메뉴 건너뛰기




Volumn 151, Issue 6, 2010, Pages 2819-2825

Insulin-like growth factor-I activates extracellularly regulated kinase to regulate the P450 side-chain cleavage insulin-like response element in granulosa cells

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; SOMATOMEDIN C; TRANSCRIPTION FACTOR SP1; 1,3 BUTADIENE DERIVATIVE; ENZYME INHIBITOR; NITRILE; PTB ASSOCIATED SPLICING FACTOR; PTB-ASSOCIATED SPLICING FACTOR; RNA BINDING PROTEIN;

EID: 77954468984     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2009-1439     Document Type: Article
Times cited : (11)

References (39)
  • 2
    • 0027017054 scopus 로고
    • Intraovarian regulation: The IGF-I example
    • Adashi EY 1992 Intraovarian regulation: the IGF-I example. Reprod Fertil Dev 4:497-504
    • (1992) Reprod Fertil Dev , vol.4 , pp. 497-504
    • Adashi, E.Y.1
  • 3
    • 0026521263 scopus 로고
    • Intraovarian peptides. Stimulators and inhibitors of follicular growth and differentiation
    • Adashi EY 1992 Intraovarian peptides. Stimulators and inhibitors of follicular growth and differentiation. Endocrinol Metab Clin North Am 21:1-17
    • (1992) Endocrinol Metab Clin North Am , vol.21 , pp. 1-17
    • Adashi, E.Y.1
  • 4
    • 0024064517 scopus 로고
    • Molecular biology of steroid hormone synthesis
    • Miller WL 1988 Molecular biology of steroid hormone synthesis. Endocr Rev 9:295-318
    • (1988) Endocr Rev , vol.9 , pp. 295-318
    • Miller, W.L.1
  • 5
    • 41549117586 scopus 로고    scopus 로고
    • Insulin-like growth factor-I regulates Kruppel-like factor-6 gene expression in a p53-dependent manner
    • DOI 10.1210/en.2007-0844
    • Bentov I, Narla G, Schayek H, Akita K, Plymate SR, LeRoith D, Friedman SL, Werner H 2008 Insulin-like growth factor-I regulates Kruppel-like factor-6 gene expression in a p53-dependent manner. Endocrinology 149:1890-1897 (Pubitemid 351468329)
    • (2008) Endocrinology , vol.149 , Issue.4 , pp. 1890-1897
    • Bentov, I.1    Narla, G.2    Schayek, H.3    Akita, K.4    Plymate, S.R.5    Leroith, D.6    Friedman, S.L.7    Werner, H.8
  • 6
    • 33846874575 scopus 로고    scopus 로고
    • The role of the IGF system in cancer growth and metastasis: Overview and recent insights
    • DOI 10.1210/er.2006-0001
    • Samani AA, Yakar S, LeRoith D, Brodt P 2007 The role of the IGF system in cancer growth and metastasis: overview and recent insights. Endocr Rev 28:20-47 (Pubitemid 46220849)
    • (2007) Endocrine Reviews , vol.28 , Issue.1 , pp. 20-47
    • Samani, A.A.1    Yakar, S.2    Leroith, D.3    Brodt, P.4
  • 7
    • 0038071783 scopus 로고    scopus 로고
    • Minireview: Integral membrane proteins that function coordinately with the insulin-like growth factor I receptor to regulate intracellular signaling
    • Clemmons DR, Maile LA 2003 Minireview: integral membrane proteins that function coordinately with the insulin-like growth factor I receptor to regulate intracellular signaling. Endocrinology 144:1664-1670
    • (2003) Endocrinology , vol.144 , pp. 1664-1670
    • Clemmons, D.R.1    Maile, L.A.2
  • 8
    • 34247377842 scopus 로고    scopus 로고
    • Regulation of Leydig cell steroidogenesis by extracellular signal-regulated kinase 1/2: Role of protein kinase a and protein kinase C signaling
    • DOI 10.1677/JOE-06-0201
    • Manna PR, Jo Y, Stocco DM 2007 Regulation of Leydig cell steroidogenesis by extracellular signal-regulated kinase 1/2: role of protein kinase A and protein kinase C signaling. J Endocrinol 193:53-63 (Pubitemid 46638532)
    • (2007) Journal of Endocrinology , vol.193 , Issue.1 , pp. 53-63
    • Manna, P.R.1    Jo, Y.2    Stocco, D.M.3
  • 9
    • 33747880805 scopus 로고    scopus 로고
    • CAMP-independent signaling regulates steroidogenesis in mouse Leydig cells in the absence of StAR phosphorylation
    • DOI 10.1677/jme.1.02065
    • Manna PR, Chandrala SP, Jo Y, Stocco DM 2006 cAMP-independent signaling regulates steroidogenesis in mouse Leydig cells in the absence of StAR phosphorylation. J Mol Endocrinol 37:81-95 (Pubitemid 44288608)
    • (2006) Journal of Molecular Endocrinology , vol.37 , Issue.1 , pp. 81-95
    • Manna, P.R.1    Chandrala, S.P.2    Jo, Y.3    Stocco, D.M.4
  • 10
    • 31444442754 scopus 로고    scopus 로고
    • Molecular mechanisms of insulin-like growth factor-I mediated regulation of the steroidogenic acute regulatory protein in mouse leydig cells
    • DOI 10.1210/me.2004-0526
    • Manna PR, Chandrala SP, King SR, Jo Y, Counis R, Huhtaniemi IT, Stocco DM 2006 Molecular mechanisms of insulin-like growth factor-I mediated regulation of the steroidogenic acute regulatory protein in mouse leydig cells. Mol Endocrinol 20:362-378 (Pubitemid 43152510)
    • (2006) Molecular Endocrinology , vol.20 , Issue.2 , pp. 362-378
    • Manna, P.R.1    Chandrala, S.P.2    King, S.R.3    Jo, Y.4    Counis, R.5    Huhtaniemi, I.T.6    Stocco, D.M.7
  • 11
    • 27644505023 scopus 로고    scopus 로고
    • Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: More complicated than we thought
    • DOI 10.1210/me.2004-0532
    • Stocco DM, Wang X, Jo Y, Manna PR 2005 Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: more complicated than we thought. Mol Endocrinol 19:2647-2659 (Pubitemid 41577240)
    • (2005) Molecular Endocrinology , vol.19 , Issue.11 , pp. 2647-2659
    • Stocco, D.M.1    Wang, X.2    Jo, Y.3    Manna, P.R.4
  • 12
    • 0025187814 scopus 로고
    • Insulin-like growth factor type I increases concentrations of messenger ribonucleic acid encoding cytochrome P450 cholesterol side-chain cleavage enzyme in primary cultures of porcine granulosa cells
    • Urban RJ, Garmey JC, Shupnik MA, Veldhuis JD 1990 Insulin-like growth factor type I increases concentrations of messenger ribonucleic acid encoding cytochrome P450 cholesterol side-chain cleavage enzyme in primary cultures of porcine granulosa cells. Endocrinology 127:2481-2488
    • (1990) Endocrinology , vol.127 , pp. 2481-2488
    • Urban, R.J.1    Garmey, J.C.2    Shupnik, M.A.3    Veldhuis, J.D.4
  • 13
    • 53649110719 scopus 로고    scopus 로고
    • Identification of ERK and JNK as signaling mediators on protein kinase C activation in cultured granulosa cells
    • Sriraman V, Modi SR, Bodenburg Y, Denner LA, Urban RJ 2008 Identification of ERK and JNK as signaling mediators on protein kinase C activation in cultured granulosa cells. Mol Cell Endocrinol 294:52-60
    • (2008) Mol Cell Endocrinol , vol.294 , pp. 52-60
    • Sriraman, V.1    Modi, S.R.2    Bodenburg, Y.3    Denner, L.A.4    Urban, R.J.5
  • 14
    • 0036919459 scopus 로고    scopus 로고
    • Role of Sp1 in insulin regulation of gene expression
    • DOI 10.1677/jme.0.0290265
    • Samson SL, Wong NC 2002 Role of Sp1 in insulin regulation of gene expression. J Mol Endocrinol 29:265-279 (Pubitemid 36024543)
    • (2002) Journal of Molecular Endocrinology , vol.29 , Issue.3 , pp. 265-279
    • Samson, S.L.-A.1    Wong, N.C.W.2
  • 15
    • 0036786497 scopus 로고    scopus 로고
    • PTB-associated splicing factor regulates growth factor-stimulated gene expression in mammalian cells
    • Urban RJ, Bodenburg Y 2002 PTB-associated splicing factor regulates growth factor-stimulated gene expression in mammalian cells. Am J Physiol Endocrinol Metab 283:E794-E798
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • Urban, R.J.1    Bodenburg, Y.2
  • 16
    • 0033972421 scopus 로고    scopus 로고
    • Expression and regulatory function of the transcription factor Sp1 in the uterine endometrium at early pregnancy: Implications for epithelial phenotype
    • DOI 10.1016/S0303-7207(99)00191-4, PII S0303720799001914
    • Simmen RC, Zhang XL, Zhang D, Wang Y, Michel FJ, Simmen FA 2000 Expression and regulatory function of the transcription factor Sp1 in the uterine endometrium at early pregnancy: implications for epithelial phenotype. Mol Cell Endocrinol 159:159-170 (Pubitemid 30067649)
    • (2000) Molecular and Cellular Endocrinology , vol.159 , Issue.1-2 , pp. 159-170
    • Simmen, R.C.M.1    Zhang, X.-L.2    Zhang, D.3    Wang, Y.4    Michel, F.J.5    Simmen, F.A.6
  • 18
    • 34249063875 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase is regulated by sp1 through the differential activation of AKT, JNK, and ERK pathways in human prostate tumor cells
    • Sroka IC, Nagle RB, Bowden GT 2007 Membrane-type 1 matrix metalloproteinase is regulated by sp1 through the differential activation of AKT, JNK, and ERK pathways in human prostate tumor cells. Neoplasia 9:406-417
    • (2007) Neoplasia , vol.9 , pp. 406-417
    • Sroka, I.C.1    Nagle, R.B.2    Bowden, G.T.3
  • 19
    • 33645698574 scopus 로고    scopus 로고
    • Transforming growth factor-β1 induces tissue inhibitor of metalloproteinase-1 expression via activation of extracellular signal-regulated kinase and Sp1 in human fibrosarcoma cells
    • Kwak HJ, Park MJ, Cho H, Park CM, Moon SI, Lee HC, Park IC, Kim MS, Rhee CH, Hong SI 2006 Transforming growth factor-β1 induces tissue inhibitor of metalloproteinase-1 expression via activation of extracellular signal-regulated kinase and Sp1 in human fibrosarcoma cells. Mol Cancer Res 4:209-220
    • (2006) Mol Cancer Res , vol.4 , pp. 209-220
    • Kwak, H.J.1    Park, M.J.2    Cho, H.3    Park, C.M.4    Moon, S.I.5    Lee, H.C.6    Park, I.C.7    Kim, M.S.8    Rhee, C.H.9    Hong, S.I.10
  • 20
    • 0037036451 scopus 로고    scopus 로고
    • Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: Their implication in vascular endothelial growth factor gene transcription
    • DOI 10.1074/jbc.M201753200
    • Milanini-Mongiat J, Pouysségur J, Pagès G 2002 Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription. J Biol Chem 277:20631-20639 (Pubitemid 34967366)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20631-20639
    • Milanini-Mongiat, J.1    Pouyssegur, J.2    Pages, G.3
  • 21
    • 1642535446 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 represses platelet-derived growth factor receptor-α(PDGFR-α) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-α promoter
    • Bonello MR, Khachigian LM 2004 Fibroblast growth factor-2 represses platelet-derived growth factor receptor-α(PDGFR-α) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-α promoter. J Biol Chem 279:2377-2382
    • (2004) J Biol Chem , vol.279 , pp. 2377-2382
    • Bonello, M.R.1    Khachigian, L.M.2
  • 22
    • 0034463165 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine P450scc insulin-like growth factor response element
    • DOI 10.1210/me.14.6.774
    • Urban RJ, Bodenburg Y, Kurosky A, Wood TG, Gasic S 2000 Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element. Mol Endocrinol 14:774-782 (Pubitemid 32260491)
    • (2000) Molecular Endocrinology , vol.14 , Issue.6 , pp. 774-782
    • Urban, R.J.1    Bodenburg, Y.2    Kurosky, A.3    Wood, T.G.4    Gasic, S.5
  • 23
    • 0347635470 scopus 로고    scopus 로고
    • Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: Effects on steroidogenesis and oncogenesis
    • DOI 10.1073/pnas.0307794100
    • Song X, Sui A, Garen A 2004 Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: effects on steroidogenesis and oncogenesis. Proc Natl Acad Sci USA 101:621-626 (Pubitemid 38084686)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.2 , pp. 621-626
    • Song, X.1    Sui, A.2    Garen, A.3
  • 24
    • 0025856790 scopus 로고
    • Characterization and molecular cloning of polypyrimidine tract-binding protein: A component of a complex necessary for pre-mRNA splicing
    • Patton JG, Mayer SA, Tempst P, Nadal-Ginard B 1991 Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing. Genes Dev 5:1237-1251 (Pubitemid 21906034)
    • (1991) Genes and Development , vol.5 , Issue.7 , pp. 1237-1251
    • Patton, J.G.1    Mayer, S.A.2    Tempst, P.3    Nadal-Ginard, B.4
  • 25
    • 34347332370 scopus 로고    scopus 로고
    • Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb
    • DOI 10.1128/MCB.02144-06
    • Dong X, Sweet J, Challis JR, Brown T, Lye SJ 2007 Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb. Mol Cell Biol 27:4863-4875 (Pubitemid 47016137)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.13 , pp. 4863-4875
    • Dong, X.1    Sweet, J.2    Challis, J.R.G.3    Brown, T.4    Lye, S.J.5
  • 26
    • 17144407579 scopus 로고    scopus 로고
    • Identification and characterization of the protein-associated splicing factor as a negative co-regulator of the progesterone receptor
    • DOI 10.1074/jbc.M409187200
    • Dong X, Shylnova O, Challis JR, Lye SJ 2005 Identification and characterization of the protein-associated splicing factor as a negative co-regulator of the progesterone receptor. J Biol Chem 280:13329-13340 (Pubitemid 40517219)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13329-13340
    • Dong, X.1    Shylnova, O.2    Challis, J.R.G.3    Lye, S.J.4
  • 27
    • 0035106562 scopus 로고    scopus 로고
    • PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors
    • DOI 10.1128/MCB.21.7.2298-2311.2001
    • Mathur M, Tucker PW, Samuels HH 2001 PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol 21:2298-2311 (Pubitemid 32222084)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2298-2311
    • Mathur, M.1    Tucker, P.W.2    Samuels, H.H.3
  • 30
    • 34548289084 scopus 로고    scopus 로고
    • MAPK kinases as nucleo-cytoplasmic shuttles for PPARγ
    • Burgermeister E, Seger R 2007 MAPK kinases as nucleo-cytoplasmic shuttles for PPARγ. Cell Cycle 6:1539-1548 (Pubitemid 47327937)
    • (2007) Cell Cycle , vol.6 , Issue.13 , pp. 1539-1548
    • Burgermeister, E.1    Seger, R.2
  • 31
    • 0035891056 scopus 로고    scopus 로고
    • Non-regulated and stimulated mechanisms cooperate in the nuclear accumulation of MEK1
    • DOI 10.1038/sj/onc/1204963
    • Yao Z, Flash I, Raviv Z, Yung Y, Asscher Y, Pleban S, Seger R 2001 Non-regulated and stimulated mechanisms cooperate in the nuclear accumulation of MEK1. Oncogene 20:7588-7596 (Pubitemid 33111859)
    • (2001) Oncogene , vol.20 , Issue.52 , pp. 7588-7596
    • Yao, Z.1    Flash, I.2    Raviv, Z.3    Yung, Y.4    Asscher, Y.5    Pleban, S.6    Seger, R.7
  • 32
    • 0034757776 scopus 로고    scopus 로고
    • The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases
    • Volmat V, Camps M, Arkinstall S, Pouysségur J, Lenormand P 2001 The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases. J Cell Sci 114:3433-3443 (Pubitemid 33019760)
    • (2001) Journal of Cell Science , vol.114 , Issue.19 , pp. 3433-3443
    • Volmat, V.1    Camps, M.2    Arkinstall, S.3    Pouysseegur, J.4    Lenormand, P.5
  • 34
    • 0036710172 scopus 로고    scopus 로고
    • NH2 terminus of PTB-associated splicing factor binds to the porcine P450scc IGF-I response element
    • Urban RJ, Bodenburg YH, Wood TG 2002 NH2 terminus of PTB-associated splicing factor binds to the porcine P450scc IGF-I response element. Am J Physiol Endocrinol Metab 283:E423-E427
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • Urban, R.J.1    Bodenburg, Y.H.2    Wood, T.G.3
  • 37
    • 33746355607 scopus 로고    scopus 로고
    • DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor
    • Zhong N, Kim CY, Rizzu P, Geula C, Porter DR, Pothos EN, Squitieri F, Heutink P, Xu J 2006 DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor. J Biol Chem 281:20940-20948
    • (2006) J Biol Chem , vol.281 , pp. 20940-20948
    • Zhong, N.1    Kim, C.Y.2    Rizzu, P.3    Geula, C.4    Porter, D.R.5    Pothos, E.N.6    Squitieri, F.7    Heutink, P.8    Xu, J.9
  • 38
    • 0036212259 scopus 로고    scopus 로고
    • Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription
    • Sewer MB, Nguyen VQ, Huang CJ, Tucker PW, Kagawa N, Waterman MR 2002 Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. Endocrinology 143:1280-1290
    • (2002) Endocrinology , vol.143 , pp. 1280-1290
    • Sewer, M.B.1    Nguyen, V.Q.2    Huang, C.J.3    Tucker, P.W.4    Kagawa, N.5    Waterman, M.R.6
  • 39
    • 0035159666 scopus 로고    scopus 로고
    • Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions
    • Shav-Tal Y, Cohen M, Lapter S, Dye B, Patton JG, Vandekerckhove J, Zipori D 2001 Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. Mol Biol Cell 12:2328-2340
    • (2001) Mol Biol Cell , vol.12 , pp. 2328-2340
    • Shav-Tal, Y.1    Cohen, M.2    Lapter, S.3    Dye, B.4    Patton, J.G.5    Vandekerckhove, J.6    Zipori, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.