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Volumn 108, Issue 1-2, 2002, Pages 7-17

c-Jun N-terminal kinase pathway mediates Lactacystin-induced cell death in a neuronal differentiated Neuro2a cell line

Author keywords

c Jun N terminal kinase; Cell death; Lactacystin; Neuro2a; Proteasome

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; CASPASE INHIBITOR; LACTACYSTIN; MUTANT PROTEIN; PROTEASOME; STRESS ACTIVATED PROTEIN KINASE; ACETYLCYSTEINE; BENZYLOXYCARBONYLVALYL ALANYL ASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYL-ALANYL-ASPARTYL FLUOROMETHYL KETONE; CASP3 PROTEIN, MOUSE; CASPASE; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; DRUG DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MULTIENZYME COMPLEX; PEPTIDE CHLOROMETHYL KETONE;

EID: 1842832451     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(02)00460-6     Document Type: Article
Times cited : (14)

References (46)
  • 2
    • 0032979438 scopus 로고    scopus 로고
    • Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation
    • Behrens A., Sibilia M., Wagner E.F. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat. Genet. 21:1999;326-329.
    • (1999) Nat. Genet. , vol.21 , pp. 326-329
    • Behrens, A.1    Sibilia, M.2    Wagner, E.F.3
  • 3
    • 0035852707 scopus 로고    scopus 로고
    • Jun N-terminal kinase 2 modulates thymocyte apoptosis and T cell activation through c-Jun and nuclear factor of activated T cell (NF-AT)
    • Behrens A., Sabapathy K., Graef I., Cleary M., Crabtree G.R., Wagner E.F. Jun N-terminal kinase 2 modulates thymocyte apoptosis and T cell activation through c-Jun and nuclear factor of activated T cell (NF-AT). Proc. Natl. Acad. Sci. USA. 98:2001;1769-1774.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1769-1774
    • Behrens, A.1    Sabapathy, K.2    Graef, I.3    Cleary, M.4    Crabtree, G.R.5    Wagner, E.F.6
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1467-1468.
    • (2001) Science , vol.292 , pp. 1467-1468
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 6
    • 0034651104 scopus 로고    scopus 로고
    • Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis
    • Canu N., Barbato C., Ciotti M.T., Serafino A., Dus L., Calissano P. Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis. J. Neurosci. 15:2000;589-599.
    • (2000) J. Neurosci. , vol.15 , pp. 589-599
    • Canu, N.1    Barbato, C.2    Ciotti, M.T.3    Serafino, A.4    Dus, L.5    Calissano, P.6
  • 7
    • 0034027927 scopus 로고    scopus 로고
    • Oxidative stress induces caspase-independent retinal apoptosis in vitro
    • Carmody R.J., Cotter T.G. Oxidative stress induces caspase-independent retinal apoptosis in vitro. Cell Death Differ. 7:2000;282-291.
    • (2000) Cell Death Differ. , vol.7 , pp. 282-291
    • Carmody, R.J.1    Cotter, T.G.2
  • 8
    • 17144441040 scopus 로고    scopus 로고
    • Correlation between structure of bcl-2 and its inhibitory function of JNK and caspase activity in dopaminergic neuronal apoptosis
    • Choi W.S., Yoon S.Y., Chang I.I., Choi E.J., Rhim H., Jin B.K., Oh T.H., Krajewski S., Reed J.C., Oh Y.J. Correlation between structure of bcl-2 and its inhibitory function of JNK and caspase activity in dopaminergic neuronal apoptosis. J. Neurochem. 74:2000;1621-1626.
    • (2000) J. Neurochem. , vol.74 , pp. 1621-1626
    • Choi, W.S.1    Yoon, S.Y.2    Chang, I.I.3    Choi, E.J.4    Rhim, H.5    Jin, B.K.6    Oh, T.H.7    Krajewski, S.8    Reed, J.C.9    Oh, Y.J.10
  • 9
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 10
    • 0034667705 scopus 로고    scopus 로고
    • Dual roles for c-JUN N-terminal kinase in development and stress responses in cerebellar granule neurons
    • Coffey E.T., Hongisto V., Dickens M., Davis R.J., Courtney M.J. Dual roles for c-JUN N-terminal kinase in development and stress responses in cerebellar granule neurons. J. Neurosci. 20:2000;7602-7613.
    • (2000) J. Neurosci. , vol.20 , pp. 7602-7613
    • Coffey, E.T.1    Hongisto, V.2    Dickens, M.3    Davis, R.J.4    Courtney, M.J.5
  • 11
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1997;1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 12
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler H.C. Activation of the cell death program by inhibition of proteasome function. Proc. Natl. Acad. Sci. USA. 94:1997;855-860.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 855-860
    • Drexler, H.C.1
  • 14
    • 0032032404 scopus 로고    scopus 로고
    • Role of the JUN kinase pathway in the regulation of c-JUN expression and apoptosis in sympathetic neurons
    • Eilers A., Whitfield J., Babij C., Rubin L.L., Ham J. Role of the JUN kinase pathway in the regulation of c-JUN expression and apoptosis in sympathetic neurons. J. Neurosci. 18:1998;1713-1724.
    • (1998) J. Neurosci. , vol.18 , pp. 1713-1724
    • Eilers, A.1    Whitfield, J.2    Babij, C.3    Rubin, L.L.4    Ham, J.5
  • 16
    • 0031662485 scopus 로고    scopus 로고
    • Physiological stress and nerve growth factor treatment regulate stress-activated protein kinase activity in PC12 cells
    • Goodman M.N., Reigh C.W., Landreth G.E. Physiological stress and nerve growth factor treatment regulate stress-activated protein kinase activity in PC12 cells. J. Neurobiol. 36:1998;537-549.
    • (1998) J. Neurobiol. , vol.36 , pp. 537-549
    • Goodman, M.N.1    Reigh, C.W.2    Landreth, G.E.3
  • 18
    • 0035895994 scopus 로고    scopus 로고
    • Inhibition of JNK by overexpression of the JNL binding domain of JIP-1 prevents apoptosis in sympathetic neurons
    • Harding T.C., Xue L., Bienemann A., Haywood D., Dickens M., Tolkovsky A.M., Uney J.B. Inhibition of JNK by overexpression of the JNL binding domain of JIP-1 prevents apoptosis in sympathetic neurons. J. Biol. Chem. 276:2001;4531-4534.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4531-4534
    • Harding, T.C.1    Xue, L.2    Bienemann, A.3    Haywood, D.4    Dickens, M.5    Tolkovsky, A.M.6    Uney, J.B.7
  • 19
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275:2000;35661-35664.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 20
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana N.R., Zemskov E.A., Wang G.h., Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10:2001;1049-1059.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.h.3    Nukina, N.4
  • 21
    • 0034927814 scopus 로고    scopus 로고
    • Apoptotic signaling in dopamine-induced cell death: The role of oxidative stress, p38 mitogen-activated protein kinase, cytochrome c and caspases
    • Junn E., Mouradian M.M. Apoptotic signaling in dopamine-induced cell death: the role of oxidative stress, p38 mitogen-activated protein kinase, cytochrome c and caspases. J. Neurochem. 78:2001;374-383.
    • (2001) J. Neurochem. , vol.78 , pp. 374-383
    • Junn, E.1    Mouradian, M.M.2
  • 22
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinase
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinase. J. Biol. Chem. 270:1995;16483-16486.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 23
    • 0035104229 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid-mediated, caspase-independent dendritic cell by CD40 activation
    • Kim K.D., Choe Y.K., Choe I.S., Lim J.S. Inhibition of glucocorticoid-mediated, caspase-independent dendritic cell by CD40 activation. J. Leukoc. Biol. 69:2001;426-434.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 426-434
    • Kim, K.D.1    Choe, Y.K.2    Choe, I.S.3    Lim, J.S.4
  • 24
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y., Kume A., Li M., Doyu M., Hata M., Ohtsuka K., Sobue G. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J. Biol. Chem. 275:2000;8772-8778.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 25
    • 0032488992 scopus 로고    scopus 로고
    • Dopamine induces apoptosis through an oxidation-involved SAPK/JNK activation pathway
    • Luo Y., Umegaki H., Wang X., Abe R., Roth G.S. Dopamine induces apoptosis through an oxidation-involved SAPK/JNK activation pathway. J. Biol. Chem. 273:1998;3756-3764.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3756-3764
    • Luo, Y.1    Umegaki, H.2    Wang, X.3    Abe, R.4    Roth, G.S.5
  • 26
    • 0034658384 scopus 로고    scopus 로고
    • JNK (c-Jun N-terminal kinase) and p38 activation in receptor-mediated and chemically-induced apoptosis of T-cells: Differential requirements for caspase activation
    • MacFarlane M., Cohen G.M., Dickens M. JNK (c-Jun N-terminal kinase) and p38 activation in receptor-mediated and chemically-induced apoptosis of T-cells: differential requirements for caspase activation. Biochem. J. 348:2000;93-101.
    • (2000) Biochem. J. , vol.348 , pp. 93-101
    • MacFarlane, M.1    Cohen, G.M.2    Dickens, M.3
  • 28
    • 0342393043 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells
    • Pasquini L.A., Besio M.M., Adamo A.M., Pasquini J.M., Soto E.F. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells. J. Neurosci. Res. 59:2000;601-611.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 601-611
    • Pasquini, L.A.1    Besio, M.M.2    Adamo, A.M.3    Pasquini, J.M.4    Soto, E.F.5
  • 29
    • 0000991680 scopus 로고    scopus 로고
    • Protesome inhibitor induce cytochrome c-caspase-3-like proteasome mediated apoptosis in cultured cortical neurons
    • Qiu J.H., Asai A., Chi S., Saito N., Hamada H., Kirino T. Protesome inhibitor induce cytochrome c-caspase-3-like proteasome mediated apoptosis in cultured cortical neurons. J. Neurosci. 20:2000;259-265.
    • (2000) J. Neurosci. , vol.20 , pp. 259-265
    • Qiu, J.H.1    Asai, A.2    Chi, S.3    Saito, N.4    Hamada, H.5    Kirino, T.6
  • 30
    • 0035877087 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated protein kinase (p38 MAPK) in cytokine-induced rat islet cell apoptosis
    • Saldeen J., Lee J.C., Welsh N. Role of p38 mitogen-activated protein kinase (p38 MAPK) in cytokine-induced rat islet cell apoptosis. Biochem. Pharmacol. 61:2001;1561-1569.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 1561-1569
    • Saldeen, J.1    Lee, J.C.2    Welsh, N.3
  • 31
    • 0033840581 scopus 로고    scopus 로고
    • MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo
    • Saporito M.S., Thomas B.A., Scott R.W. MPTP activates c-Jun NH(2)-terminal kinase (JNK) and its upstream regulatory kinase MKK4 in nigrostriatal neurons in vivo. J. Neurochem. 75:2001;1200-1208.
    • (2001) J. Neurochem. , vol.75 , pp. 1200-1208
    • Saporito, M.S.1    Thomas, B.A.2    Scott, R.W.3
  • 32
    • 0027433787 scopus 로고
    • Characterization of proteases with the specificity to cleave at the secretase-site of beta-APP
    • Schonlein C., Probst A., Huber G. Characterization of proteases with the specificity to cleave at the secretase-site of beta-APP. Neurosci. Lett. 161:1993;33-36.
    • (1993) Neurosci. Lett. , vol.161 , pp. 33-36
    • Schonlein, C.1    Probst, A.2    Huber, G.3
  • 34
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: Possible importance in Alzheimer's disease
    • Shringarpure R., Grune T., Sitte N., Davies K.J. 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell Mol. Life Sci. 57:2000;1802-1809.
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 1802-1809
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.4
  • 35
  • 41
    • 0033773607 scopus 로고    scopus 로고
    • Protesome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspase and cytochrome c release
    • Wagenknecht B., Hermisson M., Groscurth P., Liston P., Krammer P.H., Weller M. Protesome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspase and cytochrome c release. J. Neurochem. 75:2000;2288-2297.
    • (2000) J. Neurochem. , vol.75 , pp. 2288-2297
    • Wagenknecht, B.1    Hermisson, M.2    Groscurth, P.3    Liston, P.4    Krammer, P.H.5    Weller, M.6
  • 42
    • 0031972678 scopus 로고    scopus 로고
    • Phosphorylation of c-JUN is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons
    • Watson A., Eilers A., Lallemand D., Kyriakis J., Rubin L.L., Ham J. Phosphorylation of c-JUN is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons. J. Neurosci. 18:1998;751-762.
    • (1998) J. Neurosci. , vol.18 , pp. 751-762
    • Watson, A.1    Eilers, A.2    Lallemand, D.3    Kyriakis, J.4    Rubin, L.L.5    Ham, J.6
  • 43
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinase on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinase on apoptosis. Science. 270:1995;1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 46
    • 0033563113 scopus 로고    scopus 로고
    • Inhibition of ubiquitin-proteasome pathway activates a caspase-3-like protease and induces Bcl-2 cleavage in human M-07e leukaemic cells
    • Zhang X.M., Lin H., Chen C., Chen B.D. Inhibition of ubiquitin-proteasome pathway activates a caspase-3-like protease and induces Bcl-2 cleavage in human M-07e leukaemic cells. Biochem. J. 340:1999;127-213.
    • (1999) Biochem. J. , vol.340 , pp. 127-213
    • Zhang, X.M.1    Lin, H.2    Chen, C.3    Chen, B.D.4


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