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Volumn 1830, Issue 8, 2013, Pages 4017-4029

Antitumor activity of methyl gallate by inhibition of focal adhesion formation and Akt phosphorylation in glioma cells

Author keywords

Cell migration; Focal adhesion; Glioma; Glutamate; Methyl gallate

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHY 4 ISOXAZOLEPROPIONATE ACID GLUTAMATE RECEPTOR; CALCIUM ION; GALLIC ACID; GALLIC ACID METHYL ESTER; GLUTAMATE RECEPTOR; GLUTAMIC ACID; METABOTROPIC RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PAXILLIN; PROTEIN KINASE B; PROTEIN KINASE C; SERINE; UNCLASSIFIED DRUG;

EID: 84877836946     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.03.030     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 0035041023 scopus 로고    scopus 로고
    • Brain and other central nervous system tumors: Rates, trends, and epidemiology
    • DOI 10.1097/00001622-200105000-00005
    • J.G. Gurney, and N. Kadan-Lottick Brain and other central nervous system tumors: rates, trends, and epidemiology Curr. Opin. Oncol. 13 2001 160 166 (Pubitemid 32433971)
    • (2001) Current Opinion in Oncology , vol.13 , Issue.3 , pp. 160-166
    • Gurney, J.G.1    Kadan-Lottick, N.2
  • 2
    • 0030857842 scopus 로고    scopus 로고
    • Tumor cell invasion and angiogenesis in the central nervous system
    • R. Bjerkvig, M. Lund-Johansen, and K. Edvardsen Tumor cell invasion and angiogenesis in the central nervous system Curr. Opin. Oncol. 9 1997 223 229 (Pubitemid 27290444)
    • (1997) Current Opinion in Oncology , vol.9 , Issue.3 , pp. 223-229
    • Bjerkvig, R.1    Lund-Johansen, M.2    Edvardsen, K.3
  • 3
    • 0031018888 scopus 로고    scopus 로고
    • Isolation and characterization of human malignant glioma cells from histologically normal brain
    • D.L. Silbergeld, and M.R. Chicoine Isolation and characterization of human malignant glioma cells from histologically normal brain J. Neurosurg. 86 1997 525 531 (Pubitemid 27097100)
    • (1997) Journal of Neurosurgery , vol.86 , Issue.3 , pp. 525-531
    • Silbergeld, D.L.1    Chicoine, M.R.2
  • 4
    • 35148854098 scopus 로고    scopus 로고
    • Autocrine glutamate signaling promotes glioma cell invasion
    • DOI 10.1158/0008-5472.CAN-07-2034
    • S.A. Lyons, W.J. Chung, A.K. Weaver, T. Ogunrinu, and H. Sontheimer Autocrine glutamate signaling promotes glioma cell invasion Cancer Res. 67 2007 9463 9471 (Pubitemid 47535936)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9463-9471
    • Lyons, S.A.1    Chung, W.J.2    Weaver, A.K.3    Ogunrinu, T.4    Sontheimer, H.5
  • 5
  • 6
    • 0033198997 scopus 로고    scopus 로고
    • Glioma cells release excitotoxic concentrations of glutamate
    • Z.C. Ye, and H. Sontheimer Glioma cells release excitotoxic concentrations of glutamate Cancer Res. 59 1999 4383 4391 (Pubitemid 29418758)
    • (1999) Cancer Research , vol.59 , Issue.17 , pp. 4383-4391
    • Ye, Z.-C.1    Sontheimer, H.2
  • 9
    • 67649619278 scopus 로고    scopus 로고
    • AMPA receptors promote perivascular glioma invasion via beta1 integrin-dependent adhesion to the extracellular matrix
    • Y. Piao, L. Lu, and J. de Groot AMPA receptors promote perivascular glioma invasion via beta1 integrin-dependent adhesion to the extracellular matrix Neuro Oncol. 11 2009 260 273
    • (2009) Neuro Oncol. , vol.11 , pp. 260-273
    • Piao, Y.1    Lu, L.2    De Groot, J.3
  • 11
    • 77954088522 scopus 로고    scopus 로고
    • Gallic acid suppresses cell viability, proliferation, invasion and angiogenesis in human glioma cells
    • Y. Lu, F. Jiang, H. Jiang, K. Wu, X. Zheng, Y. Cai, M. Katakowski, M. Chopp, and S.S. To Gallic acid suppresses cell viability, proliferation, invasion and angiogenesis in human glioma cells Eur. J. Pharmacol. 641 2010 102 107
    • (2010) Eur. J. Pharmacol. , vol.641 , pp. 102-107
    • Lu, Y.1    Jiang, F.2    Jiang, H.3    Wu, K.4    Zheng, X.5    Cai, Y.6    Katakowski, M.7    Chopp, M.8    To, S.S.9
  • 12
    • 0035475321 scopus 로고    scopus 로고
    • Paxillin: A focal adhesion-associated adaptor protein
    • DOI 10.1038/sj.onc.1204786
    • M.D. Schaller Paxillin: a focal adhesion-associated adaptor protein Oncogene 20 2001 6459 6472 (Pubitemid 32977851)
    • (2001) Oncogene , vol.20 , Issue.44 REV. ISS. 5 , pp. 6459-6472
    • Schaller, M.D.1
  • 13
    • 3042723613 scopus 로고    scopus 로고
    • Early molecular events in the assembly of the focal adhesion-stress fiber complex during fibroblast spreading
    • DOI 10.1002/cm.20005
    • B. Zimerman, T. Volberg, and B. Geiger Early molecular events in the assembly of the focal adhesion-stress fiber complex during fibroblast spreading Cell Motil. Cytoskeleton 58 2004 143 159 (Pubitemid 38849953)
    • (2004) Cell Motility and the Cytoskeleton , vol.58 , Issue.3 , pp. 143-159
    • Zimerman, B.1    Volberg, T.2    Geiger, B.3
  • 14
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • N.O. Deakin, and C.E. Turner Paxillin comes of age J. Cell Sci. 121 2008 2435 2444
    • (2008) J. Cell Sci. , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 15
    • 0034638836 scopus 로고    scopus 로고
    • Spatial sensing in fibroblasts mediated by 3′ phosphoinositides
    • J.M. Haugh, F. Codazzi, M. Teruel, and T. Meyer Spatial sensing in fibroblasts mediated by 3′ phosphoinositides J. Cell Biol. 151 2000 1269 1280
    • (2000) J. Cell Biol. , vol.151 , pp. 1269-1280
    • Haugh, J.M.1    Codazzi, F.2    Teruel, M.3    Meyer, T.4
  • 16
    • 0034332904 scopus 로고    scopus 로고
    • Leukocytes navigate by compass: Roles of PI3Kgamma and its lipid products
    • P. Rickert, O.D. Weiner, F. Wang, H.R. Bourne, and G. Servant Leukocytes navigate by compass: roles of PI3Kgamma and its lipid products Trends Cell Biol. 10 2000 466 473
    • (2000) Trends Cell Biol. , vol.10 , pp. 466-473
    • Rickert, P.1    Weiner, O.D.2    Wang, F.3    Bourne, H.R.4    Servant, G.5
  • 17
    • 70449530509 scopus 로고    scopus 로고
    • Role of VASP phosphorylation for the regulation of microglia chemotaxis via the regulation of focal adhesion formation/maturation
    • S. Lee, and C.Y. Chung Role of VASP phosphorylation for the regulation of microglia chemotaxis via the regulation of focal adhesion formation/maturation Mol. Cell. Neurosci. 42 2009 382 390
    • (2009) Mol. Cell. Neurosci. , vol.42 , pp. 382-390
    • Lee, S.1    Chung, C.Y.2
  • 18
    • 33947540584 scopus 로고    scopus 로고
    • 12 receptors in ATP-induced microglial chemotaxis
    • DOI 10.1002/glia.20489
    • K. Ohsawa, Y. Irino, Y. Nakamura, C. Akazawa, K. Inoue, and S. Kohsaka Involvement of P2X4 and P2Y12 receptors in ATP-induced microglial chemotaxis Glia 55 2007 604 616 (Pubitemid 46474302)
    • (2007) GLIA , vol.55 , Issue.6 , pp. 604-616
    • Ohsawa, K.1    Irino, Y.2    Nakamura, Y.3    Akazawa, C.4    Inoue, K.5    Kohsaka, S.6
  • 19
    • 0344845048 scopus 로고    scopus 로고
    • Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis
    • DOI 10.1016/S1097-2765(03)00406-4
    • S. Ishibe, D. Joly, X. Zhu, and L.G. Cantley Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis Mol. Cell 12 2003 1275 1285 (Pubitemid 37487934)
    • (2003) Molecular Cell , vol.12 , Issue.5 , pp. 1275-1285
    • Ishibe, S.1    Joly, D.2    Zhu, X.3    Cantley, L.G.4
  • 20
    • 0037155919 scopus 로고    scopus 로고
    • Hepatocyte growth factor induces ERK-dependent paxillin phosphorylation and regulates paxillin-focal adhesion kinase association
    • DOI 10.1074/jbc.M107551200
    • Z.X. Liu, C.F. Yu, C. Nickel, S. Thomas, and L.G. Cantley Hepatocyte growth factor induces ERK-dependent paxillin phosphorylation and regulates paxillin-focal adhesion kinase association J. Biol. Chem. 277 2002 10452 10458 (Pubitemid 34968166)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10452-10458
    • Liu, Z.-X.1    Yu, C.F.2    Nickel, C.3    Thomas, S.4    Cantley, L.G.5
  • 21
    • 84864026147 scopus 로고    scopus 로고
    • Beta-arrestin 2-dependent activation of ERK1/2 is required for ADP-induced paxillin phosphorylation at Ser(83) and microglia chemotaxis
    • S.H. Lee, R. Hollingsworth, H.Y. Kwon, N. Lee, and C.Y. Chung beta-arrestin 2-dependent activation of ERK1/2 is required for ADP-induced paxillin phosphorylation at Ser(83) and microglia chemotaxis Glia 60 2012 1366 1377
    • (2012) Glia , vol.60 , pp. 1366-1377
    • Lee, S.H.1    Hollingsworth, R.2    Kwon, H.Y.3    Lee, N.4    Chung, C.Y.5
  • 22
    • 67249152429 scopus 로고    scopus 로고
    • Antibacterial activity of methyl gallate isolated from Galla Rhois or carvacrol combined with nalidixic acid against nalidixic acid resistant bacteria
    • J.G. Choi, O.H. Kang, Y.S. Lee, Y.C. Oh, H.S. Chae, H.J. Jang, D.W. Shin, and D.Y. Kwon Antibacterial activity of methyl gallate isolated from Galla Rhois or carvacrol combined with nalidixic acid against nalidixic acid resistant bacteria Molecules 14 2009 1773 1780
    • (2009) Molecules , vol.14 , pp. 1773-1780
    • Choi, J.G.1    Kang, O.H.2    Lee, Y.S.3    Oh, Y.C.4    Chae, H.S.5    Jang, H.J.6    Shin, D.W.7    Kwon, D.Y.8
  • 23
    • 12144289645 scopus 로고    scopus 로고
    • Protective effect of methyl gallate from Toona sinensis (Meliaceae) against hydrogen peroxide-induced oxidative stress and DNA damage in MDCK cells
    • T.J. Hsieh, T.Z. Liu, Y.C. Chia, C.L. Chern, F.J. Lu, M.C. Chuang, S.Y. Mau, S.H. Chen, Y.H. Syu, and C.H. Chen Protective effect of methyl gallate from Toona sinensis (Meliaceae) against hydrogen peroxide-induced oxidative stress and DNA damage in MDCK cells Food Chem. Toxicol. 42 2004 843 850
    • (2004) Food Chem. Toxicol. , vol.42 , pp. 843-850
    • Hsieh, T.J.1    Liu, T.Z.2    Chia, Y.C.3    Chern, C.L.4    Lu, F.J.5    Chuang, M.C.6    Mau, S.Y.7    Chen, S.H.8    Syu, Y.H.9    Chen, C.H.10
  • 24
    • 75949106543 scopus 로고    scopus 로고
    • Effects of methyl gallate and gallic acid on the production of inflammatory mediators interleukin-6 and interleukin-8 by oral epithelial cells stimulated with Fusobacterium nucleatum
    • M.S. Kang, H.S. Jang, J.S. Oh, K.H. Yang, N.K. Choi, H.S. Lim, and S.M. Kim Effects of methyl gallate and gallic acid on the production of inflammatory mediators interleukin-6 and interleukin-8 by oral epithelial cells stimulated with Fusobacterium nucleatum J. Microbiol. 47 2009 760 767
    • (2009) J. Microbiol. , vol.47 , pp. 760-767
    • Kang, M.S.1    Jang, H.S.2    Oh, J.S.3    Yang, K.H.4    Choi, N.K.5    Lim, H.S.6    Kim, S.M.7
  • 25
    • 58149133904 scopus 로고    scopus 로고
    • Inhibitory effect of methyl gallate and gallic acid on oral bacteria
    • M.S. Kang, J.S. Oh, I.C. Kang, S.J. Hong, and C.H. Choi Inhibitory effect of methyl gallate and gallic acid on oral bacteria J. Microbiol. 46 2008 744 750
    • (2008) J. Microbiol. , vol.46 , pp. 744-750
    • Kang, M.S.1    Oh, J.S.2    Kang, I.C.3    Hong, S.J.4    Choi, C.H.5
  • 27
    • 0032524997 scopus 로고    scopus 로고
    • Microglia are more efficient than astrocytes in antigen processing and in Th1 but not Th2 cell activation
    • F. Aloisi, F. Ria, G. Penna, and L. Adorini Microglia are more efficient than astrocytes in antigen processing and in Th1 but not Th2 cell activation J. Immunol. 160 1998 4671 4680 (Pubitemid 28215299)
    • (1998) Journal of Immunology , vol.160 , Issue.10 , pp. 4671-4680
    • Aloisi, F.1    Ria, F.2    Penna, G.3    Adorini, L.4
  • 28
    • 79957897718 scopus 로고    scopus 로고
    • Glutamate and the biology of gliomas
    • J. de Groot, and H. Sontheimer Glutamate and the biology of gliomas Glia 59 2011 1181 1189
    • (2011) Glia , vol.59 , pp. 1181-1189
    • De Groot, J.1    Sontheimer, H.2
  • 29
    • 0141455957 scopus 로고    scopus 로고
    • Novel pathways of F-actin polymerization in the human neutrophil
    • DOI 10.1182/blood-2002-09-2936
    • D. Chodniewicz, and D.V. Zhelev Novel pathways of F-actin polymerization in the human neutrophil Blood 102 2003 2251 2258 (Pubitemid 37122407)
    • (2003) Blood , vol.102 , Issue.6 , pp. 2251-2258
    • Chodniewicz, D.1    Zhelev, D.V.2
  • 30
    • 43149104379 scopus 로고    scopus 로고
    • Knockdown of GluR1 expression by RNA interference inhibits glioma proliferation
    • J.F. de Groot, Y. Piao, L. Lu, G.N. Fuller, and W.K. Yung Knockdown of GluR1 expression by RNA interference inhibits glioma proliferation J. Neurooncol. 88 2008 121 133
    • (2008) J. Neurooncol. , vol.88 , pp. 121-133
    • De Groot, J.F.1    Piao, Y.2    Lu, L.3    Fuller, G.N.4    Yung, W.K.5
  • 31
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Q. Hu, A. Klippel, A.J. Muslin, W.J. Fantl, and L.T. Williams Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase Science 268 1995 100 102
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 33
    • 15044359236 scopus 로고    scopus 로고
    • Linking Rap to cell adhesion
    • DOI 10.1016/j.ceb.2005.02.009, Cell Regulation
    • J.L. Bos Linking Rap to cell adhesion Curr. Opin. Cell Biol. 17 2005 123 128 (Pubitemid 40380934)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.2 , pp. 123-128
    • Bos, J.L.1
  • 34
    • 0038741814 scopus 로고    scopus 로고
    • Does Rap1 deserve a bad Rap?
    • DOI 10.1016/S0968-0004(03)00087-2
    • P.J. Stork Does Rap1 deserve a bad Rap? Trends Biochem. Sci. 28 2003 267 275 (Pubitemid 36588669)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.5 , pp. 267-275
    • Stork, P.J.S.1
  • 35
    • 1242307450 scopus 로고    scopus 로고
    • Phosphorylation of paxillin by p38MAPK is involved in the neurite extension of PC-12 cells
    • DOI 10.1083/jcb.200307081
    • C. Huang, C.H. Borchers, M.D. Schaller, and K. Jacobson Phosphorylation of paxillin by p38MAPK is involved in the neurite extension of PC-12 cells J. Cell Biol. 164 2004 593 602 (Pubitemid 38233320)
    • (2004) Journal of Cell Biology , vol.164 , Issue.4 , pp. 593-602
    • Huang, C.1    Borchers, C.H.2    Schaller, M.D.3    Jacobson, K.4
  • 36
    • 6344255031 scopus 로고    scopus 로고
    • Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis
    • DOI 10.1016/j.molcel.2004.10.006, PII S109727650400615X
    • S. Ishibe, D. Joly, Z.X. Liu, and L.G. Cantley Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis Mol. Cell 16 2004 257 267 (Pubitemid 39388840)
    • (2004) Molecular Cell , vol.16 , Issue.2 , pp. 257-267
    • Ishibe, S.1    Joly, D.2    Liu, Z.-X.3    Cantley, L.G.4
  • 37
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase
    • S.L. Bellis, J.T. Miller, and C.E. Turner Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase J. Biol. Chem. 270 1995 17437 17441
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3
  • 38
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins: Getting in on the Akt
    • DOI 10.1016/S0092-8674(02)01083-8
    • D.P. Brazil, J. Park, and B.A. Hemmings PKB binding proteins. Getting in on the Akt Cell 111 2002 293 303 (Pubitemid 35341386)
    • (2002) Cell , vol.111 , Issue.3 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 39
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • S.R. Datta, A. Brunet, and M.E. Greenberg Cellular survival: a play in three Akts Genes Dev. 13 1999 2905 2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 40
    • 0035947085 scopus 로고    scopus 로고
    • Control of cell polarity and chemotaxis by Akt/PKB and PI3 kinase through the regulation of PAKa
    • DOI 10.1016/S1097-2765(01)00247-7
    • C.Y. Chung, G. Potikyan, and R.A. Firtel Control of cell polarity and chemotaxis by Akt/PKB and PI3 kinase through the regulation of PAKa Mol. Cell 7 2001 937 947 (Pubitemid 32525741)
    • (2001) Molecular Cell , vol.7 , Issue.5 , pp. 937-947
    • Chung, C.Y.1    Potikyan, G.2    Firtel, R.A.3
  • 41
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • DOI 10.1242/jcs.00703
    • S. Merlot, and R.A. Firtel Leading the way: directional sensing through phosphatidylinositol 3-kinase and other signaling pathways J. Cell Sci. 116 2003 3471 3478 (Pubitemid 37063391)
    • (2003) Journal of Cell Science , vol.116 , Issue.17 , pp. 3471-3478
    • Merlot, S.1    Firtel, R.A.2
  • 42
    • 0035489468 scopus 로고    scopus 로고
    • PKB/AKT: Functional insights from genetic models
    • DOI 10.1038/35096067
    • M.P. Scheid, and J.R. Woodgett PKB/AKT: functional insights from genetic models Nat. Rev. Mol. Cell Biol. 2 2001 760 768 (Pubitemid 33679838)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.10 , pp. 760-768
    • Scheid, M.P.1    Woodgett, J.R.2
  • 43
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-AKT pathway in human cancer
    • I. Vivanco, and C.L. Sawyers The phosphatidylinositol 3-Kinase AKT pathway in human cancer Nat. Rev. Cancer 2 2002 489 501 (Pubitemid 37328931)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.7 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 44
    • 0028912822 scopus 로고
    • The metabotropic glutamate receptors: Structure and functions
    • J.P. Pin, and R. Duvoisin The metabotropic glutamate receptors: structure and functions Neuropharmacology 34 1995 1 26
    • (1995) Neuropharmacology , vol.34 , pp. 1-26
    • Pin, J.P.1    Duvoisin, R.2
  • 45
    • 0032834028 scopus 로고    scopus 로고
    • Pharmacological agents acting at subtypes of metabotropic glutamate receptors
    • DOI 10.1016/S0028-3908(99)00092-1, PII S0028390899000921
    • D.D. Schoepp, D.E. Jane, and J.A. Monn Pharmacological agents acting at subtypes of metabotropic glutamate receptors Neuropharmacology 38 1999 1431 1476 (Pubitemid 29457728)
    • (1999) Neuropharmacology , vol.38 , Issue.10 , pp. 1431-1476
    • Schoepp, D.D.1    Jane, D.E.2    Monn, J.A.3
  • 46
    • 33846474121 scopus 로고    scopus 로고
    • G-protein-coupled receptors and cancer
    • DOI 10.1038/nrc2069, PII NRC2069
    • R.T. Dorsam, and J.S. Gutkind G-protein-coupled receptors and cancer Nat. Rev. Cancer 7 2007 79 94 (Pubitemid 46164746)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.2 , pp. 79-94
    • Dorsam, R.T.1    Gutkind, J.S.2
  • 47
    • 0030962938 scopus 로고    scopus 로고
    • Characterization of metabotropic glutamate receptors in rat C6 glioma cells
    • DOI 10.1016/S0014-2999(97)00154-4, PII S0014299997001544
    • J.L. Albasanz, M. Ros, and M. Martin Characterization of metabotropic glutamate receptors in rat C6 glioma cells Eur. J. Pharmacol. 326 1997 85 91 (Pubitemid 27205049)
    • (1997) European Journal of Pharmacology , vol.326 , Issue.1 , pp. 85-91
    • Albasanz, J.L.1    Ros, M.2    Martin, M.3
  • 48
    • 0038810014 scopus 로고    scopus 로고
    • Expression and functional role of mGluR3 and mGluR5 in human astrocytes and glioma cells: Opposite regulation of glutamate transporter proteins
    • DOI 10.1046/j.1460-9568.2003.02657.x
    • E. Aronica, J.A. Gorter, H. Ijlst-Keizers, A.J. Rozemuller, B. Yankaya, S. Leenstra, and D. Troost Expression and functional role of mGluR3 and mGluR5 in human astrocytes and glioma cells: opposite regulation of glutamate transporter proteins Eur. J. Neurosci. 17 2003 2106 2118 (Pubitemid 36713971)
    • (2003) European Journal of Neuroscience , vol.17 , Issue.10 , pp. 2106-2118
    • Aronica, E.1    Gorter, J.A.2    Ijlst-Keizers, H.3    Rozemuller, A.J.4    Yankaya, B.5    Leenstra, S.6    Troost, D.7
  • 49
    • 0034711316 scopus 로고    scopus 로고
    • Integrin engagement, the actin cytoskeleton, and c-Src are required for the calcitonin-induced tyrosine phosphorylation of paxillin and HEF1, but not for calcitonin-induced Erk1/2 phosphorylation
    • DOI 10.1074/jbc.M001818200
    • Z. Zhang, R. Baron, and W.C. Horne Integrin engagement, the actin cytoskeleton, and c-Src are required for the calcitonin-induced tyrosine phosphorylation of paxillin and HEF1, but not for calcitonin-induced Erk1/2 phosphorylation J. Biol. Chem. 275 2000 37219 37223 (Pubitemid 32002142)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37219-37223
    • Zhang, Z.1    Baron, R.2    Horne, W.C.3


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