = 10.1111/j.1742-4658.2005.04977.x | url = | issn = }}</ref><ref name="min2004">{{cite journal | author = Min L, Takemori H, Nonaka Y, Katoh Y, Doi J, Horike N, Osamu H, Raza FS, Vinson GP, Okamoto M | title = Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis | journal = Mol. Cell. Endocrinol. | volume = 215 | issue = 1-2 | pages = 143–8 | year = 2004 | month = February | pmid = 15026187 | doi = 10.1016/j.mce.2003.11.025 | url = | issn = }}</ref> which are important in drug, hormone and lipid metabolism. PGRMC1 also binds to PAIRBP1 [plasminogen activator inhibitor 1 [[mRNA]] binding protein.<ref name="peluso2008b" /> 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),<ref name="pmid15782218">{{cite journal | author = Suchanek M, Radzikowska A, Thiele C | title = Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells | journal = Nat. Methods | volume = 2 | issue = 4 | pages = 261–7 | year = 2005 | month = April | pmid = 15782218 | doi = 10.1038/nmeth752 | url = | issn = }}</ref> which regulates cholesterol synthesis.<ref name="pmid12202038">{{cite journal | author =Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS | title = Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER | journal = Cell | volume = 110 | issue = 4 | pages = 489–500 | year = 2002 | month = August | pmid = 12202038 | doi = | url = http://linkinghub.elsevier.com/retrieve/pii/S0092867402008723 | issn = }}</ref>


==Expression==
==Expression==
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<ref name="hand2003b" /><ref name="hughes2007">
<ref name="hand2003b" /><ref name="hughes2007">
<ref>Mallory, JC, Crudden, G, Johnson, BL, Mo, C, Pierson, CA, Bard, M, Craven, RJ (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5): 1669-1679. </ref>. 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 <ref name="hand2003b" /><ref name="hughes2007"><ref>Mallory, JC, Crudden, G, Johnson, BL, Mo, C, Pierson, CA, Bard, M, Craven, RJ (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5): 1669-1679. </ref>. This function is conserved between the unrelated fungi [[Saccharomyces cerevisiae]] and [[Schizosaccharomyces pombe]]. Dap1 also regulates the metabolism of iron in yeast <ref name="craven2007" />.
<ref>Mallory, JC, Crudden, G, Johnson, BL, Mo, C, Pierson, CA, Bard, M, Craven, RJ (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5): 1669-1679. </ref>. 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 <ref name="hand2003b" /><ref name="hughes2007"><ref>Mallory, JC, Crudden, G, Johnson, BL, Mo, C, Pierson, CA, Bard, M, Craven, RJ (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5): 1669-1679. </ref>. This function is conserved between the unrelated fungi [[Saccharomyces cerevisiae]] and [[Schizosaccharomyces pombe]]. Dap1 also regulates the metabolism of iron in yeast <ref name="craven2007" />.
In yeast and humans, PGRMC1 binds directly to P450 proteins, including [[Cyp51]], [[Cyp3A4]], [[Cyp7A1]] and [[Cyp21A2]] <ref name="hughes2007">. PGRMC1 also activates Cyp21 when the two proteins are co-expressed <ref>Min, L, Strushkevich, NV, Harnastai, IN, Iwamoto, H, Gilep, AA, Takemori, H, Usanov, SA, Nonaka, Y, Hori, H, Vinson, GP, Okamoto, M (2005) Molecular identification of adrenal inner zone antigen as a heme-binding protein. Febs J 272(22): 5832-5843. </ref><ref name="min2004" />, indicating that PGRMC1 promotes progesterone turnover. Just as Dap1 is required for the action of Erg11 in the sythesis of ergosterol in yeast, PGRMC1 regulates the Cyp51-catalyzed demethylation step in human cholesterol synthesis <ref name="hughes2007">. Thus, PGRMC1 and its homologues bind and regulate P450 proteins, and it has been likened to “a helping hand for P450 proteins” <ref>Debose-Boyd, RA (2007) A helping hand for cytochrome p450 enzymes. Cell Metab 5(2): 81-83. </ref>.
In yeast and humans, PGRMC1 binds directly to P450 proteins, including [[CYP51A1]], [[CYP3A4]], [[CYP7A1]] and [[CYP21A2]] <ref name="hughes2007">. PGRMC1 also activates Cyp21 when the two proteins are co-expressed <ref>Min, L, Strushkevich, NV, Harnastai, IN, Iwamoto, H, Gilep, AA, Takemori, H, Usanov, SA, Nonaka, Y, Hori, H, Vinson, GP, Okamoto, M (2005) Molecular identification of adrenal inner zone antigen as a heme-binding protein. Febs J 272(22): 5832-5843. </ref><ref name="min2004" />, indicating that PGRMC1 promotes progesterone turnover. Just as Dap1 is required for the action of Erg11 in the sythesis of ergosterol in yeast, PGRMC1 regulates the Cyp51-catalyzed demethylation step in human cholesterol synthesis <ref name="hughes2007">. Thus, PGRMC1 and its homologues bind and regulate P450 proteins, and it has been likened to “a helping hand for P450 proteins” <ref>Debose-Boyd, RA (2007) A helping hand for cytochrome p450 enzymes. Cell Metab 5(2): 81-83. </ref>.


==Roles in signaling and apoptosis==
==Roles in signaling and apoptosis==
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==References==
==References==
{{reflist}}
{{Reflist|2}}




Revision as of 20:48, 16 July 2008

Template:PBB Progesterone receptor membrane component 1 (abbreviated PGRMC1) is a protein which co-purifies with progesterone binding proteins in the liver and ovary.[1][2] 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.[2]

The sole biochemical function of PGRMC1 is heme-binding.[3][4] PGRMC1 shares key structural motifs with cytochrome b5.[5] PGRMC1 binds and activates P450 proteins,[6][7][8] which are important in drug, hormone and lipid metabolism. PGRMC1 also binds to PAIRBP1 [plasminogen activator inhibitor 1 mRNA binding protein.[2] 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),[9] which regulates cholesterol synthesis.[10]

Expression

PGRMC1 is highly expressed in the liver and kidney in humans [11] with lower expression in the brain, lung, heart, skeletal muscle and pancreas [11] [12] [13]. In rodents, PGRMC1 is found in the liver, lung, kidney and brain [12] [13]. PGRMC1 is over-expressed in breast tumors and in cancer cell lines from the colon, thyroid, ovary, lung, and cervix [14] [15]. Microarray analyses have detected PGRMC1 expression in colon, lung and breast tumors [16] [17] [18]. PGRMC1 expression is induced by the non-genotoxic carcinogen 2,3,7,8-tetrachlorodibenzo-p-Dioxin in the rat liver [13], but this induction is specific to males [19]. PGRMC1 is expressed in the ovary and corpus luteum, where its expression is induced by progesterone [20] and during pregnancy [21], respectively. PGRMC1/25-Dx is expressed in various regions of the brain [hypothalamic area, circumventricular organs, ependymal cells of the lateral ventricles, meninges[12][22]], including regions known to facilitate lordosis [12].

PGRMC1 binding to heme and P450s is conserved from yeast to humans

The PGRMC1 yeast homologue, Dap1 (damage associated protein 1), binds heme [4][23] through a penta-coordinate mechanism [4] [24]. Yeast cells lacking the DAP1 gene are sensitive to DNA damage [25], and heme-binding is essential for damage resistance [23]. Dap1 is also required for a critical step in cholesterol synthesis in which the P450 protein Erg11/Cyp51 removes a methyl group from lanosterol [26] [25]Cite error: A <ref> tag is missing the closing </ref> (see the help page).. 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 [25]Cite error: A <ref> tag is missing the closing </ref> (see the help page).. This function is conserved between the unrelated fungi Saccharomyces cerevisiae and Schizosaccharomyces pombe. Dap1 also regulates the metabolism of iron in yeast [26]. In yeast and humans, PGRMC1 binds directly to P450 proteins, including CYP51A1, CYP3A4, CYP7A1 and CYP21A2 Cite error: A <ref> tag is missing the closing </ref> (see the help page).[8], indicating that PGRMC1 promotes progesterone turnover. Just as Dap1 is required for the action of Erg11 in the sythesis of ergosterol in yeast, PGRMC1 regulates the Cyp51-catalyzed demethylation step in human cholesterol synthesis Cite error: A <ref> tag is missing the closing </ref> (see the help page)..

Roles in signaling and apoptosis

The yeast PGRMC1 homologue is required for resistance to damage [25]. PGRMC1 also promotes survival in human cancer cells after treatment with chemotherapy [3] [2]. In contrast, PGRMC1 promotes cell death in cancer cells after oxidative damage [27]. PGRMC1 alters several known survival signaling proteins, including the Akt protein kinase and the cell death-associated protein IκB [27]. Progesterone inhibits apoptosis in immortalized granulosa cells, and this activity requires PGRMC1 and its binding partner, PAIRBP1 [plasminogen activator inhibitor 1 mRNA binding protein [2]]. However, PAIR-BP1 is not a progesterone binding protein, and the component of the PGRMC1 complex that binds to progesterone is unknown.

References

  1. ^ Meyer C, Schmid R, Scriba PC, Wehling M (1996). "Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes". Eur. J. Biochem. 239 (3): 726–31. PMID 8774719. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ a b c d e Peluso JJ, Romak J, Liu X (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. PMID 17991724. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ a b Crudden G, Chitti RE, Craven RJ (2006). "Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs". J. Pharmacol. Exp. Ther. 316 (1): 448–55. doi:10.1124/jpet.105.094631. PMID 16234411. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ a b c Ghosh K, Thompson AM, Goldbeck RA, Shi X, Whitman S, Oh E, Zhiwu Z, Vulpe C, Holman TR (2005). "Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p". Biochemistry. 44 (50): 16729–36. doi:10.1021/bi0511585. PMID 16342963. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  5. ^ Mifsud W, Bateman A (2002). "Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain". Genome Biol. 3 (12): RESEARCH0068. PMC 151170. PMID 12537557.
  6. ^ Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ (2007). "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes". Cell Metab. 5 (2): 143–9. doi:10.1016/j.cmet.2006.12.009. PMID 17276356. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  7. ^ Min L, Strushkevich NV, Harnastai IN, Iwamoto H, Gilep AA, Takemori H, Usanov SA, Nonaka Y, Hori H, Vinson GP, Okamoto M (2005). "Molecular identification of adrenal inner zone antigen as a heme-binding protein". FEBS J. 272 (22): 5832–43. doi:10.1111/j.1742-4658.2005.04977.x. PMID 16279947. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  8. ^ a b Min L, Takemori H, Nonaka Y, Katoh Y, Doi J, Horike N, Osamu H, Raza FS, Vinson GP, Okamoto M (2004). "Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis". Mol. Cell. Endocrinol. 215 (1–2): 143–8. doi:10.1016/j.mce.2003.11.025. PMID 15026187. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  9. ^ Suchanek M, Radzikowska A, Thiele C (2005). "Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells". Nat. Methods. 2 (4): 261–7. doi:10.1038/nmeth752. PMID 15782218. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  10. ^ Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS (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. PMID 12202038. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  11. ^ a b Gerdes, D, Wehling, M, Leube, B, Falkenstein, E (1998) Cloning and tissue expression of two putative steroid membrane receptors. Biol Chem 379(7): 907-911.
  12. ^ a b c d Krebs, CJ, Jarvis, ED, Chan, J, Lydon, JP, Ogawa, S, Pfaff, DW (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): 12816-12821.
  13. ^ a b c Selmin, O, Lucier, GW, Clark, GC, Tritscher, AM, Vanden Heuvel, JP, Gastel, JA, Walker, NJ, Sutter, TR, Bell, DA (1996) Isolation and characterization of a novel gene induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver. Carcinogenesis 17(12): 2609-2615.
  14. ^ Crudden, G, Loesel, R, Craven, RJ (2005) Overexpression of the cytochrome p450 activator hpr6 (heme-1 domain protein/human progesterone receptor) in tumors. Tumour Biol 26(3): 142-146.
  15. ^ Peluso, JJ, Liu, X, Saunders, MM, Claffey, KP, Phoenix, K (2008a) Regulation of ovarian cancer cell viability and sensitivity to cisplatin by progesterone receptor membrane component-1. J Clin Endocrinol Metab 93(5): 1592-1599.
  16. ^ Difilippantonio, S, Chen, Y, Pietas, A, Schluns, K, Pacyna-Gengelbach, M, Deutschmann, N, Padilla-Nash, HM, Ried, T, Petersen, I (2003) Gene expression profiles in human non-small and small-cell lung cancers. Eur J Cancer 39(13): 1936-1947.
  17. ^ 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 (2006) Gene expression profiles of multiple breast cancer phenotypes and response to neoadjuvant chemotherapy. Clin Cancer Res 12(3 Pt 1): 819-826.
  18. ^ Irby, RB, Malek, RL, Bloom, G, Tsai, J, Letwin, N, Frank, BC, Verratti, K, Yeatman, TJ, Lee, NH (2005) Iterative microarray and RNA interference-based interrogation of the SRC-induced invasive phenotype. Cancer research 65(5): 1814-1821.
  19. ^ Selmin, O, Thorne, PA, Blachere, FM, Johnson, PD, Romagnolo, DF (2005) Transcriptional activation of the membrane-bound progesterone receptor (mPR) by dioxin, in endocrine-responsive tissues. Molecular reproduction and development 70(2): 166-174.
  20. ^ Nilsson, EE, Stanfield, J, Skinner, MK (2006) Interactions between progesterone and tumor necrosis factor-alpha in the regulation of primordial follicle assembly. Reproduction (Cambridge, England) 132(6): 877-886.
  21. ^ Cai, Z, Stocco, C (2005) Expression and regulation of progestin membrane receptors in the rat corpus luteum. Endocrinology 146(12): 5522-5532.
  22. ^ Meffre, D, Delespierre, B, Gouezou, M, Leclerc, P, Vinson, GP, Schumacher, M, Stein, DG, Guennoun, R (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): 1314-1326.
  23. ^ a b Mallory, JC, Crudden, G, Johnson, BL, Mo, C, Pierson, CA, Bard, M, Craven, RJ (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae. Mol Cell Biol 25(5): 1669-1679.
  24. ^ Thompson, AM, Reddi, AR, Shi, X, Goldbeck, RA, Moenne-Loccoz, P, Gibney, BR, Holman, TR (2007) Measurement of the Heme Affinity for Yeast Dap1p, and Its Importance in Cellular Function. Biochemistry.
  25. ^ a b c d Hand, RA, Jia, N, Bard, M, Craven, RJ (2003b) Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor. Eukaryot Cell 2(2): 306-317.
  26. ^ a b Craven, RJ, Mallory, JC, Hand, RA (2007) Regulation of iron homeostasis mediated by the heme-binding protein Dap1 (damage resistance protein 1) via the P450 protein Erg11/Cyp51. J Biol Chem 282(50): 36543-36551.
  27. ^ a b Hand, RA, Craven, RJ (2003a) Hpr6.6 protein mediates cell death from oxidative damage in MCF-7 human breast cancer cells. J Cell Biochem 90(3): 534-547.


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Quelle: https://en.wikipedia.org/wiki/Special%3ADiff%2F226101395