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Volumn 1, Issue , 2012, Pages

Erythropoietin prevents PC12 cells from beta-amyloid-induced apoptosis via PI3K/Akt pathway

Author keywords

Alzheimer's disease; Apoptosis; Beta amyloid peptide; Erythropoietin

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; AMYLOID BETA PROTEIN; CASPASE 3; ERYTHROPOIETIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN KINASE B;

EID: 84883602573     PISSN: None     EISSN: 20479158     Source Type: Journal    
DOI: 10.1186/2047-9158-1-7     Document Type: Article
Times cited : (37)

References (54)
  • 1
    • 0031879073 scopus 로고    scopus 로고
    • Molecular mechanism of neuronal cell death in Alzheimer's disease
    • Yoshioka K. Molecular mechanism of neuronal cell death in Alzheimer's disease. Nippon Ronen Igakkai Zasshi 1998, 35(4):265-267.
    • (1998) Nippon Ronen Igakkai Zasshi , vol.35 , Issue.4 , pp. 265-267
    • Yoshioka, K.1
  • 2
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman CW, Anderson AJ. A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol Neurobiol 1995, 10(1):19-45.
    • (1995) Mol Neurobiol , vol.10 , Issue.1 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 3
    • 0029912056 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in Alzheimer's disease
    • Cotman CW, Su JH. Mechanisms of neuronal death in Alzheimer's disease. Brain Pathol 1996, 6(4):493-506.
    • (1996) Brain Pathol , vol.6 , Issue.4 , pp. 493-506
    • Cotman, C.W.1    Su, J.H.2
  • 4
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe DJ. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 1999, 399(6738 Suppl):A23-A31.
    • (1999) Nature , vol.399 , Issue.6738 SUPPL
    • Selkoe, D.J.1
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81(2):741-766.
    • (2001) Physiol Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 6
    • 0028853727 scopus 로고
    • Immunoreactivity for Bcl-2 protein within neurons in the Alzheimer's disease brain increases with disease severity
    • Satou T, Cummings BJ, Cotman CW. Immunoreactivity for Bcl-2 protein within neurons in the Alzheimer's disease brain increases with disease severity. Brain Res 1995, 697(1-2):35-43.
    • (1995) Brain Res , vol.697 , Issue.1-2 , pp. 35-43
    • Satou, T.1    Cummings, B.J.2    Cotman, C.W.3
  • 7
    • 0030638139 scopus 로고    scopus 로고
    • Bax protein expression is increased in Alzheimer's brain: correlations with DNA damage, Bcl-2 expression, and brain pathology
    • Su JH, Deng G, Cotman CW. Bax protein expression is increased in Alzheimer's brain: correlations with DNA damage, Bcl-2 expression, and brain pathology. J Neuropathol Exp Neurol 1997, 56(1):86-93.
    • (1997) J Neuropathol Exp Neurol , vol.56 , Issue.1 , pp. 86-93
    • Su, J.H.1    Deng, G.2    Cotman, C.W.3
  • 8
    • 0342646961 scopus 로고    scopus 로고
    • Recombinant erythropoietin in urine
    • Lasne F, de Ceaurriz J. Recombinant erythropoietin in urine. Nature 2000, 405(6787):635.
    • (2000) Nature , vol.405 , Issue.6787 , pp. 635
    • Lasne, F.1    de Ceaurriz, J.2
  • 9
    • 0035833541 scopus 로고    scopus 로고
    • Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-kappaB signalling cascades
    • Digicaylioglu M, Lipton SA. Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-kappaB signalling cascades. Nature 2001, 412(6847):641-647.
    • (2001) Nature , vol.412 , Issue.6847 , pp. 641-647
    • Digicaylioglu, M.1    Lipton, S.A.2
  • 10
    • 0034284026 scopus 로고    scopus 로고
    • Erythropoietin protects cultured cortical neurons, but not astroglia, from hypoxia and AMPA toxicity
    • Sinor AD, Greenberg DA. Erythropoietin protects cultured cortical neurons, but not astroglia, from hypoxia and AMPA toxicity. Neurosci Lett 2000, 290(3):213-215.
    • (2000) Neurosci Lett , vol.290 , Issue.3 , pp. 213-215
    • Sinor, A.D.1    Greenberg, D.A.2
  • 11
    • 0032516086 scopus 로고    scopus 로고
    • In vivo evidence that erythropoietin protects neurons from ischemic damage
    • Sakanaka M, et al. In vivo evidence that erythropoietin protects neurons from ischemic damage. Proc Natl Acad Sci USA 1998, 95(8):4635-4640.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.8 , pp. 4635-4640
    • Sakanaka, M.1
  • 12
    • 0035957426 scopus 로고    scopus 로고
    • Erythropoietin prevents neuronal apoptosis after cerebral ischemia and metabolic stress
    • Siren AL, et al. Erythropoietin prevents neuronal apoptosis after cerebral ischemia and metabolic stress. Proc Natl Acad Sci USA 2001, 98(7):4044-4049.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.7 , pp. 4044-4049
    • Siren, A.L.1
  • 13
    • 34848841517 scopus 로고    scopus 로고
    • Exploring recombinant human erythropoietin in chronic progressive multiple sclerosis
    • Ehrenreich H, et al. Exploring recombinant human erythropoietin in chronic progressive multiple sclerosis. Brain 2007, 130(Pt 10):2577-2588.
    • (2007) Brain , vol.130 , Issue.PART 10 , pp. 2577-2588
    • Ehrenreich, H.1
  • 14
    • 3242733091 scopus 로고    scopus 로고
    • Age-related changes in erythropoietin immunoreactivity in the cerebral cortex and hippocampus of rats
    • Chung YH, et al. Age-related changes in erythropoietin immunoreactivity in the cerebral cortex and hippocampus of rats. Brain Res 2004, 1018(1):141-146.
    • (2004) Brain Res , vol.1018 , Issue.1 , pp. 141-146
    • Chung, Y.H.1
  • 15
    • 34447634320 scopus 로고    scopus 로고
    • New protein kinase C activator regulates amyloid precursor protein processing in vitro by increasing alpha-secretase activity
    • Yang HQ, et al. New protein kinase C activator regulates amyloid precursor protein processing in vitro by increasing alpha-secretase activity. Eur J Neurosci 2007, 26(2):381-391.
    • (2007) Eur J Neurosci , vol.26 , Issue.2 , pp. 381-391
    • Yang, H.Q.1
  • 16
    • 57049090468 scopus 로고    scopus 로고
    • Protective effects of erythropoietin on tau phosphorylation induced by beta-amyloid
    • Sun ZK, et al. Protective effects of erythropoietin on tau phosphorylation induced by beta-amyloid. J Neurosci Res 2008, 86(13):3018-3027.
    • (2008) J Neurosci Res , vol.86 , Issue.13 , pp. 3018-3027
    • Sun, Z.K.1
  • 17
    • 0033890345 scopus 로고    scopus 로고
    • Stem cell factor and erythropoietin inhibit apoptosis of human erythroid progenitor cells through different signalling pathways
    • Sui X, Krantz SB, Zhao ZJ. Stem cell factor and erythropoietin inhibit apoptosis of human erythroid progenitor cells through different signalling pathways. Br J Haematol 2000, 110(1):63-70.
    • (2000) Br J Haematol , vol.110 , Issue.1 , pp. 63-70
    • Sui, X.1    Krantz, S.B.2    Zhao, Z.J.3
  • 18
    • 0036754036 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase is important for erythropoietin-induced erythropoiesis from CD34(+) hematopoietic progenitor cells
    • Myklebust JH, et al. Activation of phosphatidylinositol 3-kinase is important for erythropoietin-induced erythropoiesis from CD34(+) hematopoietic progenitor cells. Exp Hematol 2002, 30(9):990-1000.
    • (2002) Exp Hematol , vol.30 , Issue.9 , pp. 990-1000
    • Myklebust, J.H.1
  • 19
    • 0033151527 scopus 로고    scopus 로고
    • Protein kinase B (c-Akt), phosphatidylinositol 3-kinase, and STAT5 are activated by erythropoietin (EPO) in HCD57 erythroid cells but are constitutively active in an EPO-independent, apoptosis-resistant subclone (HCD57-SREI cells)
    • Bao H, et al. Protein kinase B (c-Akt), phosphatidylinositol 3-kinase, and STAT5 are activated by erythropoietin (EPO) in HCD57 erythroid cells but are constitutively active in an EPO-independent, apoptosis-resistant subclone (HCD57-SREI cells). Blood 1999, 93(11):3757-3773.
    • (1999) Blood , vol.93 , Issue.11 , pp. 3757-3773
    • Bao, H.1
  • 20
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297(5580):353-356.
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 21
    • 4344669435 scopus 로고    scopus 로고
    • Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease
    • Pereira C, et al. Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease. J Mol Neurosci 2004, 23(1-2):97-104.
    • (2004) J Mol Neurosci , vol.23 , Issue.1-2 , pp. 97-104
    • Pereira, C.1
  • 22
    • 32644475566 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: an intriguing role for methionine 35
    • Clementi ME, et al. Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: an intriguing role for methionine 35. Biochem Biophys Res Commun 2006, 342(1):206-213.
    • (2006) Biochem Biophys Res Commun , vol.342 , Issue.1 , pp. 206-213
    • Clementi, M.E.1
  • 23
    • 0031893945 scopus 로고    scopus 로고
    • Erythropoietin and erythropoietin receptor in the developing human central nervous system
    • Juul SE, et al. Erythropoietin and erythropoietin receptor in the developing human central nervous system. Pediatr Res 1998, 43(1):40-49.
    • (1998) Pediatr Res , vol.43 , Issue.1 , pp. 40-49
    • Juul, S.E.1
  • 24
    • 0034641710 scopus 로고    scopus 로고
    • Erythropoietin crosses the blood-brain barrier to protect against experimental brain injury
    • Brines ML, et al. Erythropoietin crosses the blood-brain barrier to protect against experimental brain injury. Proc Natl Acad Sci USA 2000, 97(19):10526-10531.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.19 , pp. 10526-10531
    • Brines, M.L.1
  • 25
    • 0344011513 scopus 로고    scopus 로고
    • Erythropoietin protects the in vitro blood-brain barrier against VEGF-induced permeability
    • Martinez-Estrada OM, et al. Erythropoietin protects the in vitro blood-brain barrier against VEGF-induced permeability. Eur J Neurosci 2003, 18(9):2538-2544.
    • (2003) Eur J Neurosci , vol.18 , Issue.9 , pp. 2538-2544
    • Martinez-Estrada, O.M.1
  • 26
    • 0027232014 scopus 로고
    • Trophic effect of erythropoietin and other hematopoietic factors on central cholinergic neurons in vitro and in vivo
    • Konishi Y, et al. Trophic effect of erythropoietin and other hematopoietic factors on central cholinergic neurons in vitro and in vivo. Brain Res 1993, 609(1-2):29-35.
    • (1993) Brain Res , vol.609 , Issue.1-2 , pp. 29-35
    • Konishi, Y.1
  • 27
    • 5444234867 scopus 로고    scopus 로고
    • Erythropoietin: novel approaches to neuroprotection in human brain disease
    • Ehrenreich H, et al. Erythropoietin: novel approaches to neuroprotection in human brain disease. Metab Brain Dis 2004, 19(3-4):195-206.
    • (2004) Metab Brain Dis , vol.19 , Issue.3-4 , pp. 195-206
    • Ehrenreich, H.1
  • 28
    • 0034626873 scopus 로고    scopus 로고
    • Survival of hippocampal neurons in culture upon hypoxia: effect of erythropoietin
    • Lewczuk P, et al. Survival of hippocampal neurons in culture upon hypoxia: effect of erythropoietin. Neuroreport 2000, 11(16):3485-3488.
    • (2000) Neuroreport , vol.11 , Issue.16 , pp. 3485-3488
    • Lewczuk, P.1
  • 29
    • 0037109201 scopus 로고    scopus 로고
    • Amyloid beta-peptide alters the distribution of early endosomes and inhibits phosphorylation of Akt in the presence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT)
    • Kubo T, Nishimura S, Oda T. Amyloid beta-peptide alters the distribution of early endosomes and inhibits phosphorylation of Akt in the presence of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT). Brain Res Mol Brain Res 2002, 106(1-2):94-100.
    • (2002) Brain Res Mol Brain Res , vol.106 , Issue.1-2 , pp. 94-100
    • Kubo, T.1    Nishimura, S.2    Oda, T.3
  • 30
    • 0028982103 scopus 로고
    • The toxicity in vitro of beta-amyloid protein
    • Iversen LL, et al. The toxicity in vitro of beta-amyloid protein. Biochem J 1995, 311(Pt 1):1-16.
    • (1995) Biochem J , vol.311 , Issue.PART 1 , pp. 1-16
    • Iversen, L.L.1
  • 31
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike CJ, et al. Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J Neurochem 1995, 64(1):253-265.
    • (1995) J Neurochem , vol.64 , Issue.1 , pp. 253-265
    • Pike, C.J.1
  • 32
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science 1990, 250(4978):279-282.
    • (1990) Science , vol.250 , Issue.4978 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 33
    • 3843139571 scopus 로고    scopus 로고
    • Solution structure of amyloid beta-peptide (25-35) in different media
    • D'Ursi AM, et al. Solution structure of amyloid beta-peptide (25-35) in different media. J Med Chem 2004, 47(17):4231-4238.
    • (2004) J Med Chem , vol.47 , Issue.17 , pp. 4231-4238
    • D'Ursi, A.M.1
  • 34
    • 7644227597 scopus 로고    scopus 로고
    • Transferrin neutralization of amyloid beta 25-35 cytotoxicity
    • Giunta S, et al. Transferrin neutralization of amyloid beta 25-35 cytotoxicity. Clin Chim Acta 2004, 350(1-2):129-136.
    • (2004) Clin Chim Acta , vol.350 , Issue.1-2 , pp. 129-136
    • Giunta, S.1
  • 35
    • 17544372317 scopus 로고    scopus 로고
    • Abeta(31-35) peptide induce apoptosis in PC 12 cells: contrast with Abeta(25-35) peptide and examination of underlying mechanisms
    • Misiti F, et al. Abeta(31-35) peptide induce apoptosis in PC 12 cells: contrast with Abeta(25-35) peptide and examination of underlying mechanisms. Neurochem Int 2005, 46(7):575-583.
    • (2005) Neurochem Int , vol.46 , Issue.7 , pp. 575-583
    • Misiti, F.1
  • 36
    • 33745677648 scopus 로고    scopus 로고
    • Comparative study of endoplasmic reticulum stress-induced neuronal death in rat cultured hippocampal and cerebellar granule neurons
    • Kosuge Y, et al. Comparative study of endoplasmic reticulum stress-induced neuronal death in rat cultured hippocampal and cerebellar granule neurons. Neurochem Int 2006, 49(3):285-293.
    • (2006) Neurochem Int , vol.49 , Issue.3 , pp. 285-293
    • Kosuge, Y.1
  • 38
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked
    • Yang J, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997, 275(5303):1129-1132.
    • (1997) Science , vol.275 , Issue.5303 , pp. 1129-1132
    • Yang, J.1
  • 39
    • 0032418092 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?
    • Tsujimoto Y. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?. Genes Cells 1998, 3(11):697-707.
    • (1998) Genes Cells , vol.3 , Issue.11 , pp. 697-707
    • Tsujimoto, Y.1
  • 40
    • 0027318190 scopus 로고
    • Bcl-2 inhibits death of central neural cells induced by multiple agents
    • Zhong LT, et al. bcl-2 inhibits death of central neural cells induced by multiple agents. Proc Natl Acad Sci USA 1993, 90(10):4533-4537.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.10 , pp. 4533-4537
    • Zhong, L.T.1
  • 41
    • 0030780106 scopus 로고    scopus 로고
    • Movement of Bax from the cytosol to mitochondria during apoptosis
    • Wolter KG, et al. Movement of Bax from the cytosol to mitochondria during apoptosis. J Cell Biol 1997, 139(5):1281-1292.
    • (1997) J Cell Biol , vol.139 , Issue.5 , pp. 1281-1292
    • Wolter, K.G.1
  • 42
    • 0034522342 scopus 로고    scopus 로고
    • Caspases: key players in programmed cell death
    • Grutter MG. Caspases: key players in programmed cell death. Curr Opin Struct Biol 2000, 10(6):649-655.
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.6 , pp. 649-655
    • Grutter, M.G.1
  • 43
    • 12844287571 scopus 로고    scopus 로고
    • Salvianic acid A protects human neuroblastoma SH-SY5Y cells against MPP + -induced cytotoxicity
    • Wang XJ, Xu JX. Salvianic acid A protects human neuroblastoma SH-SY5Y cells against MPP + -induced cytotoxicity. Neurosci Res 2005, 51(2):129-138.
    • (2005) Neurosci Res , vol.51 , Issue.2 , pp. 129-138
    • Wang, X.J.1    Xu, J.X.2
  • 44
    • 34447136104 scopus 로고    scopus 로고
    • Resveratrol protects SH-SY5Y neuroblastoma cells from apoptosis induced by dopamine
    • Lee MK, et al. Resveratrol protects SH-SY5Y neuroblastoma cells from apoptosis induced by dopamine. Exp Mol Med 2007, 39(3):376-384.
    • (2007) Exp Mol Med , vol.39 , Issue.3 , pp. 376-384
    • Lee, M.K.1
  • 45
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death
    • Stadelmann C, et al. Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death. Am J Pathol 1999, 155(5):1459-1466.
    • (1999) Am J Pathol , vol.155 , Issue.5 , pp. 1459-1466
    • Stadelmann, C.1
  • 46
    • 27744447179 scopus 로고    scopus 로고
    • Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides
    • Awasthi A, Matsunaga Y, Yamada T. Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides. Exp Neurol 2005, 196(2):282-289.
    • (2005) Exp Neurol , vol.196 , Issue.2 , pp. 282-289
    • Awasthi, A.1    Matsunaga, Y.2    Yamada, T.3
  • 47
    • 0033527555 scopus 로고    scopus 로고
    • Selective loss of poly(ADP-ribose) and the 85-kDa fragment of poly(ADP-ribose) polymerase in nucleoli during alkylation-induced apoptosis of HeLa cells
    • Alvarez-Gonzalez R, et al. Selective loss of poly(ADP-ribose) and the 85-kDa fragment of poly(ADP-ribose) polymerase in nucleoli during alkylation-induced apoptosis of HeLa cells. J Biol Chem 1999, 274(45):32122-32126.
    • (1999) J Biol Chem , vol.274 , Issue.45 , pp. 32122-32126
    • Alvarez-Gonzalez, R.1
  • 48
    • 33645552166 scopus 로고    scopus 로고
    • Induction of apoptosis by disturbing mitochondrial-membrane potential and cleaving PARP in Jurkat T cells through treatment with acetoxyscirpenol mycotoxins
    • Lee DH, Park T, Kim HW. Induction of apoptosis by disturbing mitochondrial-membrane potential and cleaving PARP in Jurkat T cells through treatment with acetoxyscirpenol mycotoxins. Biol Pharm Bull 2006, 29(4):648-654.
    • (2006) Biol Pharm Bull , vol.29 , Issue.4 , pp. 648-654
    • Lee, D.H.1    Park, T.2    Kim, H.W.3
  • 49
    • 0032509239 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavable mutant
    • Oliver FJ, et al. Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavable mutant. J Biol Chem 1998, 273(50):33533-33539.
    • (1998) J Biol Chem , vol.273 , Issue.50 , pp. 33533-33539
    • Oliver, F.J.1
  • 50
    • 0028785893 scopus 로고
    • Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation
    • Damen JE, et al. Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. Embo J 1995, 14(22):5557-5568.
    • (1995) Embo J , vol.14 , Issue.22 , pp. 5557-5568
    • Damen, J.E.1
  • 51
    • 0026091735 scopus 로고
    • Induction of tyrosine phosphorylation by the erythropoietin receptor correlates with mitogenesis
    • Miura O, et al. Induction of tyrosine phosphorylation by the erythropoietin receptor correlates with mitogenesis. Mol Cell Biol 1991, 11(10):4895-4902.
    • (1991) Mol Cell Biol , vol.11 , Issue.10 , pp. 4895-4902
    • Miura, O.1
  • 52
    • 0030966371 scopus 로고    scopus 로고
    • Mitogenic signaling and inhibition of apoptosis via the erythropoietin receptor Box-1 domain
    • Joneja B, Wojchowski DM. Mitogenic signaling and inhibition of apoptosis via the erythropoietin receptor Box-1 domain. J Biol Chem 1997, 272(17):11176-11184.
    • (1997) J Biol Chem , vol.272 , Issue.17 , pp. 11176-11184
    • Joneja, B.1    Wojchowski, D.M.2
  • 53
    • 0034680872 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase plays an essential role in the erythropoietin-dependent proliferation of CTLL-2 cells
    • Sakamoto H, Kitamura T, Yoshimura A. Mitogen-activated protein kinase plays an essential role in the erythropoietin-dependent proliferation of CTLL-2 cells. J Biol Chem 2000, 275(46):35857-35862.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 35857-35862
    • Sakamoto, H.1    Kitamura, T.2    Yoshimura, A.3
  • 54
    • 0034585294 scopus 로고    scopus 로고
    • Enhancement of erythropoietin-stimulated cell proliferation by Anandamide correlates with increased activation of the mitogen-activated protein kinases ERK1 and ERK2
    • Valk P, et al. Enhancement of erythropoietin-stimulated cell proliferation by Anandamide correlates with increased activation of the mitogen-activated protein kinases ERK1 and ERK2. Hematol J 2000, 1(4):254-263.
    • (2000) Hematol J , vol.1 , Issue.4 , pp. 254-263
    • Valk, P.1


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