메뉴 건너뛰기




Volumn 50, Issue 3, 2014, Pages 663-674

Tumour co-expression of apelin and its receptor is the basis of an autocrine loop involved in the growth of colon adenocarcinomas

Author keywords

Apoptosis; Colon cancer; G protein coupled receptors; Signalisation; Tumour growth

Indexed keywords

ADENYLATE CYCLASE; APELIN; APELIN RECEPTOR; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN KINASE B;

EID: 84893640486     PISSN: 09598049     EISSN: 18790852     Source Type: Journal    
DOI: 10.1016/j.ejca.2013.11.017     Document Type: Article
Times cited : (87)

References (53)
  • 1
    • 77956330487 scopus 로고    scopus 로고
    • doi:10.1038/mp.a000304.01 AfCS-nature molecule pages
    • Audigier Y. Apelin receptor. AfCS-nature molecule pages; 2006. http://dx.doi.org/10.1038/mp.a000304.01.
    • (2006) Apelin Receptor
    • Audigier, Y.1
  • 2
    • 0027717002 scopus 로고
    • A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11
    • B.F. O'Dowd, M. Heiber, and A. Chan et al. A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11 Gene 136 1-2 1993 355 360
    • (1993) Gene , vol.136 , Issue.12 , pp. 355-360
    • O'Dowd, B.F.1    Heiber, M.2    Chan, A.3
  • 3
    • 0030273124 scopus 로고    scopus 로고
    • Expression of a new G protein-coupled receptor X-msr is associated with an endothelial lineage in Xenopus laevis
    • E. Devic, L. Paquereau, P. Vernier, B. Knibiehler, and Y. Audigier Expression of a new G protein-coupled receptor X-msr is associated with an endothelial lineage in Xenopus laevis Mech Dev 59 2 1996 129 140
    • (1996) Mech Dev , vol.59 , Issue.2 , pp. 129-140
    • Devic, E.1    Paquereau, L.2    Vernier, P.3    Knibiehler, B.4    Audigier, Y.5
  • 4
    • 0032811273 scopus 로고    scopus 로고
    • Amino acid sequence and embryonic expression of msr/apj, the mouse homolog of Xenopus X-msr and human APJ
    • E. Devic, K. Rizzoti, S. Bodin, B. Knibiehler, and Y. Audigier Amino acid sequence and embryonic expression of msr/apj, the mouse homolog of Xenopus X-msr and human APJ Mech Dev 84 1-2 1999 199 203
    • (1999) Mech Dev , vol.84 , Issue.12 , pp. 199-203
    • Devic, E.1    Rizzoti, K.2    Bodin, S.3    Knibiehler, B.4    Audigier, Y.5
  • 5
    • 0032552988 scopus 로고    scopus 로고
    • Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor
    • K. Tatemoto, M. Hosoya, and Y. Habata et al. Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor Biochem Biophys Res Commun 251 2 1998 471 476
    • (1998) Biochem Biophys Res Commun , vol.251 , Issue.2 , pp. 471-476
    • Tatemoto, K.1    Hosoya, M.2    Habata, Y.3
  • 6
    • 33745865147 scopus 로고    scopus 로고
    • The apelin receptor is coupled to Gi1 or Gi2 protein and is differentially desensitized by apelin fragments
    • B. Masri, N. Morin, L. Pedebernade, B. Knibiehler, and Y. Audigier The apelin receptor is coupled to Gi1 or Gi2 protein and is differentially desensitized by apelin fragments J Biol Chem 281 27 2006 18317 18326
    • (2006) J Biol Chem , vol.281 , Issue.27 , pp. 18317-18326
    • Masri, B.1    Morin, N.2    Pedebernade, L.3    Knibiehler, B.4    Audigier, Y.5
  • 7
    • 0036289790 scopus 로고    scopus 로고
    • Apelin (65-77) activates extracellular signal-regulated kinases via a PTX-sensitive G protein
    • B. Masri, H. Lahlou, H. Mazarguil, B. Knibiehler, and Y. Audigier Apelin (65-77) activates extracellular signal-regulated kinases via a PTX-sensitive G protein Biochem Biophys Res Commun 290 1 2002 539 545
    • (2002) Biochem Biophys Res Commun , vol.290 , Issue.1 , pp. 539-545
    • Masri, B.1    Lahlou, H.2    Mazarguil, H.3    Knibiehler, B.4    Audigier, Y.5
  • 8
    • 10044296019 scopus 로고    scopus 로고
    • Apelin (65-77) activates p70 S6 kinase and is mitogenic for umbilical endothelial cells
    • B. Masri, N. Morin, M. Cornu, B. Knibiehler, and Y. Audigier Apelin (65-77) activates p70 S6 kinase and is mitogenic for umbilical endothelial cells FASEB J 18 15 2004 1909 1911
    • (2004) FASEB J , vol.18 , Issue.15 , pp. 1909-1911
    • Masri, B.1    Morin, N.2    Cornu, M.3    Knibiehler, B.4    Audigier, Y.5
  • 9
    • 0034517030 scopus 로고    scopus 로고
    • Cloning, pharmacological characterization and brain distribution of the rat apelin receptor
    • N. De Mota, Z. Lenkei, and C. Llorens-Cortes Cloning, pharmacological characterization and brain distribution of the rat apelin receptor Neuroendocrinology 72 6 2000 400 407
    • (2000) Neuroendocrinology , vol.72 , Issue.6 , pp. 400-407
    • De Mota, N.1    Lenkei, Z.2    Llorens-Cortes, C.3
  • 10
    • 0034697792 scopus 로고    scopus 로고
    • Distribution of mRNA encoding B78/apj, the rat homologue of the human APJ receptor, and its endogenous ligand apelin in brain and peripheral tissues
    • A.M. O'Carroll, T.L. Selby, M. Palkovits, and S.J. Lolait Distribution of mRNA encoding B78/apj, the rat homologue of the human APJ receptor, and its endogenous ligand apelin in brain and peripheral tissues Biochim Biophys Acta 1492 1 2000 72 80
    • (2000) Biochim Biophys Acta , vol.1492 , Issue.1 , pp. 72-80
    • O'Carroll, A.M.1    Selby, T.L.2    Palkovits, M.3    Lolait, S.J.4
  • 11
    • 3142746678 scopus 로고    scopus 로고
    • Apelin, a potent diuretic neuropeptide counteracting vasopressin actions through inhibition of vasopressin neuron activity and vasopressin release
    • N. De Mota, A. Reaux-Le Goazigo, and S. El Messari et al. Apelin, a potent diuretic neuropeptide counteracting vasopressin actions through inhibition of vasopressin neuron activity and vasopressin release Proc Natl Acad Sci U S A 101 28 2004 10464 10469
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.28 , pp. 10464-10469
    • De Mota, N.1    Reaux-Le Goazigo, A.2    El Messari, S.3
  • 12
    • 0035668442 scopus 로고    scopus 로고
    • Expression of the murine msr/apj receptor and its ligand apelin is upregulated during formation of the retinal vessels
    • M. Saint-Geniez, B. Masri, F. Malecaze, B. Knibiehler, and Y. Audigier Expression of the murine msr/apj receptor and its ligand apelin is upregulated during formation of the retinal vessels Mech Dev 110 1-2 2002 183 186
    • (2002) Mech Dev , vol.110 , Issue.12 , pp. 183-186
    • Saint-Geniez, M.1    Masri, B.2    Malecaze, F.3    Knibiehler, B.4    Audigier, Y.5
  • 13
    • 33745947584 scopus 로고    scopus 로고
    • Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo
    • C.M. Cox, S.L. D'Agostino, M.K. Miller, R.L. Heimark, and P.A. Krieg Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo Dev Biol 296 1 2006 177 189
    • (2006) Dev Biol , vol.296 , Issue.1 , pp. 177-189
    • Cox, C.M.1    D'Agostino, S.L.2    Miller, M.K.3    Heimark, R.L.4    Krieg, P.A.5
  • 14
    • 0037032005 scopus 로고    scopus 로고
    • Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility
    • I. Szokodi, P. Tavi, and G. Foldes et al. Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility Circ Res 91 5 2002 434 440
    • (2002) Circ Res , vol.91 , Issue.5 , pp. 434-440
    • Szokodi, I.1    Tavi, P.2    Foldes, G.3
  • 15
    • 20144380036 scopus 로고    scopus 로고
    • Apelin, a newly identified adipokine upregulated by insulin and obesity
    • J. Boucher, B. Masri, and D. Daviaud et al. Apelin, a newly identified adipokine upregulated by insulin and obesity Endocrinology 146 4 2005 1764 1771
    • (2005) Endocrinology , vol.146 , Issue.4 , pp. 1764-1771
    • Boucher, J.1    Masri, B.2    Daviaud, D.3
  • 16
    • 25844530179 scopus 로고    scopus 로고
    • The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice
    • M. Sorhede Winzell, C. Magnusson, and B. Ahren The apj receptor is expressed in pancreatic islets and its ligand, apelin, inhibits insulin secretion in mice Regul Pept 131 1-3 2005 12 17
    • (2005) Regul Pept , vol.131 , Issue.13 , pp. 12-17
    • Sorhede Winzell, M.1    Magnusson, C.2    Ahren, B.3
  • 18
    • 10744223499 scopus 로고    scopus 로고
    • Apelin, a new enteric peptide: Localization in the gastrointestinal tract, ontogeny, and stimulation of gastric cell proliferation and of cholecystokinin secretion
    • G. Wang, Y. Anini, and W. Wei et al. Apelin, a new enteric peptide: localization in the gastrointestinal tract, ontogeny, and stimulation of gastric cell proliferation and of cholecystokinin secretion Endocrinology 145 3 2004 1342 1348
    • (2004) Endocrinology , vol.145 , Issue.3 , pp. 1342-1348
    • Wang, G.1    Anini, Y.2    Wei, W.3
  • 19
    • 33645767219 scopus 로고    scopus 로고
    • Transcriptomes of purified gastric ECL and parietal cells: Identification of a novel pathway regulating acid secretion
    • N.W. Lambrecht, I. Yakubov, C. Zer, and G. Sachs Transcriptomes of purified gastric ECL and parietal cells: identification of a novel pathway regulating acid secretion Physiol Genomics 25 1 2006 153 165
    • (2006) Physiol Genomics , vol.25 , Issue.1 , pp. 153-165
    • Lambrecht, N.W.1    Yakubov, I.2    Zer, C.3    Sachs, G.4
  • 20
    • 70349745165 scopus 로고    scopus 로고
    • Ontogeny of apelin and its receptor in the rodent gastrointestinal tract
    • G. Wang, R. Kundu, and S. Han et al. Ontogeny of apelin and its receptor in the rodent gastrointestinal tract Regul Pept 158 1-3 2009 32 39
    • (2009) Regul Pept , vol.158 , Issue.13 , pp. 32-39
    • Wang, G.1    Kundu, R.2    Han, S.3
  • 21
    • 34250173089 scopus 로고    scopus 로고
    • Increased colonic apelin production in rodents with experimental colitis and in humans with IBD
    • S. Han, G. Wang, and S. Qiu et al. Increased colonic apelin production in rodents with experimental colitis and in humans with IBD Regul Pept 142 3 2007 131 137
    • (2007) Regul Pept , vol.142 , Issue.3 , pp. 131-137
    • Han, S.1    Wang, G.2    Qiu, S.3
  • 23
    • 0027432324 scopus 로고
    • Up-regulation of vascular endothelial growth factor and its cognate receptors in a rat glioma model of tumor angiogenesis
    • K.H. Plate, G. Breier, B. Millauer, A. Ullrich, and W. Risau Up-regulation of vascular endothelial growth factor and its cognate receptors in a rat glioma model of tumor angiogenesis Cancer Res 53 23 1993 5822 5827
    • (1993) Cancer Res , vol.53 , Issue.23 , pp. 5822-5827
    • Plate, K.H.1    Breier, G.2    Millauer, B.3    Ullrich, A.4    Risau, W.5
  • 24
    • 36849008270 scopus 로고    scopus 로고
    • Apelin is a potent activator of tumour neoangiogenesis
    • S.C. Sorli, S. Le Gonidec, B. Knibiehler, and Y. Audigier Apelin is a potent activator of tumour neoangiogenesis Oncogene 26 55 2007 7692 7699
    • (2007) Oncogene , vol.26 , Issue.55 , pp. 7692-7699
    • Sorli, S.C.1    Le Gonidec, S.2    Knibiehler, B.3    Audigier, Y.4
  • 25
    • 77955093458 scopus 로고    scopus 로고
    • Apelin expression in human non-small cell lung cancer: Role in angiogenesis and prognosis
    • J. Berta, I. Kenessey, and J. Dobos et al. Apelin expression in human non-small cell lung cancer: role in angiogenesis and prognosis J Thorac Oncol 5 8 2010 1120 1129
    • (2010) J Thorac Oncol , vol.5 , Issue.8 , pp. 1120-1129
    • Berta, J.1    Kenessey, I.2    Dobos, J.3
  • 26
    • 84862816779 scopus 로고    scopus 로고
    • Hypoxia-induced up-regulation of apelin is associated with a poor prognosis in oral squamous cell carcinoma patients
    • K. Heo, Y.H. Kim, and H.J. Sung et al. Hypoxia-induced up-regulation of apelin is associated with a poor prognosis in oral squamous cell carcinoma patients Oral Oncol 48 6 2012 500 506
    • (2012) Oral Oncol , vol.48 , Issue.6 , pp. 500-506
    • Heo, K.1    Kim, Y.H.2    Sung, H.J.3
  • 27
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • K.J. Livak, and T.D. Schmittgen Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method Methods 25 4 2001 402 408
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 28
    • 0017670751 scopus 로고
    • Plasma cell immunoglobulin secretion: Arrest is accompanied by alterations of the golgi complex
    • A.M. Tartakoff, and P. Vassalli Plasma cell immunoglobulin secretion: arrest is accompanied by alterations of the golgi complex J Exp Med 146 5 1977 1332 1345
    • (1977) J Exp Med , vol.146 , Issue.5 , pp. 1332-1345
    • Tartakoff, A.M.1    Vassalli, P.2
  • 29
    • 78449303542 scopus 로고    scopus 로고
    • Apelin suppresses apoptosis of human vascular smooth muscle cells via APJ/PI3-K/Akt signaling pathways
    • R.R. Cui, D.A. Mao, and L. Yi et al. Apelin suppresses apoptosis of human vascular smooth muscle cells via APJ/PI3-K/Akt signaling pathways Amino Acids 39 5 2010 1193 1200
    • (2010) Amino Acids , vol.39 , Issue.5 , pp. 1193-1200
    • Cui, R.R.1    Mao, D.A.2    Yi, L.3
  • 30
    • 33845753359 scopus 로고    scopus 로고
    • Apelin suppresses apoptosis of human osteoblasts
    • H. Xie, L.Q. Yuan, and X.H. Luo et al. Apelin suppresses apoptosis of human osteoblasts Apoptosis 12 1 2007 247 254
    • (2007) Apoptosis , vol.12 , Issue.1 , pp. 247-254
    • Xie, H.1    Yuan, L.Q.2    Luo, X.H.3
  • 31
    • 33847201433 scopus 로고    scopus 로고
    • Apelin and its receptor control heart field formation during zebrafish gastrulation
    • X.X. Zeng, T.P. Wilm, D.S. Sepich, and L. Solnica-Krezel Apelin and its receptor control heart field formation during zebrafish gastrulation Dev Cell 12 3 2007 391 402
    • (2007) Dev Cell , vol.12 , Issue.3 , pp. 391-402
    • Zeng, X.X.1    Wilm, T.P.2    Sepich, D.S.3    Solnica-Krezel, L.4
  • 32
    • 70350608068 scopus 로고    scopus 로고
    • Apelin protects against cardiomyocyte apoptosis induced by glucose deprivation
    • Z. Zhang, B. Yu, and G.Z. Tao Apelin protects against cardiomyocyte apoptosis induced by glucose deprivation Chin Med J (Engl) 122 19 2009 2360 2365
    • (2009) Chin Med J (Engl) , vol.122 , Issue.19 , pp. 2360-2365
    • Zhang, Z.1    Yu, B.2    Tao, G.Z.3
  • 33
    • 7644230704 scopus 로고    scopus 로고
    • Apelin is a novel angiogenic factor in retinal endothelial cells
    • A. Kasai, N. Shintani, and M. Oda et al. Apelin is a novel angiogenic factor in retinal endothelial cells Biochem Biophys Res Commun 325 2 2004 395 400
    • (2004) Biochem Biophys Res Commun , vol.325 , Issue.2 , pp. 395-400
    • Kasai, A.1    Shintani, N.2    Oda, M.3
  • 34
    • 11144240956 scopus 로고    scopus 로고
    • Modification of the terminal residue of apelin-13 antagonizes its hypotensive action
    • D.K. Lee, V.R. Saldivia, T. Nguyen, R. Cheng, S.R. George, and B.F. O'Dowd Modification of the terminal residue of apelin-13 antagonizes its hypotensive action Endocrinology 146 1 2005 231 236
    • (2005) Endocrinology , vol.146 , Issue.1 , pp. 231-236
    • Lee, D.K.1    Saldivia, V.R.2    Nguyen, T.3    Cheng, R.4    George, S.R.5    O'Dowd, B.F.6
  • 35
    • 0023748414 scopus 로고
    • Genetic alterations during colorectal tumor development
    • B. Vogelstein, E.R. Fearon, and S.R. Hamilton et al. Genetic alterations during colorectal tumor development N Engl J Med 319 9 1988 525 532
    • (1988) N Engl J Med , vol.319 , Issue.9 , pp. 525-532
    • Vogelstein, B.1    Fearon, E.R.2    Hamilton, S.R.3
  • 37
    • 84876735112 scopus 로고    scopus 로고
    • Apelin-13 regulates proliferation, migration and survival of retinal Muller cells under hypoxia
    • Q. Lu, Y.R. Jiang, J. Qian, and Y. Tao Apelin-13 regulates proliferation, migration and survival of retinal Muller cells under hypoxia Diabetes Res Clin Pract 99 2 2013 158 167
    • (2013) Diabetes Res Clin Pract , vol.99 , Issue.2 , pp. 158-167
    • Lu, Q.1    Jiang, Y.R.2    Qian, J.3    Tao, Y.4
  • 38
    • 33845403070 scopus 로고    scopus 로고
    • Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha
    • I. Mylonis, G. Chachami, and M. Samiotaki et al. Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha J Biol Chem 281 44 2006 33095 33106
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33095-33106
    • Mylonis, I.1    Chachami, G.2    Samiotaki, M.3
  • 39
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions
    • S. Yoon, and R. Seger The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions Growth Factors 24 1 2006 21 44
    • (2006) Growth Factors , vol.24 , Issue.1 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 41
    • 34249800363 scopus 로고    scopus 로고
    • Hypoxia inducible factor regulates the cardiac expression and secretion of apelin
    • V.P. Ronkainen, J.J. Ronkainen, and S.L. Hanninen et al. Hypoxia inducible factor regulates the cardiac expression and secretion of apelin FASEB J 21 8 2007 1821 1830
    • (2007) FASEB J , vol.21 , Issue.8 , pp. 1821-1830
    • Ronkainen, V.P.1    Ronkainen, J.J.2    Hanninen, S.L.3
  • 42
    • 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
    • J. Milanini-Mongiat, J. Pouyssegur, and G. Pages 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 23 2002 20631 20639
    • (2002) J Biol Chem , vol.277 , Issue.23 , pp. 20631-20639
    • Milanini-Mongiat, J.1    Pouyssegur, J.2    Pages, G.3
  • 43
    • 0028074316 scopus 로고
    • Phosphatidylinositol-3-OH kinase as a direct target of Ras
    • P. Rodriguez-Viciana, P.H. Warne, and R. Dhand et al. Phosphatidylinositol-3-OH kinase as a direct target of Ras Nature 370 6490 1994 527 532
    • (1994) Nature , vol.370 , Issue.6490 , pp. 527-532
    • Rodriguez-Viciana, P.1    Warne, P.H.2    Dhand, R.3
  • 44
    • 2942724235 scopus 로고    scopus 로고
    • MTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways
    • P.K. Majumder, P.G. Febbo, and R. Bikoff et al. MTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways Nat Med 10 6 2004 594 601
    • (2004) Nat Med , vol.10 , Issue.6 , pp. 594-601
    • Majumder, P.K.1    Febbo, P.G.2    Bikoff, R.3
  • 45
    • 13044250465 scopus 로고    scopus 로고
    • Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems
    • K. Podsypanina, L.H. Ellenson, and A. Nemes et al. Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems Proc Natl Acad Sci U S A 96 4 1999 1563 1568
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.4 , pp. 1563-1568
    • Podsypanina, K.1    Ellenson, L.H.2    Nemes, A.3
  • 46
    • 6344275304 scopus 로고    scopus 로고
    • Sp1 is involved in Akt-mediated induction of VEGF expression through an HIF-1-independent mechanism
    • N. Pore, S. Liu, and H.K. Shu et al. Sp1 is involved in Akt-mediated induction of VEGF expression through an HIF-1-independent mechanism Mol Biol Cell 15 11 2004 4841 4853
    • (2004) Mol Biol Cell , vol.15 , Issue.11 , pp. 4841-4853
    • Pore, N.1    Liu, S.2    Shu, H.K.3
  • 47
    • 0035918149 scopus 로고    scopus 로고
    • Cyclic AMP inhibits Akt activity by blocking the membrane localization of PDK1
    • S. Kim, K. Jee, D. Kim, H. Koh, and J. Chung Cyclic AMP inhibits Akt activity by blocking the membrane localization of PDK1 J Biol Chem 276 16 2001 12864 12870
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12864-12870
    • Kim, S.1    Jee, K.2    Kim, D.3    Koh, H.4    Chung, J.5
  • 48
    • 0035813228 scopus 로고    scopus 로고
    • Cyclic AMP inhibits extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways by inhibiting Rap1
    • L. Wang, F. Liu, and M.L. Adamo Cyclic AMP inhibits extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways by inhibiting Rap1 J Biol Chem 276 40 2001 37242 37249
    • (2001) J Biol Chem , vol.276 , Issue.40 , pp. 37242-37249
    • Wang, L.1    Liu, F.2    Adamo, M.L.3
  • 49
    • 56449106087 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in colorectal cancer
    • I.A. Voutsadakis The ubiquitin-proteasome system in colorectal cancer Biochim Biophys Acta 1782 12 2008 800 808
    • (2008) Biochim Biophys Acta , vol.1782 , Issue.12 , pp. 800-808
    • Voutsadakis, I.A.1
  • 50
    • 33748159249 scopus 로고    scopus 로고
    • Proteasome inhibitor bortezomib increases PTEN expression and enhances trastuzumab-induced growth inhibition in trastuzumabresistant cells
    • T. Fujita, H. Doihara, and K. Washio et al. Proteasome inhibitor bortezomib increases PTEN expression and enhances trastuzumab-induced growth inhibition in trastuzumabresistant cells Anticancer Drugs 17 4 2006 455 462
    • (2006) Anticancer Drugs , vol.17 , Issue.4 , pp. 455-462
    • Fujita, T.1    Doihara, H.2    Washio, K.3
  • 51
    • 33749573178 scopus 로고    scopus 로고
    • Cytotoxic synergy between the multikinase inhibitor sorafenib and the proteasome inhibitor bortezomib in vitro: Induction of apoptosis through Akt and c-Jun NH2-terminal kinase pathways
    • C. Yu, B.B. Friday, and J.P. Lai et al. Cytotoxic synergy between the multikinase inhibitor sorafenib and the proteasome inhibitor bortezomib in vitro: induction of apoptosis through Akt and c-Jun NH2-terminal kinase pathways Mol Cancer Ther 5 9 2006 2378 2387
    • (2006) Mol Cancer Ther , vol.5 , Issue.9 , pp. 2378-2387
    • Yu, C.1    Friday, B.B.2    Lai, J.P.3
  • 52
    • 53049087511 scopus 로고    scopus 로고
    • Down-regulation of phospho-Akt is a major molecular determinant of bortezomib-induced apoptosis in hepatocellular carcinoma cells
    • K.F. Chen, P.Y. Yeh, K.H. Yeh, Y.S. Lu, S.Y. Huang, and A.L. Cheng Down-regulation of phospho-Akt is a major molecular determinant of bortezomib-induced apoptosis in hepatocellular carcinoma cells Cancer Res 68 16 2008 6698 6707
    • (2008) Cancer Res , vol.68 , Issue.16 , pp. 6698-6707
    • Chen, K.F.1    Yeh, P.Y.2    Yeh, K.H.3    Lu, Y.S.4    Huang, S.Y.5    Cheng, A.L.6
  • 53
    • 34247591454 scopus 로고    scopus 로고
    • Paracrine and autocrine mechanisms of apelin signaling govern embryonic and tumor angiogenesis
    • R.E. Kalin, M.P. Kretz, A.M. Meyer, A. Kispert, F.L. Heppner, and A.W. Brandli Paracrine and autocrine mechanisms of apelin signaling govern embryonic and tumor angiogenesis Dev Biol 305 2 2007 599 614
    • (2007) Dev Biol , vol.305 , Issue.2 , pp. 599-614
    • Kalin, R.E.1    Kretz, M.P.2    Meyer, A.M.3    Kispert, A.4    Heppner, F.L.5    Brandli, A.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.