메뉴 건너뛰기




Volumn 37, Issue 5, 2004, Pages 597-606

4-Hydroxynonenal and regulation of cell cycle: Effects on the pRb/E2F pathway

Author keywords

4 Hydroxynonenal; AP 1; cAMP response element binding protein; CBP; CD11b, CD67; cluster of differentiation 11b, 67; CREB; dimethylsulfoxide; DMSO; DP; E2F; Free radicals; HL 60; p300 CREB binding protein; pRb; transcription factor activator protein 1

Indexed keywords

4 HYDROXYNONENAL; ALDEHYDE DERIVATIVE; CYCLIN A; CYCLIN D1; CYCLIN D2; MYC PROTEIN; PROTEIN P21; TRANSCRIPTION FACTOR E2F4;

EID: 3343002135     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.05.023     Document Type: Review
Times cited : (60)

References (88)
  • 4
    • 0020521409 scopus 로고
    • Lipid peroxidation in hepatomas of different degrees of deviation
    • Rossi M.A., Cecchini G. Lipid peroxidation in hepatomas of different degrees of deviation. Cell Biochem. Funct. 1:1983;49-54
    • (1983) Cell Biochem. Funct. , vol.1 , pp. 49-54
    • Rossi, M.A.1    Cecchini, G.2
  • 5
    • 0042671376 scopus 로고    scopus 로고
    • 4-hydroxynonenal from pathology to physiology
    • Dianzani M.U. 4-hydroxynonenal from pathology to physiology. Mol. Aspects Med. 24:2003;263-272
    • (2003) Mol. Aspects Med. , vol.24 , pp. 263-272
    • Dianzani, M.U.1
  • 6
    • 0024412692 scopus 로고
    • Effect of two aliphatic aldehydes, methylglyoxal and 4-hydroxypentenal, on the growth of Yoshida ascites hepatoma AH-130
    • Tessitore L., Bonelli G., Costelli P., Matera L., Pileri A., Baccino F.M., Dianzani M.U. Effect of two aliphatic aldehydes, methylglyoxal and 4-hydroxypentenal, on the growth of Yoshida ascites hepatoma AH-130. Chem. Biol. Interact. 70:1989;227-240
    • (1989) Chem. Biol. Interact. , vol.70 , pp. 227-240
    • Tessitore, L.1    Bonelli, G.2    Costelli, P.3    Matera, L.4    Pileri, A.5    Baccino, F.M.6    Dianzani, M.U.7
  • 8
    • 0026793576 scopus 로고
    • 4-Hydroxynonenal, a product of cellular lipid peroxidation, which modulates c-myc and globin gene expression in K562 erythroleukemic cells
    • Fazio V.M., Barrera G., Martinotti S., Farace M.G., Giglioni B., Frati L., Manzari V., Dianzani M.D. 4-Hydroxynonenal, a product of cellular lipid peroxidation, which modulates c-myc and globin gene expression in K562 erythroleukemic cells. Cancer Res. 52:1992;4866-4871
    • (1992) Cancer Res. , vol.52 , pp. 4866-4871
    • Fazio, V.M.1    Barrera, G.2    Martinotti, S.3    Farace, M.G.4    Giglioni, B.5    Frati, L.6    Manzari, V.7    Dianzani, M.D.8
  • 10
    • 0002801443 scopus 로고
    • Repeated treatments with a low HNE concentration affect K562 cell proliferation
    • A. et al. Columbano. New York: Plenum
    • Barrera G., Biasi F., Fazio V.M., Paradisi L., Dianzani M.U. Repeated treatments with a low HNE concentration affect K562 cell proliferation. Columbano A., et al. Chemical Carcinogenesis. 1991;337-342 Plenum, New York
    • (1991) Chemical Carcinogenesis , pp. 337-342
    • Barrera, G.1    Biasi, F.2    Fazio, V.M.3    Paradisi, L.4    Dianzani, M.U.5
  • 13
    • 0023015912 scopus 로고
    • Induction by physiological agents of differentiation of the human leukemia cell line HL-60 to cells with functional characteristics
    • Breitman T.R., Hemmi H., Imaizumi M. Induction by physiological agents of differentiation of the human leukemia cell line HL-60 to cells with functional characteristics. Prog. Clin. Biol. Res. 226:1986;215-233
    • (1986) Prog. Clin. Biol. Res. , vol.226 , pp. 215-233
    • Breitman, T.R.1    Hemmi, H.2    Imaizumi, M.3
  • 18
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr C.J. Cancer cell cycles. Science. 274:1996;1672-1677
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 19
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: Cyclins revisited
    • Murray A.W. Recycling the cell cycle: cyclins revisited. Cell. 116:2004;221-234
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 20
    • 0033004490 scopus 로고    scopus 로고
    • Inhibition of D1, D2, and A-cyclin expression in HL-60 cells by the lipid peroxidation product 4-hydroxynonenal
    • Pizzimenti S., Barrera G., Dianzani M.U., Brüsselbach S. Inhibition of D1, D2, and A-cyclin expression in HL-60 cells by the lipid peroxidation product 4-hydroxynonenal. Free Radic. Biol. Med. 26:1999;1578-1586
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 1578-1586
    • Pizzimenti, S.1    Barrera, G.2    Dianzani, M.U.3    Brüsselbach, S.4
  • 21
    • 0028988585 scopus 로고
    • Inhibitors of mammalian G1 cyclin-dependent kinases
    • Sherr C.J., Roberts J.M. Inhibitors of mammalian G1 cyclin-dependent kinases. Genes Dev. 9:1995;1149-1163
    • (1995) Genes Dev. , vol.9 , pp. 1149-1163
    • Sherr, C.J.1    Roberts, J.M.2
  • 22
    • 0029134016 scopus 로고
    • Role of the cyclin-dependent kinase inhibitors in the development of cancer
    • Hirama T., Koeffler H.P. Role of the cyclin-dependent kinase inhibitors in the development of cancer. Blood. 86:1995;841-854
    • (1995) Blood , vol.86 , pp. 841-854
    • Hirama, T.1    Koeffler, H.P.2
  • 25
    • 0027938209 scopus 로고
    • Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
    • Hunter T., Pines J. Cyclins and cancer II: cyclin D and CDK inhibitors come of age. Cell. 79:1994;573-582
    • (1994) Cell , vol.79 , pp. 573-582
    • Hunter, T.1    Pines, J.2
  • 26
    • 0027987170 scopus 로고
    • Induction of differentiation in human promyelocytic HL-60 leukemia cells activates p21 WAF1/CIP1 expression in absence of p53
    • Jiang H., Lin J., Su Z., Collart F.R., Huberman E., Fischer P.B. Induction of differentiation in human promyelocytic HL-60 leukemia cells activates p21 WAF1/CIP1 expression in absence of p53. Oncogene. 9:1994;3397-3406
    • (1994) Oncogene , vol.9 , pp. 3397-3406
    • Jiang, H.1    Lin, J.2    Su, Z.3    Collart, F.R.4    Huberman, E.5    Fischer, P.B.6
  • 27
    • 0028985518 scopus 로고
    • P-53 independent induction of WAF1/CIP1 in human leukaemia cells is correlated with growth arrest accompanying monocyte/macrophage differentiation
    • Zhang W., Grasso L., McClain G.D., Gambel A.M., Cha Y., Travali S., Deisserot A.B., Mercer W.E. p-53 independent induction of WAF1/CIP1 in human leukaemia cells is correlated with growth arrest accompanying monocyte/macrophage differentiation. Cancer Res. 55:1995;668-674
    • (1995) Cancer Res. , vol.55 , pp. 668-674
    • Zhang, W.1    Grasso, L.2    McClain, G.D.3    Gambel, A.M.4    Cha, Y.5    Travali, S.6    Deisserot, A.B.7    Mercer, W.E.8
  • 29
    • 0030561571 scopus 로고    scopus 로고
    • The retinoblastoma protein pathway and the restriction point
    • Bartek J., Bartkova J., Lukas J. The retinoblastoma protein pathway and the restriction point. Curr. Opin. Cell Biol. 8:1996;805-814
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 805-814
    • Bartek, J.1    Bartkova, J.2    Lukas, J.3
  • 30
    • 0025905183 scopus 로고
    • The E2F transcription factor is a cellular target for the RB protein
    • Chellappan S.P., Hiebert S., Mudryj M., Horowitz J.M., Nevins J.R. The E2F transcription factor is a cellular target for the RB protein. Cell. 65:1991;1053-1061
    • (1991) Cell , vol.65 , pp. 1053-1061
    • Chellappan, S.P.1    Hiebert, S.2    Mudryj, M.3    Horowitz, J.M.4    Nevins, J.R.5
  • 31
    • 0034306996 scopus 로고    scopus 로고
    • The Rb/E2F pathway: Expanding roles and emerging paradigms
    • Harbour J.W., Dean D.C. The Rb/E2F pathway: expanding roles and emerging paradigms. Genes Dev. 14:2000;2393-2409
    • (2000) Genes Dev. , vol.14 , pp. 2393-2409
    • Harbour, J.W.1    Dean, D.C.2
  • 32
    • 0029868367 scopus 로고    scopus 로고
    • A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation
    • Ikeda M., Laszlo J., Nevins J.R. A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation. Proc. Natl. Acad. Sci. USA. 93:1996;3215-3220
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3215-3220
    • Ikeda, M.1    Laszlo, J.2    Nevins, J.R.3
  • 33
    • 0024651359 scopus 로고
    • Nuclear factor E2F mediates basic transcription and trans-activation by E1a of the human myc promoter
    • Thalmeier K., Synovzik H., Mertz R., Winnacker E.L., Lipp M. Nuclear factor E2F mediates basic transcription and trans-activation by E1a of the human myc promoter. Genes Dev. 3:1992;527-536
    • (1992) Genes Dev. , vol.3 , pp. 527-536
    • Thalmeier, K.1    Synovzik, H.2    Mertz, R.3    Winnacker, E.L.4    Lipp, M.5
  • 35
    • 0028356521 scopus 로고
    • E2F-dependent regulation of human MYC: Trans-activation by cyclins D1 and a overrides tumour suppressor protein functions
    • Oswald F., Lovec H., Moroy T., Lipp M. E2F-dependent regulation of human MYC: trans-activation by cyclins D1 and A overrides tumour suppressor protein functions. Oncogene. 9:1994;2029-2036
    • (1994) Oncogene , vol.9 , pp. 2029-2036
    • Oswald, F.1    Lovec, H.2    Moroy, T.3    Lipp, M.4
  • 36
    • 0037445901 scopus 로고    scopus 로고
    • E2F and cell cycle control: A double-edged sword
    • Stevens C., La Thangue N.B. E2F and cell cycle control: a double-edged sword. Arch. Biochem. Biophys. 412:2003;157-169
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 157-169
    • Stevens, C.1    La Thangue, N.B.2
  • 37
    • 0026526437 scopus 로고
    • E2F: A link between the Rb tumor suppressor protein and viral oncoproteins
    • Nevins J.R. E2F: a link between the Rb tumor suppressor protein and viral oncoproteins. Science. 258:1992;424-429
    • (1992) Science , vol.258 , pp. 424-429
    • Nevins, J.R.1
  • 38
    • 0032568323 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p21 gene during cell cycle progression is under the control of the transcription factor E2F
    • Hiyama H., Iavarone A., Reeves S.A. Regulation of the cdk inhibitor p21 gene during cell cycle progression is under the control of the transcription factor E2F. Oncogene. 16:1998;1513-1523
    • (1998) Oncogene , vol.16 , pp. 1513-1523
    • Hiyama, H.1    Iavarone, A.2    Reeves, S.A.3
  • 39
    • 0029105092 scopus 로고
    • Overexpression of the E2F-1 transcription factor gene mediates cell transformation
    • Yang X.H., Sladek T.L. Overexpression of the E2F-1 transcription factor gene mediates cell transformation. Gene Expr. 4:1995;195-204
    • (1995) Gene Expr. , vol.4 , pp. 195-204
    • Yang, X.H.1    Sladek, T.L.2
  • 40
    • 0028360766 scopus 로고
    • Overexpression of E2F-1 in rat embryo fibroblasts leads to neoplastic transformation
    • Singh P., Wong S.H., Hong W. Overexpression of E2F-1 in rat embryo fibroblasts leads to neoplastic transformation. EMBO J. 13:1994;3329-3338
    • (1994) EMBO J. , vol.13 , pp. 3329-3338
    • Singh, P.1    Wong, S.H.2    Hong, W.3
  • 41
    • 0026636908 scopus 로고
    • Retinoblastoma protein switches the E2F site from positive to negative element
    • Weintraub S.J., Prater C.A., Dean D.C. Retinoblastoma protein switches the E2F site from positive to negative element. Nature. 358:1992;259-261
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 42
    • 0031823036 scopus 로고    scopus 로고
    • The growth arrest and downregulation of c-myc transcription induced by ceramide are related events dependent on p21 induction, Rb underphospholylation and E2F sequestering
    • Alesse E., Zazzeroni F., Angelucci A., Giannini G., Di Marcotullio L., Gulino A. The growth arrest and downregulation of c-myc transcription induced by ceramide are related events dependent on p21 induction, Rb underphospholylation and E2F sequestering. Cell Death Differ. 5:1998;381-389
    • (1998) Cell Death Differ. , vol.5 , pp. 381-389
    • Alesse, E.1    Zazzeroni, F.2    Angelucci, A.3    Giannini, G.4    Di Marcotullio, L.5    Gulino, A.6
  • 43
    • 0034731371 scopus 로고    scopus 로고
    • Opposite functions for E2F1 and E2F4 in human epidermal keratinocyte differentiation
    • Paramio J.M., Segrelles C., Casanova M.L., Jorcano J.L. Opposite functions for E2F1 and E2F4 in human epidermal keratinocyte differentiation. J. Biol. Chem. 275:2000;41219-41226
    • (2000) J. Biol. Chem. , vol.275 , pp. 41219-41226
    • Paramio, J.M.1    Segrelles, C.2    Casanova, M.L.3    Jorcano, J.L.4
  • 46
    • 0035810042 scopus 로고    scopus 로고
    • The p107 tumor suppressor induces stable E2F DNA binding to repress target promoters
    • O'Connor R.J., Schaley J.E., Feeney G., Hearing P. The p107 tumor suppressor induces stable E2F DNA binding to repress target promoters. Oncogene. 20:2001;1882-1891
    • (2001) Oncogene , vol.20 , pp. 1882-1891
    • O'Connor, R.J.1    Schaley, J.E.2    Feeney, G.3    Hearing, P.4
  • 47
    • 0030690423 scopus 로고    scopus 로고
    • Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH
    • Pearson A., Greenblatt J. Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH. Oncogene. 15:1997;2643-2658
    • (1997) Oncogene , vol.15 , pp. 2643-2658
    • Pearson, A.1    Greenblatt, J.2
  • 48
    • 0032984610 scopus 로고    scopus 로고
    • Activation of the murine dihydrofolate reductase promoter by E2F1: A requirement for CBP recruitment
    • Fry C.J., Pearson A., Malinowski E., Bartley S.M., Greenblatt J., Farnham P.J. Activation of the murine dihydrofolate reductase promoter by E2F1: a requirement for CBP recruitment. J Biol. Chem. 274:1999;15883-15891
    • (1999) J Biol. Chem. , vol.274 , pp. 15883-15891
    • Fry, C.J.1    Pearson, A.2    Malinowski, E.3    Bartley, S.M.4    Greenblatt, J.5    Farnham, P.J.6
  • 49
    • 0032168984 scopus 로고    scopus 로고
    • The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase
    • Ferreira R., Magnaghi-Jaulin L., Robin P., Harel-Bellan A., Trouche D. The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc. Natl. Acad. Sci. USA. 95:1998;10493-10498
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10493-10498
    • Ferreira, R.1    Magnaghi-Jaulin, L.2    Robin, P.3    Harel-Bellan, A.4    Trouche, D.5
  • 50
    • 0028948323 scopus 로고
    • A direct role of transcription factor E2F in c-myc gene expression during granulocytic and macrophage-like differentiation of HL-60 cells
    • Ishida S., Shudo K., Takada S., Koike K. A direct role of transcription factor E2F in c-myc gene expression during granulocytic and macrophage-like differentiation of HL-60 cells. Cell Growth Differ. 6:1995;229-237
    • (1995) Cell Growth Differ. , vol.6 , pp. 229-237
    • Ishida, S.1    Shudo, K.2    Takada, S.3    Koike, K.4
  • 52
    • 0041876082 scopus 로고    scopus 로고
    • Functional reconstitution of Ral-binding GTPase activating protein, RLIP76, in proteoliposomes catalyzing ATP-dependent transport of glutathione conjugate of 4-hydroxynonenal
    • Sharma R., Sharma A., Yang Y., Awasthi S., Yang Y., Singhal S.S., Zimniak P., Awasthi Y.C. Functional reconstitution of Ral-binding GTPase activating protein, RLIP76, in proteoliposomes catalyzing ATP-dependent transport of glutathione conjugate of 4-hydroxynonenal. Acta Biochim Pol. 49:2002;693-701
    • (2002) Acta Biochim Pol. , vol.49 , pp. 693-701
    • Sharma, R.1    Sharma, A.2    Yang, Y.3    Awasthi, S.4    Yang, Y.5    Singhal, S.S.6    Zimniak, P.7    Awasthi, Y.C.8
  • 54
  • 55
    • 0033593225 scopus 로고    scopus 로고
    • Activation of stress signaling pathways by the end product of lipid peroxidation: 4-hydroxy-2-nonenal is a potential inducer of intracellular peroxide production
    • Uchida K., Shiraishi M., Naito Y., Torii Y., Nakamura Y., Osawa T. Activation of stress signaling pathways by the end product of lipid peroxidation: 4-hydroxy-2-nonenal is a potential inducer of intracellular peroxide production. J. Biol. Chem. 274:1999;2234-2242
    • (1999) J. Biol. Chem. , vol.274 , pp. 2234-2242
    • Uchida, K.1    Shiraishi, M.2    Naito, Y.3    Torii, Y.4    Nakamura, Y.5    Osawa, T.6
  • 56
    • 0033985185 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxy-2,3-nonenal increases AP-1-binding activity through caspase activation in neurons
    • Camandola S., Poli G., Mattson M.P. The lipid peroxidation product 4-hydroxy-2,3-nonenal increases AP-1-binding activity through caspase activation in neurons. J. Neurochem. 74:2000;159-168
    • (2000) J. Neurochem. , vol.74 , pp. 159-168
    • Camandola, S.1    Poli, G.2    Mattson, M.P.3
  • 57
    • 0035881921 scopus 로고    scopus 로고
    • Transfection of mGSTA4 in HL-60 cells protects against 4-hydroxynonenal-induced apoptosis by inhibiting JNK-mediated signaling
    • Cheng J.Z., Singhal S.S., Sharma A., Saini M., Yang Y., Awasthi S., Zimniak P., Awasthi Y.C. Transfection of mGSTA4 in HL-60 cells protects against 4-hydroxynonenal-induced apoptosis by inhibiting JNK-mediated signaling. Arch. Biochem. Biophys. 392:2001;197-207
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 197-207
    • Cheng, J.Z.1    Singhal, S.S.2    Sharma, A.3    Saini, M.4    Yang, Y.5    Awasthi, S.6    Zimniak, P.7    Awasthi, Y.C.8
  • 59
    • 0027326559 scopus 로고
    • Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes
    • Uchida K., Szweda L.I., Chae H.Z., Stadtman E.R. Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes. Proc. Natl. Acad. Sci. USA. 90:1993;8742-8746
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8742-8746
    • Uchida, K.1    Szweda, L.I.2    Chae, H.Z.3    Stadtman, E.R.4
  • 60
    • 0034654638 scopus 로고    scopus 로고
    • Deoxyguanosine adducts of t-4-hydroxy-2-nonenal are endogenous DNA lesions in rodents and humans: Detection and potential sources
    • Chung F.L., Nath R.G., Ocando J., Nishikawa A., Zhang L. Deoxyguanosine adducts of t-4-hydroxy-2-nonenal are endogenous DNA lesions in rodents and humans: detection and potential sources. Cancer Res. 60:2000;1507-1511
    • (2000) Cancer Res. , vol.60 , pp. 1507-1511
    • Chung, F.L.1    Nath, R.G.2    Ocando, J.3    Nishikawa, A.4    Zhang, L.5
  • 61
    • 0036850924 scopus 로고    scopus 로고
    • The major lipid peroxidation product, trans-4-hydroxy-2-nonenal, preferentially forms DNA adducts at codon 249 of human p53 gene, a unique mutational hotspot in hepatocellular carcinoma
    • Hu W., Feng Z., Eveleigh J., Iyer G., Pan J., Amin S., Chung F.L., Tang M.S. The major lipid peroxidation product, trans-4-hydroxy-2-nonenal, preferentially forms DNA adducts at codon 249 of human p53 gene, a unique mutational hotspot in hepatocellular carcinoma. Carcinogenesis. 23:2002;1781-1789
    • (2002) Carcinogenesis , vol.23 , pp. 1781-1789
    • Hu, W.1    Feng, Z.2    Eveleigh, J.3    Iyer, G.4    Pan, J.5    Amin, S.6    Chung, F.L.7    Tang, M.S.8
  • 63
  • 64
    • 17144448343 scopus 로고    scopus 로고
    • Interaction between 4-hydroxy-2,3-alkenals and the platelet-derived growth factor beta receptor: Reduced tyrosine phosphorylation and down-stream signaling in hepatic stellate cells
    • Robino G., Parola M., Marra F., CaIigiuri A., De Franco R.M.S., Zamara E., Bellomo G., Gentilini P., Pinzani M., Dianzani M.D. Interaction between 4-hydroxy-2,3-alkenals and the platelet-derived growth factor beta receptor: reduced tyrosine phosphorylation and down-stream signaling in hepatic stellate cells. J. BioI. Chem. 275:2000;40461-40567
    • (2000) J. BioI. Chem. , vol.275 , pp. 40461-40567
    • Robino, G.1    Parola, M.2    Marra, F.3    Caiigiuri, A.4    De Franco, R.M.S.5    Zamara, E.6    Bellomo, G.7    Gentilini, P.8    Pinzani, M.9    Dianzani, M.D.10
  • 65
    • 0021869251 scopus 로고
    • Effects of 4-hydroxynonenal in adenylate cyclase and 5′- nucleotidase activities in rat liver plasma membranes
    • Paradisi L., Panagini C., Parola M., Barrera G., Dianzani M.D. Effects of 4-hydroxynonenal in adenylate cyclase and 5′-nucleotidase activities in rat liver plasma membranes. Chem. Biol. lnteract. 53:1985;209-217
    • (1985) Chem. Biol. Lnteract. , vol.53 , pp. 209-217
    • Paradisi, L.1    Panagini, C.2    Parola, M.3    Barrera, G.4    Dianzani, M.D.5
  • 66
    • 0042689412 scopus 로고
    • Stimulation of 4-hydroxy-2,3-trans-nonenal, a lipid peroxidation production hepatic phospholipase C
    • Rossi M.A., Garramone A., Dianzani M.U. Stimulation of 4-hydroxy-2,3-trans-nonenal, a lipid peroxidation production hepatic phospholipase C. J. Tissue React. 10:1988;323-325
    • (1988) J. Tissue React. , vol.10 , pp. 323-325
    • Rossi, M.A.1    Garramone, A.2    Dianzani, M.U.3
  • 67
    • 0027856040 scopus 로고
    • Effect of 4-hydroxy-2,3-trans-nonenal and related aldehydes on phospholipase C activity of rat neutrophils
    • Rossi M.A., Fidale F., Di Mauro C., Esterbauer H., Dianzani M.U. Effect of 4-hydroxy-2,3-trans-nonenal and related aldehydes on phospholipase C activity of rat neutrophils. Int. J. Tissue React. 15:1993;201-205
    • (1993) Int. J. Tissue React. , vol.15 , pp. 201-205
    • Rossi, M.A.1    Fidale, F.2    Di Mauro, C.3    Esterbauer, H.4    Dianzani, M.U.5
  • 73
  • 74
    • 0025008516 scopus 로고
    • Influence of 4-hydroxynonenal on chemiluminescence production by unstimulated and opsonized zymosan-stimulated human neutrophils
    • Di Mauro C., Cavalli G., Amprimo M.C., Paradisi L., Scano G., Curzio M., Dianzani M.U. Influence of 4-hydroxynonenal on chemiluminescence production by unstimulated and opsonized zymosan-stimulated human neutrophils. Cell Biochem. Funct. 8:1990;147-155
    • (1990) Cell Biochem. Funct. , vol.8 , pp. 147-155
    • Di Mauro, C.1    Cavalli, G.2    Amprimo, M.C.3    Paradisi, L.4    Scano, G.5    Curzio, M.6    Dianzani, M.U.7
  • 75
    • 0029801425 scopus 로고    scopus 로고
    • Effect of 4-hydroxynonenal on superoxide anion production from primed human neutrophils
    • Dianzani C., Parrini M., Ferrara C., Fantozzi R. Effect of 4-hydroxynonenal on superoxide anion production from primed human neutrophils. Cell Biochem. Funct. 14:1996;193-200
    • (1996) Cell Biochem. Funct. , vol.14 , pp. 193-200
    • Dianzani, C.1    Parrini, M.2    Ferrara, C.3    Fantozzi, R.4
  • 76
    • 0030690288 scopus 로고    scopus 로고
    • Biogenic 4-hydroxynonenal activates transcription factor AP-l but not NF-kB in cells of the macrophage lineage
    • Camandola S., Scavazza A., Leonarduzzi G., Biasi F., Chiarpotto E., Azzi A., Poli G. Biogenic 4-hydroxynonenal activates transcription factor AP-l but not NF-kB in cells of the macrophage lineage. BioFactors. 6:1997;173-179
    • (1997) BioFactors , vol.6 , pp. 173-179
    • Camandola, S.1    Scavazza, A.2    Leonarduzzi, G.3    Biasi, F.4    Chiarpotto, E.5    Azzi, A.6    Poli, G.7
  • 77
    • 0033389114 scopus 로고    scopus 로고
    • Effect of 4-hydroxynonenal, a product of lipid peroxidation, on natural cell mediated cytotoxicity
    • Tricarico M., Rinaldi M., Bonmassar E., Fuggetta M.P., Barrera G., Fazio V.M. Effect of 4-hydroxynonenal, a product of lipid peroxidation, on natural cell mediated cytotoxicity. Anticancer Res. 19:1999;5149-5154
    • (1999) Anticancer Res. , vol.19 , pp. 5149-5154
    • Tricarico, M.1    Rinaldi, M.2    Bonmassar, E.3    Fuggetta, M.P.4    Barrera, G.5    Fazio, V.M.6
  • 78
    • 0036889467 scopus 로고    scopus 로고
    • Effect of 4-hydroxynonenal, a lipid peroxidation product, on exocytosis in HL-60 cells
    • Maggiora M., Dianzani M.U., Rossi M.A. Effect of 4-hydroxynonenal, a lipid peroxidation product, on exocytosis in HL-60 cells. Cell Biochem. Funct. 20:2002;303-307
    • (2002) Cell Biochem. Funct. , vol.20 , pp. 303-307
    • Maggiora, M.1    Dianzani, M.U.2    Rossi, M.A.3
  • 79
    • 0027226140 scopus 로고
    • Stimulation of lipid peroxidation or 4-hydroxynonenal treatment increases procollagen alpha (I) gene expression and synthesis in human liver fat-storing cells
    • Parola M., Pinzani M., Casini A., Albano E., Poli G., Gentilini A., Gentilini P., Dianzani M.U. Stimulation of lipid peroxidation or 4-hydroxynonenal treatment increases procollagen alpha (I) gene expression and synthesis in human liver fat-storing cells. Biochem. Biophys. Res. Commun. 194:1993;1044-1050
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1044-1050
    • Parola, M.1    Pinzani, M.2    Casini, A.3    Albano, E.4    Poli, G.5    Gentilini, A.6    Gentilini, P.7    Dianzani, M.U.8
  • 80
    • 0343446113 scopus 로고    scopus 로고
    • Lipid metabolite involvement in the activation of the human heme oxygenase-1 gene
    • Basu-Modak S., Luscher P., Tyrrell R.M. Lipid metabolite involvement in the activation of the human heme oxygenase-1 gene. Free Radic. Biol. Med. 20:1996;887-897
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 887-897
    • Basu-Modak, S.1    Luscher, P.2    Tyrrell, R.M.3
  • 81
    • 0030756676 scopus 로고    scopus 로고
    • The lipid peroxidation end product 4-hydroxy-2,3-nonenal upregulates transforming growth factor beta l expression in the macrophage lineage: A link between oxidative injury and fibrosclerosis
    • Leonarduzzi G., Scavazza A., Biasi F., Chiarpotto E., Camandola S., Vogel S., Dargel R., Poli G. The lipid peroxidation end product 4-hydroxy-2,3-nonenal upregulates transforming growth factor beta l expression in the macrophage lineage: a link between oxidative injury and fibrosclerosis. FASEB J. 11:1997;851-857
    • (1997) FASEB J. , vol.11 , pp. 851-857
    • Leonarduzzi, G.1    Scavazza, A.2    Biasi, F.3    Chiarpotto, E.4    Camandola, S.5    Vogel, S.6    Dargel, R.7    Poli, G.8
  • 86
    • 0032562272 scopus 로고    scopus 로고
    • Induction of rat aortic smooth muscle cell growth by the lipid peroxidation product 4-hydroxy-2-nonenal
    • Ruef J., Rao G.N., Li F., Bode C., Patterson C., Bhatnagar A., Runge M.S. Induction of rat aortic smooth muscle cell growth by the lipid peroxidation product 4-hydroxy-2-nonenal. Circulation. 97:1998;1071-1078
    • (1998) Circulation , vol.97 , pp. 1071-1078
    • Ruef, J.1    Rao, G.N.2    Li, F.3    Bode, C.4    Patterson, C.5    Bhatnagar, A.6    Runge, M.S.7
  • 87
    • 0031577288 scopus 로고    scopus 로고
    • Modulation of human T-lymphocyte proliferation by 4-hydroxynonenal, the bioactive product of neutrophil-dependent lipid peroxidation
    • Cambiaggi C., Dominici S., Comporti M., Pompella A. Modulation of human T-lymphocyte proliferation by 4-hydroxynonenal, the bioactive product of neutrophil-dependent lipid peroxidation. Life Sci. 61:1997;777-785
    • (1997) Life Sci. , vol.61 , pp. 777-785
    • Cambiaggi, C.1    Dominici, S.2    Comporti, M.3    Pompella, A.4
  • 88
    • 0036468883 scopus 로고    scopus 로고
    • Synergistic effect of 4-hydroxynonenal and PPAR ligands in controlling human leukemic cell growth and differentiation
    • Pizzimenti S., Laurora S., Briatore F., Ferretti C., Dianzani M.U., Barrera G. Synergistic effect of 4-hydroxynonenal and PPAR ligands in controlling human leukemic cell growth and differentiation. Free Radic. Biol. Med. 32:2002;233-245
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 233-245
    • Pizzimenti, S.1    Laurora, S.2    Briatore, F.3    Ferretti, C.4    Dianzani, M.U.5    Barrera, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.