메뉴 건너뛰기




Volumn 26, Issue 7, 2012, Pages 1189-1202

Biasing the prostaglandin F2α receptor responses toward EGFR-dependent transactivation of MAPK

Author keywords

[No Author keywords available]

Indexed keywords

11 FLUORO 9,15 DIHYDROXY 15 (2 INDANYL) 16,17,18,19,20 PENTANORPROSTA 5,13 DIENOIC ACID; BETA ARRESTIN; BIMATOPROST; CLOPROSTENOL; EPIDERMAL GROWTH FACTOR RECEPTOR; FLUPROSTENOL; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROSTAGLANDIN F2 ALPHA DERIVATIVE; PROSTAGLANDIN F2 ALPHA RECEPTOR; PROSTAGLANDIN RECEPTOR; THYMIDINE; UNCLASSIFIED DRUG;

EID: 84863315292     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2011-1245     Document Type: Article
Times cited : (20)

References (59)
  • 2
    • 0141838129 scopus 로고    scopus 로고
    • Myometrial activation and preterm labour: Evidence supporting a role for the prostaglandin F receptor-a review
    • Olson DM, Zaragoza DB, Shallow MC, Cook JL, Mitchell BF, Grigsby P, Hirst J 2003 Myometrial activation and preterm labour: evidence supporting a role for the prostaglandin F receptor-a review. Placenta 24(Suppl A):S47-S54
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Olson, D.M.1    Zaragoza, D.B.2    Shallow, M.C.3    Cook, J.L.4    Mitchell, B.F.5    Grigsby, P.6    Hirst, J.7
  • 3
    • 0035047940 scopus 로고    scopus 로고
    • G protein-coupled prostanoid receptors and the kidney
    • Breyer MD, Breyer RM 2001 G protein-coupled prostanoid receptors and the kidney. Annu Rev Physiol 63:579-605
    • (2001) Annu Rev Physiol , vol.63 , pp. 579-605
    • Breyer, M.D.1    Breyer, R.M.2
  • 4
    • 0023819228 scopus 로고
    • The effect of prostaglandin F2α on intraocular pressure in normotensive human subjects
    • Lee PY, Shao H, Xu LA, Qu CK 1988 The effect of prostaglandin F2α on intraocular pressure in normotensive human subjects. Invest Ophthalmol Vis Sci 29:1474-1477
    • (1988) Invest Ophthalmol Vis Sci , vol.29 , pp. 1474-1477
    • Lee, P.Y.1    Shao, H.2    Xu, L.A.3    Qu, C.K.4
  • 6
  • 7
    • 0025919688 scopus 로고
    • Prostaglandin F2α stimulates proliferation of clonal osteoblastic MC3T3-E1 cells by up-regulation of insulin-like growth factor I receptors
    • Hakeda Y, Harada S, Matsumoto T, Tezuka K, Higashino K, Kodama H, Hashimoto-Goto T, Ogata E, Kumegawa M 1991 Prostaglandin F2α stimulates proliferation of clonal osteoblastic MC3T3-E1 cells by up-regulation of insulin-like growth factor I receptors. J Biol Chem 266:21044-21050
    • (1991) J Biol Chem , vol.266 , pp. 21044-21050
    • Hakeda, Y.1    Harada, S.2    Matsumoto, T.3    Tezuka, K.4    Higashino, K.5    Kodama, H.6    Hashimoto-Goto, T.7    Ogata, E.8    Kumegawa, M.9
  • 8
    • 85047676780 scopus 로고    scopus 로고
    • Prostaglandin F2α stimulates the Raf/MEK1/mitogen-activated protein kinase signaling cascade in bovine luteal cells
    • Chen DB, Westfall SD, Fong HW, Roberson MS, Davis JS 1998 Prostaglandin F2α stimulates the Raf/MEK1/mitogen-activated protein kinase signaling cascade in bovine luteal cells. Endocrinology 139:3876-3885
    • (1998) Endocrinology , vol.139 , pp. 3876-3885
    • Chen, D.B.1    Westfall, S.D.2    Fong, H.W.3    Roberson, M.S.4    Davis, J.S.5
  • 9
    • 0033544916 scopus 로고    scopus 로고
    • Activation of FP prostanoid receptor isoforms leads to Rho-mediated changes in cell morphology and in the cell cytoskeleton
    • Pierce KL, Fujino H, Srinivasan D, Regan JW 1999 Activation of FP prostanoid receptor isoforms leads to Rho-mediated changes in cell morphology and in the cell cytoskeleton. J Biol Chem 274:35944-35949
    • (1999) J Biol Chem , vol.274 , pp. 35944-35949
    • Pierce, K.L.1    Fujino, H.2    Srinivasan, D.3    Regan, J.W.4
  • 11
    • 0023355825 scopus 로고
    • Prostaglandin F2α stimulates phosphatidylinositol 4,5-bisphos-phate hydrolysis and mobilizes intracellular Ca2+ in bovine luteal cells
    • Davis JS, Weakland LL, Weiland DA, Farese RV, West LA 1987 Prostaglandin F2α stimulates phosphatidylinositol 4,5-bisphos-phate hydrolysis and mobilizes intracellular Ca2+ in bovine luteal cells. Proc Natl Acad Sci USA 84:3728-3732
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3728-3732
    • Davis, J.S.1    Weakland, L.L.2    Weiland, D.A.3    Farese, R.V.4    West, L.A.5
  • 12
    • 0031307859 scopus 로고    scopus 로고
    • Prostaglandin F2α (PGF2α) triggers protein kinase C (PKC) and tyrosine kinase activity in cultured mammalian cells
    • Jimenez de Asua L, Goin M 1997 Prostaglandin F2α (PGF2α) triggers protein kinase C (PKC) and tyrosine kinase activity in cultured mammalian cells. Adv Exp Med Biol 400A:531-538
    • (1997) Adv Exp Med Biol , vol.400 A , pp. 531-538
    • de Asua, L.J.1    Goin, M.2
  • 15
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic I, Tokiwa G, Lev S, Courtneidge SA, Schlessinger J 1996 A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383:547-550
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 16
    • 0030613761 scopus 로고    scopus 로고
    • Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A
    • Daaka Y, Luttrell LM, Lefkowitz RJ 1997 Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A. Nature 390:88-91
    • (1997) Nature , vol.390 , pp. 88-91
    • Daaka, Y.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 17
    • 0035952645 scopus 로고    scopus 로고
    • New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades
    • Pierce KL, Luttrell LM, Lefkowitz RJ 2001 New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades. Oncogene 20:1532-1539
    • (2001) Oncogene , vol.20 , pp. 1532-1539
    • Pierce, K.L.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 18
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: The promise and the problem
    • Kenakin T 2003 Ligand-selective receptor conformations revisited: the promise and the problem. Trends Pharmacol Sci 24:346-354
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 19
    • 34447642715 scopus 로고    scopus 로고
    • The evasive nature of drug efficacy: Implications for drug discovery
    • Galandrin S, Oligny-Longpre G, Bouvier M 2007 The evasive nature of drug efficacy: implications for drug discovery. Trends Pharmacol Sci 28:423-430
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 423-430
    • Galandrin, S.1    Oligny-Longpre, G.2    Bouvier, M.3
  • 20
    • 70350464948 scopus 로고    scopus 로고
    • Allosteric modulators of g protein-coupled receptors: Future therapeutics for complex physiological disorders
    • Wang L, Martin B, Brenneman R, Luttrell LM, Maudsley S 2009 Allosteric modulators of g protein-coupled receptors: future therapeutics for complex physiological disorders. J Pharmacol Exp Ther 331:340-348
    • (2009) J Pharmacol Exp Ther , vol.331 , pp. 340-348
    • Wang, L.1    Martin, B.2    Brenneman, R.3    Luttrell, L.M.4    Maudsley, S.5
  • 21
    • 77956398267 scopus 로고    scopus 로고
    • Orthosteric- and allosteric-induced ligand-directed trafficking at GPCRs
    • Digby GJ, Conn PJ, Lindsley CW 2010 Orthosteric- and allosteric-induced ligand-directed trafficking at GPCRs. Curr Opin Drug Dis-cov Dev 13:587-594
    • (2010) Curr Opin Drug Dis-cov Dev , vol.13 , pp. 587-594
    • Digby, G.J.1    Conn, P.J.2    Lindsley, C.W.3
  • 22
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: A novel approach for the treatment of CNS disorders
    • Conn PJ, Christopoulos A, Lindsley CW 2009 Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat Rev Drug Discov 8:41-54
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 23
    • 0032774749 scopus 로고    scopus 로고
    • AL-8810: A novel prostaglandin F2α analog with selective antagonist effects at the prostaglandin F2α (FP) receptor
    • Griffin BW, Klimko P, Crider JY, Sharif NA 1999 AL-8810: a novel prostaglandin F2α analog with selective antagonist effects at the prostaglandin F2α (FP) receptor. J Pharmacol Exp Ther 290:1278 -1284
    • (1999) J Pharmacol Exp Ther , vol.290 , pp. 1278-1284
    • Griffin, B.W.1    Klimko, P.2    Crider, J.Y.3    Sharif, N.A.4
  • 24
    • 79961023886 scopus 로고    scopus 로고
    • Novel suppression mechanism operating in early phase of adipogenesis by positive feedback loop for enhancement of cyclooxygenase-2 expression through prostaglandin F2α receptor mediated activation of MEK/ERK-CREB cascade
    • Ueno T, Fujimori K 2011 Novel suppression mechanism operating in early phase of adipogenesis by positive feedback loop for enhancement of cyclooxygenase-2 expression through prostaglandin F2α receptor mediated activation of MEK/ERK-CREB cascade. FEBS J 278:2901-2912
    • (2011) FEBS J , vol.278 , pp. 2901-2912
    • Ueno, T.1    Fujimori, K.2
  • 25
    • 20444465634 scopus 로고    scopus 로고
    • Acute effects of PGF2α on MMP-2 secretion from human ciliary muscle cells: A PKC- and ERK-dependent process
    • Husain S, Jafri F, Crosson CE 2005 Acute effects of PGF2α on MMP-2 secretion from human ciliary muscle cells: a PKC- and ERK-dependent process. Invest Ophthalmol Vis Sci 46:1706-1713
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 1706-1713
    • Husain, S.1    Jafri, F.2    Crosson, C.E.3
  • 26
    • 34547111277 scopus 로고    scopus 로고
    • F-prostanoid receptor regulation of fibroblast growth factor 2 signaling in endometrial adenocarcinoma cells
    • Sales KJ, Boddy SC, Williams AR, Anderson RA, Jabbour HN 2007 F-prostanoid receptor regulation of fibroblast growth factor 2 signaling in endometrial adenocarcinoma cells. Endocrinology 148: 3635-3644
    • (2007) Endocrinology , vol.148 , pp. 3635-3644
    • Sales, K.J.1    Boddy, S.C.2    Williams, A.R.3    Anderson, R.A.4    Jabbour, H.N.5
  • 28
    • 57049140415 scopus 로고    scopus 로고
    • c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway
    • Zimmerman B, Simaan M, Lee MH, Luttrell LM, Laporte SA 2009 c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway. Cell Signal 21:103-110
    • (2009) Cell Signal , vol.21 , pp. 103-110
    • Zimmerman, B.1    Simaan, M.2    Lee, M.H.3    Luttrell, L.M.4    Laporte, S.A.5
  • 31
    • 33744721062 scopus 로고    scopus 로고
    • Implication of prostaglandin receptors in the accumulation of osteoprotegerin in human osteoblast cultures
    • Samadfam R, Gallant MA, Miousse MC, Parent JL, de Brum-Fernandes AJ 2006 Implication of prostaglandin receptors in the accumulation of osteoprotegerin in human osteoblast cultures. J Rheumatol 33:1167-1175
    • (2006) J Rheumatol , vol.33 , pp. 1167-1175
    • Samadfam, R.1    Gallant, M.A.2    Miousse, M.C.3    Parent, J.L.4    de Brum-Fernandes, A.J.5
  • 32
    • 0042266374 scopus 로고    scopus 로고
    • Trans-activation of the epidermal growth factor receptor mediates parathyroid hormone and prostaglandin F2α -stimulated mitogen-acti-vated protein kinase activation in cultured transgenic murine osteoblasts
    • Ahmed I, Gesty-Palmer D, Drezner MK, Luttrell LM 2003 Trans-activation of the epidermal growth factor receptor mediates parathyroid hormone and prostaglandin F2α -stimulated mitogen-acti-vated protein kinase activation in cultured transgenic murine osteoblasts. Mol Endocrinol 17:1607-1621
    • (2003) Mol Endocrinol , vol.17 , pp. 1607-1621
    • Ahmed, I.1    Gesty-Palmer, D.2    Drezner, M.K.3    Luttrell, L.M.4
  • 33
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H, Leserer M, Abraham R, Wallasch C, Ullrich A 1999 EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402:884-888
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3    Leserer, M.4    Abraham, R.5    Wallasch, C.6    Ullrich, A.7
  • 34
    • 0029558408 scopus 로고
    • In vitro phosphorylation of the epidermal growth factor receptor autophosphoryla-tion domain by c-src: Identification of phosphorylation sites and c-src SH2 domain binding sites
    • Lombardo CR, Consler TG, Kassel DB 1995 In vitro phosphorylation of the epidermal growth factor receptor autophosphoryla-tion domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites. Biochemistry 34:16456-16466
    • (1995) Biochemistry , vol.34 , pp. 16456-16466
    • Lombardo, C.R.1    Consler, T.G.2    Kassel, D.B.3
  • 35
    • 0030614911 scopus 로고    scopus 로고
    • Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation
    • Luttrell LM, Della Rocca GJ, van Biesen T, Luttrell DK, Lefkowitz RJ 1997 Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J Biol Chem 272:4637-4644
    • (1997) J Biol Chem , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    della Rocca, G.J.2    van Biesen, T.3    Luttrell, D.K.4    Lefkowitz, R.J.5
  • 36
    • 0036709020 scopus 로고    scopus 로고
    • Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling
    • Pouyssegur J, Volmat V, Lenormand P 2002 Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling. Biochem Pharmacol 64:755-763
    • (2002) Biochem Pharmacol , vol.64 , pp. 755-763
    • Pouyssegur, J.1    Volmat, V.2    Lenormand, P.3
  • 37
    • 51249090123 scopus 로고    scopus 로고
    • The regulation of extracellular signal-regulated kinase (ERK) in mammalian cells
    • Ramos JW 2008 The regulation of extracellular signal-regulated kinase (ERK) in mammalian cells. Int J Biochem Cell Biol 40:2707-2719
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 2707-2719
    • Ramos, J.W.1
  • 38
    • 0347997608 scopus 로고    scopus 로고
    • MAPK signal pathways in the regulation of cell proliferation in mammalian cells
    • Zhang W, Liu HT 2002 MAPK signal pathways in the regulation of cell proliferation in mammalian cells. Cell Res 12:9-18
    • (2002) Cell Res , vol.12 , pp. 9-18
    • Zhang, W.1    Liu, H.T.2
  • 39
    • 34248563290 scopus 로고    scopus 로고
    • 1 to S-phase transition
    • Meloche S, Pouyssegur J 2007 The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1 to S-phase transition. Oncogene 26:3227-3239
    • (2007) Oncogene , vol.26 , pp. 3227-3239
    • Meloche, S.1    Pouyssegur, J.2
  • 41
    • 77952415656 scopus 로고    scopus 로고
    • Beyond desensitization: Physiological relevance of arrestin-dependent signaling
    • Luttrell LM, Gesty-Palmer D 2010 Beyond desensitization: physiological relevance of arrestin-dependent signaling. Pharmacol Rev 62:305-330
    • (2010) Pharmacol Rev , vol.62 , pp. 305-330
    • Luttrell, L.M.1    Gesty-Palmer, D.2
  • 42
    • 0141703263 scopus 로고    scopus 로고
    • Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2
    • Wei H, Ahn S, Shenoy SK, Karnik SS, Hunyady L, Luttrell LM, Lefkowitz RJ 2003 Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc Natl Acad Sci USA 100:10782-10787
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10782-10787
    • Wei, H.1    Ahn, S.2    Shenoy, S.K.3    Karnik, S.S.4    Hunyady, L.5    Luttrell, L.M.6    Lefkowitz, R.J.7
  • 44
    • 45749146195 scopus 로고    scopus 로고
    • Conformational rearrangements and signaling cascades involved in ligand-biased mitogen-activated protein kinase signaling through the β1-adrenergic receptor
    • Galandrin S, Oligny-Longpre G, Bonin H, Ogawa K, Gales C, Bouvier M 2008 Conformational rearrangements and signaling cascades involved in ligand-biased mitogen-activated protein kinase signaling through the β1-adrenergic receptor. Mol Pharmacol 74:162-172
    • (2008) Mol Pharmacol , vol.74 , pp. 162-172
    • Galandrin, S.1    Oligny-Longpre, G.2    Bonin, H.3    Ogawa, K.4    Gales, C.5    Bouvier, M.6
  • 46
    • 18144422077 scopus 로고    scopus 로고
    • The oxytocin receptor antagonist atosiban inhibits cell growth via a "biased agonist" mechanism
    • Reversi A, Rimoldi V, Marrocco T, Cassoni P, Bussolati G, Parenti M, Chini B 2005 The oxytocin receptor antagonist atosiban inhibits cell growth via a "biased agonist" mechanism. J Biol Chem 280:16311-16318
    • (2005) J Biol Chem , vol.280 , pp. 16311-16318
    • Reversi, A.1    Rimoldi, V.2    Marrocco, T.3    Cassoni, P.4    Bussolati, G.5    Parenti, M.6    Chini, B.7
  • 48
    • 0018643960 scopus 로고
    • Synthesis and biological activity of car-boxyl-terminus modified prostaglandin analogues
    • Schaaf TK, Hess HJ 1979 Synthesis and biological activity of car-boxyl-terminus modified prostaglandin analogues. J Med Chem 22:1340-1346
    • (1979) J Med Chem , vol.22 , pp. 1340-1346
    • Schaaf, T.K.1    Hess, H.J.2
  • 49
    • 0017902567 scopus 로고
    • Amide and i-amino derivatives of F prostaglandins as prostaglandin antagonists
    • Maddox YT, Ramwell PW, Shiner CS, Corey EJ 1978 Amide and i-amino derivatives of F prostaglandins as prostaglandin antagonists. Nature 273:549-552
    • (1978) Nature , vol.273 , pp. 549-552
    • Maddox, Y.T.1    Ramwell, P.W.2    Shiner, C.S.3    Corey, E.J.4
  • 50
    • 0033668921 scopus 로고    scopus 로고
    • Synthetic modification of prostaglandin F2α indicates different structural determinants for binding to the prostaglandin F receptor versus the prostaglandin transporter
    • Schuster VL, Itoh S, Andrews SW, Burk RM, Chen J, Kedzie KM, Gil DW, Woodward DF 2000 Synthetic modification of prostaglandin F2α indicates different structural determinants for binding to the prostaglandin F receptor versus the prostaglandin transporter. Mol Pharmacol 58:1511-1516
    • Mol Pharmacol , vol.58 , pp. 1511-1516
    • Schuster, V.L.1    Itoh, S.2    Andrews, S.W.3    Burk, R.M.4    Chen, J.5    Kedzie, K.M.6    Gil, D.W.7    Woodward, D.F.8
  • 52
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka BK, Deupi X 2007 Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 28:397-406
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 53
    • 77958039571 scopus 로고    scopus 로고
    • Energy landscapes as a tool to integrate GPCR structure, dynamics, and function
    • Deupi X, Kobilka BK 2010 Energy landscapes as a tool to integrate GPCR structure, dynamics, and function. Physiology (Bethesda) 25:293-303
    • (2010) Physiology (Bethesda) , vol.25 , pp. 293-303
    • Deupi, X.1    Kobilka, B.K.2
  • 54
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions
    • Yoon S, Seger R 2006 The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24:21-44
    • (2006) Growth Factors , vol.24 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 55
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ 1995 Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 56
    • 0027156503 scopus 로고
    • Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90-kDa ri-bosomal S6 kinase in PC12 cells. Distinct effects of the neurotrophic factor, nerve growth factor, and the mitogenic factor, epidermal growth factor
    • Nguyen TT, Scimeca JC, Filloux C, Peraldi P, Carpentier JL, Van Obberghen E 1993 Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90-kDa ri-bosomal S6 kinase in PC12 cells. Distinct effects of the neurotrophic factor, nerve growth factor, and the mitogenic factor, epidermal growth factor. J Biol Chem 268:9803-9810
    • (1993) J Biol Chem , vol.268 , pp. 9803-9810
    • Nguyen, T.T.1    Scimeca, J.C.2    Filloux, C.3    Peraldi, P.4    Carpentier, J.L.5    van Obberghen, E.6
  • 57
    • 0026486878 scopus 로고
    • Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor
    • Traverse S, Gomez N, Paterson H, Marshall C, Cohen P 1992 Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem J 288(Pt 2):351-355
    • (1992) Biochem J , vol.288 , Issue.Pt 2 , pp. 351-355
    • Traverse, S.1    Gomez, N.2    Paterson, H.3    Marshall, C.4    Cohen, P.5
  • 58
    • 34250814224 scopus 로고    scopus 로고
    • Molecular mechanisms mediating the G protein-coupled receptor regulation of cell cycle progression
    • New DC, Wong YH 2007 Molecular mechanisms mediating the G protein-coupled receptor regulation of cell cycle progression. J Mol Signal 2:2
    • (2007) J Mol Signal , vol.2 , pp. 2
    • New, D.C.1    Wong, Y.H.2
  • 59
    • 0037151052 scopus 로고    scopus 로고
    • New signaling pathway for parathyroid hormone and cyclic AMP action on extracellular-regulated kinase and cell proliferation in bone cells. Checkpoint of modulation by cyclic AMP
    • Fujita T, Meguro T, Fukuyama R, Nakamuta H, Koida M 2002 New signaling pathway for parathyroid hormone and cyclic AMP action on extracellular-regulated kinase and cell proliferation in bone cells. Checkpoint of modulation by cyclic AMP. J Biol Chem 277:22191-22200
    • (2002) J Biol Chem , vol.277 , pp. 22191-22200
    • Fujita, T.1    Meguro, T.2    Fukuyama, R.3    Nakamuta, H.4    Koida, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.