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Volumn 320, Issue 2, 2012, Pages 150-157

A-class prostaglandins: Early findings and new perspectives for overcoming tumor chemoresistance

Author keywords

AKR1B10; Chemoresistance; Cyclopentenone; GST

Indexed keywords

13,14 DIHYDRO 15 DEOXY DELTA7 PROSTAGLANDIN A1 METHYL ESTER; 15 HYDROXY 9 OXOPROSTA 7,10,13 TRIENOIC ACID; 3,4 DIHYDRO 2,8 DIISOPROPYL 3 THIOXO 2H 1,4 BENZOXAZINE 4 ACETIC ACID; 8 ISO PROSTAGLANDIN A1; 8 ISO PROSTAGLANDIN A2; ABC TRANSPORTER; AKR 1B10; ANTHRACYCLINE DERIVATIVE; CISPLATIN; DAUNORUBICIN; DNA TOPOISOMERASE; DOXORUBICIN; ETOPOSIDE; GLUTATHIONE; METHOTREXATE; MITOXANTRONE; PACLITAXEL; PROSTAGLANDIN A; PROSTAGLANDIN A1; PROSTAGLANDIN A2; UNCLASSIFIED DRUG;

EID: 84859625071     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2012.03.003     Document Type: Review
Times cited : (25)

References (85)
  • 1
    • 53849096994 scopus 로고    scopus 로고
    • An overview of cancer multidrug resistance: a still unsolved problem
    • Lage H. An overview of cancer multidrug resistance: a still unsolved problem. Cell. Mol. Life Sci. 2008, 65:3145-3167.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3145-3167
    • Lage, H.1
  • 2
    • 80053426842 scopus 로고    scopus 로고
    • Targeted therapies for breast cancer
    • Higgins M.J., Baselga J. Targeted therapies for breast cancer. J. Clin. Invest. 2011, 121:3797-3803.
    • (2011) J. Clin. Invest. , vol.121 , pp. 3797-3803
    • Higgins, M.J.1    Baselga, J.2
  • 3
    • 0014026978 scopus 로고
    • Prostaglandins in human seminal plasma. Prostaglandins and related factors 46
    • Hamberg M., Samuelsson B. Prostaglandins in human seminal plasma. Prostaglandins and related factors 46. J. Biol. Chem. 1966, 241:257-263.
    • (1966) J. Biol. Chem. , vol.241 , pp. 257-263
    • Hamberg, M.1    Samuelsson, B.2
  • 5
    • 0033977323 scopus 로고    scopus 로고
    • Metabolism of polyunsaturated fatty acids by skin epidermal enzymes: generation of antiinflammatory and antiproliferative metabolites
    • Ziboh V.A., Miller C.C., Cho Y. Metabolism of polyunsaturated fatty acids by skin epidermal enzymes: generation of antiinflammatory and antiproliferative metabolites. Am. J. Clin. Nutr. 2000, 71:361S-366S.
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Ziboh, V.A.1    Miller, C.C.2    Cho, Y.3
  • 6
    • 0035976575 scopus 로고    scopus 로고
    • Prostaglandins and leukotrienes: advances in eicosanoid biology
    • Funk C.D. Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 2001, 294:1871-1875.
    • (2001) Science , vol.294 , pp. 1871-1875
    • Funk, C.D.1
  • 7
    • 0022542070 scopus 로고
    • Inhibition of human melanoma growth by prostaglandin A, D, and J analogues
    • Bregman M.D., Funk C., Fukushima M. Inhibition of human melanoma growth by prostaglandin A, D, and J analogues. Cancer Res. 1986, 46:2740-2744.
    • (1986) Cancer Res. , vol.46 , pp. 2740-2744
    • Bregman, M.D.1    Funk, C.2    Fukushima, M.3
  • 8
    • 0022655430 scopus 로고
    • Antitumor activity of delta 7-prostaglandin A1 and delta 12-prostaglandin J2 in vitro and in vivo
    • Kato T., Fukushima M., Kurozumi S., Noyori R. Antitumor activity of delta 7-prostaglandin A1 and delta 12-prostaglandin J2 in vitro and in vivo. Cancer Res. 1986, 46:3538-3542.
    • (1986) Cancer Res. , vol.46 , pp. 3538-3542
    • Kato, T.1    Fukushima, M.2    Kurozumi, S.3    Noyori, R.4
  • 9
    • 0033566762 scopus 로고    scopus 로고
    • Antitumor activity of 13,14-dihydro-15-deoxy-delta7-prostaglandin-A1-methyl ester integrated into lipid microspheres against human ovarian carcinoma cells resistant to cisplatin in vivo
    • Sasaki H., Niimi S., Akiyama M., Tanaka T., Hazato A., Kurozumi S., Fukushima S., Fukushima M. Antitumor activity of 13,14-dihydro-15-deoxy-delta7-prostaglandin-A1-methyl ester integrated into lipid microspheres against human ovarian carcinoma cells resistant to cisplatin in vivo. Cancer Res. 1999, 59:3919-3922.
    • (1999) Cancer Res. , vol.59 , pp. 3919-3922
    • Sasaki, H.1    Niimi, S.2    Akiyama, M.3    Tanaka, T.4    Hazato, A.5    Kurozumi, S.6    Fukushima, S.7    Fukushima, M.8
  • 10
    • 0032535082 scopus 로고    scopus 로고
    • Anti-cancer-prostaglandin-induced cell-cycle arrest and its modulation by an inhibitor of the ATP-dependent glutathione S-conjugate export pump (GS-X pump)
    • Ishikawa T., Akimaru K., Nakanishi M., Tomokiyo K., Furuta K., Suzuki M., Noyori R. Anti-cancer-prostaglandin-induced cell-cycle arrest and its modulation by an inhibitor of the ATP-dependent glutathione S-conjugate export pump (GS-X pump). Biochem. J. 1998, 336:569-576.
    • (1998) Biochem. J. , vol.336 , pp. 569-576
    • Ishikawa, T.1    Akimaru, K.2    Nakanishi, M.3    Tomokiyo, K.4    Furuta, K.5    Suzuki, M.6    Noyori, R.7
  • 11
    • 0038752800 scopus 로고    scopus 로고
    • Involvement of c-jun N-terminal kinase activation in 15-deoxy-delta12,14-prostaglandin J2-and prostaglandin A1-induced apoptosis in AGS gastric epithelial cells
    • Liu J.D., Lin S.Y., Ho Y.S., Pan S., Hung L.F., Tsai S.H., Lin J.K., Liang Y.C. Involvement of c-jun N-terminal kinase activation in 15-deoxy-delta12,14-prostaglandin J2-and prostaglandin A1-induced apoptosis in AGS gastric epithelial cells. Mol. Carcinog. 2003, 37:16-24.
    • (2003) Mol. Carcinog. , vol.37 , pp. 16-24
    • Liu, J.D.1    Lin, S.Y.2    Ho, Y.S.3    Pan, S.4    Hung, L.F.5    Tsai, S.H.6    Lin, J.K.7    Liang, Y.C.8
  • 12
    • 0028580432 scopus 로고
    • Preclinical studies of antitumor prostaglandins by using human ovarian cancer cells
    • Kikuchi Y., Kita T., Hirata J., Fukushima M. Preclinical studies of antitumor prostaglandins by using human ovarian cancer cells. Cancer Metast. Rev. 1994, 13:309-315.
    • (1994) Cancer Metast. Rev. , vol.13 , pp. 309-315
    • Kikuchi, Y.1    Kita, T.2    Hirata, J.3    Fukushima, M.4
  • 13
    • 0021879439 scopus 로고
    • Requirement of a reactive alpha, beta-unsaturated carbonyl for inhibition of tumor growth and induction of differentiation by "A" series prostaglandins
    • Honn K.V., Marnett L.J. Requirement of a reactive alpha, beta-unsaturated carbonyl for inhibition of tumor growth and induction of differentiation by "A" series prostaglandins. Biochem. Biophys. Res. Commun. 1985, 129:34-40.
    • (1985) Biochem. Biophys. Res. Commun. , vol.129 , pp. 34-40
    • Honn, K.V.1    Marnett, L.J.2
  • 14
    • 0022845732 scopus 로고
    • Modulation of the growth of a human erythroleukemic cell line (K562) by prostaglandins: antiproliferative action of prostaglandin A
    • Santoro M.G., Crisari A., Benedetto A., Amici C. Modulation of the growth of a human erythroleukemic cell line (K562) by prostaglandins: antiproliferative action of prostaglandin A. Cancer Res. 1986, 46:6073-6077.
    • (1986) Cancer Res. , vol.46 , pp. 6073-6077
    • Santoro, M.G.1    Crisari, A.2    Benedetto, A.3    Amici, C.4
  • 15
    • 0030737735 scopus 로고    scopus 로고
    • Antiviral activity of cyclopentenone prostanoids
    • Santoro M.G. Antiviral activity of cyclopentenone prostanoids. Trends Microbiol. 1997, 5:276-281.
    • (1997) Trends Microbiol. , vol.5 , pp. 276-281
    • Santoro, M.G.1
  • 16
    • 0037053290 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma agonists inhibit HIV-1 replication in macrophages by transcriptional and post-transcriptional effects
    • Hayes M.M., Lane B.R., King S.R., Markovitz D.M., Coffey M.J. Peroxisome proliferator-activated receptor gamma agonists inhibit HIV-1 replication in macrophages by transcriptional and post-transcriptional effects. J. Biol. Chem. 2002, 277:16913-16919.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16913-16919
    • Hayes, M.M.1    Lane, B.R.2    King, S.R.3    Markovitz, D.M.4    Coffey, M.J.5
  • 17
    • 0035800780 scopus 로고    scopus 로고
    • Activation of I kappa b kinase by herpes simplex virus type 1. A novel target for anti-herpetic therapy
    • Amici C., Belardo G., Rossi A., Santoro M.G. Activation of I kappa b kinase by herpes simplex virus type 1. A novel target for anti-herpetic therapy. J. Biol. Chem. 2001, 276:28759-28766.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28759-28766
    • Amici, C.1    Belardo, G.2    Rossi, A.3    Santoro, M.G.4
  • 18
    • 33745401240 scopus 로고    scopus 로고
    • Specific binding of heat shock protein 70 with HN-protein inhibits the HN-protein assembly in Sendai virus-infected Vero cells
    • Hirayama E., Hattori M., Kim J. Specific binding of heat shock protein 70 with HN-protein inhibits the HN-protein assembly in Sendai virus-infected Vero cells. Virus Res. 2006, 120:199-207.
    • (2006) Virus Res. , vol.120 , pp. 199-207
    • Hirayama, E.1    Hattori, M.2    Kim, J.3
  • 19
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkB kinase
    • Rossi A., Kapahi P., Natoli G., Takahashi T., Chen Y., Karin M., Santoro M.G. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkB kinase. Nature 2000, 403:103-108.
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 24
    • 0021038651 scopus 로고
    • Development of antineoplastic prostaglandins
    • Fukushima M. Development of antineoplastic prostaglandins. Gan To Kagaku Ryoho 1983, 10:1930-1935.
    • (1983) Gan To Kagaku Ryoho , vol.10 , pp. 1930-1935
    • Fukushima, M.1
  • 25
    • 79958065568 scopus 로고    scopus 로고
    • Electrophilic eicosanoids: signaling and targets
    • Pérez-Sala D. Electrophilic eicosanoids: signaling and targets. Chem. Biol. Interact. 2011, 192:96-100.
    • (2011) Chem. Biol. Interact. , vol.192 , pp. 96-100
    • Pérez-Sala, D.1
  • 26
    • 77952902184 scopus 로고    scopus 로고
    • Anti-inflammatory prostanoids: focus on the interactions between electrophile signalling and resolution of inflammation
    • Díez-Dacal B., Pérez-Sala D. Anti-inflammatory prostanoids: focus on the interactions between electrophile signalling and resolution of inflammation. ScientificWorldJournal 2010, 10:655-675.
    • (2010) ScientificWorldJournal , vol.10 , pp. 655-675
    • Díez-Dacal, B.1    Pérez-Sala, D.2
  • 27
    • 79958849861 scopus 로고    scopus 로고
    • Proteomic studies on protein modification by cyclopentenone prostaglandins: expanding our view on electrophile actions
    • Garzón B., Oeste C.L., Díez-Dacal B., Pérez-Sala D. Proteomic studies on protein modification by cyclopentenone prostaglandins: expanding our view on electrophile actions. J. Proteom. 2011, 74:2243-2263.
    • (2011) J. Proteom. , vol.74 , pp. 2243-2263
    • Garzón, B.1    Oeste, C.L.2    Díez-Dacal, B.3    Pérez-Sala, D.4
  • 29
    • 0034614206 scopus 로고    scopus 로고
    • Preparation and evaluation of o/w type emulsions containing antitumor prostaglandin
    • Fukushima S., Kishimoto S., Takeuchi Y., Fukushima M. Preparation and evaluation of o/w type emulsions containing antitumor prostaglandin. Adv. Drug Deliv. Rev. 2000, 45:65-75.
    • (2000) Adv. Drug Deliv. Rev. , vol.45 , pp. 65-75
    • Fukushima, S.1    Kishimoto, S.2    Takeuchi, Y.3    Fukushima, M.4
  • 30
    • 0020700123 scopus 로고
    • Evidence for cAMP-independent inhibition of S-phase DNA synthesis by prostaglandins
    • Wiley M.H., Feingold K.R., Grunfeld C., Quesney-Huneeus V., Wu J.M. Evidence for cAMP-independent inhibition of S-phase DNA synthesis by prostaglandins. J. Biol. Chem. 1983, 258:491-496.
    • (1983) J. Biol. Chem. , vol.258 , pp. 491-496
    • Wiley, M.H.1    Feingold, K.R.2    Grunfeld, C.3    Quesney-Huneeus, V.4    Wu, J.M.5
  • 31
    • 0023932966 scopus 로고
    • Inhibitory effects of prostaglandin A2 on c-myc expression and cell cycle progression in human leukemia cell line HL-60
    • Ishioka C., Kanamaru R., Sato T., Dei T., Konishi Y., Asamura M., Wakui A. Inhibitory effects of prostaglandin A2 on c-myc expression and cell cycle progression in human leukemia cell line HL-60. Cancer Res. 1988, 48:2813-2818.
    • (1988) Cancer Res. , vol.48 , pp. 2813-2818
    • Ishioka, C.1    Kanamaru, R.2    Sato, T.3    Dei, T.4    Konishi, Y.5    Asamura, M.6    Wakui, A.7
  • 32
    • 85047680422 scopus 로고    scopus 로고
    • Prostaglandin A2 specifically represses insulin-like growth factor-I gene expression in C6 rat glioma cells
    • Bui T., Kuo C., Rotwein P., Straus D.S. Prostaglandin A2 specifically represses insulin-like growth factor-I gene expression in C6 rat glioma cells. Endocrinology 1997, 138:985-993.
    • (1997) Endocrinology , vol.138 , pp. 985-993
    • Bui, T.1    Kuo, C.2    Rotwein, P.3    Straus, D.S.4
  • 33
    • 0026574274 scopus 로고
    • Cell growth inhibition by prostaglandin A2 results in elevated expression of gadd153 mRNA
    • Choi A.M., Fargnoli J., Carlson S.G., Holbrook N.J. Cell growth inhibition by prostaglandin A2 results in elevated expression of gadd153 mRNA. Exp. Cell Res. 1992, 199:85-89.
    • (1992) Exp. Cell Res. , vol.199 , pp. 85-89
    • Choi, A.M.1    Fargnoli, J.2    Carlson, S.G.3    Holbrook, N.J.4
  • 34
    • 0029670838 scopus 로고    scopus 로고
    • Inhibition of G1 cyclin-dependent kinase activity during growth arrest of human breast carcinoma cells by prostaglandin A2
    • Gorospe M., Liu Y., Xu Q., Chrest F.J., Holbrook N.J. Inhibition of G1 cyclin-dependent kinase activity during growth arrest of human breast carcinoma cells by prostaglandin A2. Mol. Cell. Biol. 1996, 16:762-770.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 762-770
    • Gorospe, M.1    Liu, Y.2    Xu, Q.3    Chrest, F.J.4    Holbrook, N.J.5
  • 36
    • 33748854572 scopus 로고    scopus 로고
    • Influence of prostaglandin A2 on Bax, Bcl-2 and PCNA expression in MCF-7 cells
    • Joubert A., Bianchi P., Maritz C., Joubert F. Influence of prostaglandin A2 on Bax, Bcl-2 and PCNA expression in MCF-7 cells. Biomed. Res. 2006, 27:157-162.
    • (2006) Biomed. Res. , vol.27 , pp. 157-162
    • Joubert, A.1    Bianchi, P.2    Maritz, C.3    Joubert, F.4
  • 40
    • 33947576648 scopus 로고    scopus 로고
    • Prostanoids with cyclopentenone structure as tools for the characterization of electrophilic eicosanoid-protein interactomes
    • Stamatakis K., Pérez-Sala D. Prostanoids with cyclopentenone structure as tools for the characterization of electrophilic eicosanoid-protein interactomes. Ann. N.Y. Acad. Sci. 2006, 1091:548-570.
    • (2006) Ann. N.Y. Acad. Sci. , vol.1091 , pp. 548-570
    • Stamatakis, K.1    Pérez-Sala, D.2
  • 42
    • 77950371207 scopus 로고    scopus 로고
    • Heat-shock protein 70 binds to a novel sequence in 5' UTR of tumor suppressor SMAR1 and regulates its mRNA stability upon prostaglandin A2 treatment
    • Pavithra L., Sreenath K., Singh S., Chattopadhyay S. Heat-shock protein 70 binds to a novel sequence in 5' UTR of tumor suppressor SMAR1 and regulates its mRNA stability upon prostaglandin A2 treatment. FEBS Lett. 2010, 584:1187-1192.
    • (2010) FEBS Lett. , vol.584 , pp. 1187-1192
    • Pavithra, L.1    Sreenath, K.2    Singh, S.3    Chattopadhyay, S.4
  • 44
    • 0025254113 scopus 로고
    • Growth inhibition of Friend erythroleukaemia cell tumours in vivo by a synthetic analogue of prostaglandin A: an action independent of natural killer-activity
    • Marini S., Palamara A.T., Garaci E., Santoro M.G. Growth inhibition of Friend erythroleukaemia cell tumours in vivo by a synthetic analogue of prostaglandin A: an action independent of natural killer-activity. Br. J. Cancer 1990, 61:394-399.
    • (1990) Br. J. Cancer , vol.61 , pp. 394-399
    • Marini, S.1    Palamara, A.T.2    Garaci, E.3    Santoro, M.G.4
  • 46
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signaling: the role of cysteine modification in controlling antioxidant defenses in response to electrophilic lipid oxidation products
    • Levonen A.L., Landar A., Ramachandran A., Ceaser E.K., Dickinson D.A., Zanoni G., Morrow J.D., Darley-Usmar V.M. Cellular mechanisms of redox cell signaling: the role of cysteine modification in controlling antioxidant defenses in response to electrophilic lipid oxidation products. Biochem. J. 2004, 378:373-382.
    • (2004) Biochem. J. , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 49
    • 33746211260 scopus 로고    scopus 로고
    • Induction of Fas clustering and apoptosis by coral prostanoid in human hormone-resistant prostate cancer cells
    • Chiang P.C., Kung F.L., Huang D.M., Li T.K., Fan J.R., Pan S.L., Shen Y.C., Guh J.H. Induction of Fas clustering and apoptosis by coral prostanoid in human hormone-resistant prostate cancer cells. Eur. J. Pharmacol. 2006, 542:22-30.
    • (2006) Eur. J. Pharmacol. , vol.542 , pp. 22-30
    • Chiang, P.C.1    Kung, F.L.2    Huang, D.M.3    Li, T.K.4    Fan, J.R.5    Pan, S.L.6    Shen, Y.C.7    Guh, J.H.8
  • 51
    • 0026719642 scopus 로고
    • Adjuvant effects of antineoplastic prostaglandins to cisplatin in nude mice bearing human ovarian cancer cells
    • Kikuchi Y., Kita T., Miyauchi M., Hirata J., Sasa H., Nagata I., Fukushima M. Adjuvant effects of antineoplastic prostaglandins to cisplatin in nude mice bearing human ovarian cancer cells. J. Cancer Res. Clin. Oncol. 1992, 118:453-457.
    • (1992) J. Cancer Res. Clin. Oncol. , vol.118 , pp. 453-457
    • Kikuchi, Y.1    Kita, T.2    Miyauchi, M.3    Hirata, J.4    Sasa, H.5    Nagata, I.6    Fukushima, M.7
  • 52
    • 0028302217 scopus 로고
    • Prostaglandins in the treatment of cancer
    • Sasaki H., Fukushima M. Prostaglandins in the treatment of cancer. Anticancer Drugs 1994, 5:131-138.
    • (1994) Anticancer Drugs , vol.5 , pp. 131-138
    • Sasaki, H.1    Fukushima, M.2
  • 53
    • 73949135792 scopus 로고    scopus 로고
    • Mechanisms of multidrug resistance in cancer
    • Gillet J.P., Gottesman M.M. Mechanisms of multidrug resistance in cancer. Methods Mol. Biol. 2010, 596:47-76.
    • (2010) Methods Mol. Biol. , vol.596 , pp. 47-76
    • Gillet, J.P.1    Gottesman, M.M.2
  • 55
    • 0032176019 scopus 로고    scopus 로고
    • Inhibition of topoisomerases by antitumor prostaglandins
    • Suzuki K., Shono F., Uyeda M. Inhibition of topoisomerases by antitumor prostaglandins. Biosci. Biotechnol. Biochem. 1998, 62:2073-2075.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 2073-2075
    • Suzuki, K.1    Shono, F.2    Uyeda, M.3
  • 56
    • 0036689688 scopus 로고    scopus 로고
    • Inhibitory properties of antitumor prostaglandins against topoisomerases
    • Suzuki K., Uyeda M. Inhibitory properties of antitumor prostaglandins against topoisomerases. Biosci. Biotechnol. Biochem. 2002, 66:1706-1712.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1706-1712
    • Suzuki, K.1    Uyeda, M.2
  • 57
    • 2442704131 scopus 로고    scopus 로고
    • All in the family: aldose reductase and closely related aldo-keto reductases
    • Petrash J.M. All in the family: aldose reductase and closely related aldo-keto reductases. Cell. Mol. Life Sci. 2004, 61:737-749.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 737-749
    • Petrash, J.M.1
  • 58
    • 35348887886 scopus 로고    scopus 로고
    • Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention
    • Yan R., Zu X., Ma J., Liu Z., Adeyanju M., Cao D. Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention. Int. J. Cancer 2007, 121:2301-2306.
    • (2007) Int. J. Cancer , vol.121 , pp. 2301-2306
    • Yan, R.1    Zu, X.2    Ma, J.3    Liu, Z.4    Adeyanju, M.5    Cao, D.6
  • 59
    • 33344470911 scopus 로고    scopus 로고
    • Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics
    • Martin H.J., Breyer-Pfaff U., Wsol V., Venz S., Block S., Maser E. Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics. Drug Metab. Dispos. 2006, 34:464-470.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 464-470
    • Martin, H.J.1    Breyer-Pfaff, U.2    Wsol, V.3    Venz, S.4    Block, S.5    Maser, E.6
  • 60
    • 0034578076 scopus 로고    scopus 로고
    • Prostaglandin A1 inhibits stress-induced NF-kappaB activation and reverses resistance to topoisomerase II inhibitors
    • Boller Y.C., Brandes L.M., Russell R.L., Lin Z.P., Patierno S.R., Kennedy K.A. Prostaglandin A1 inhibits stress-induced NF-kappaB activation and reverses resistance to topoisomerase II inhibitors. Oncol. Res. 2000, 12:383-395.
    • (2000) Oncol. Res. , vol.12 , pp. 383-395
    • Boller, Y.C.1    Brandes, L.M.2    Russell, R.L.3    Lin, Z.P.4    Patierno, S.R.5    Kennedy, K.A.6
  • 61
    • 33751161701 scopus 로고    scopus 로고
    • Induction of apoptosis in estrogen receptor-negative breast cancer cells by natural and synthetic cyclopentenones: role of the IkappaB kinase/nuclear factor-kappaB pathway
    • Ciucci A., Gianferretti P., Piva R., Guyot T., Snape T.J., Roberts S.M., Santoro M.G. Induction of apoptosis in estrogen receptor-negative breast cancer cells by natural and synthetic cyclopentenones: role of the IkappaB kinase/nuclear factor-kappaB pathway. Mol. Pharmacol. 2006, 70:1812-1821.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1812-1821
    • Ciucci, A.1    Gianferretti, P.2    Piva, R.3    Guyot, T.4    Snape, T.J.5    Roberts, S.M.6    Santoro, M.G.7
  • 62
    • 0016591103 scopus 로고
    • The conjugation of prostaglandin A1 and glutathione catalyzed by homogeneous glutathione S-transferases from human and rat liver
    • Cagen L.M., Pisano J.J., Ketley J.N., Habig W.H., Jakoby W.B. The conjugation of prostaglandin A1 and glutathione catalyzed by homogeneous glutathione S-transferases from human and rat liver. Biochim. Biophys. Acta 1975, 398:205-208.
    • (1975) Biochim. Biophys. Acta , vol.398 , pp. 205-208
    • Cagen, L.M.1    Pisano, J.J.2    Ketley, J.N.3    Habig, W.H.4    Jakoby, W.B.5
  • 65
    • 2542456661 scopus 로고    scopus 로고
    • Reactions of some cyclopentenones with selected cysteine derivatives and biological activities of the product thioethers
    • Bickley J.F., Ciucci A., Evans P., Roberts S.M., Ross N., Santoro G.M. Reactions of some cyclopentenones with selected cysteine derivatives and biological activities of the product thioethers. Bioorg. Med. Chem. 2004, 12:3221-3227.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3221-3227
    • Bickley, J.F.1    Ciucci, A.2    Evans, P.3    Roberts, S.M.4    Ross, N.5    Santoro, G.M.6
  • 66
    • 0027473175 scopus 로고
    • Organic synthesis of prostaglandins: advancing biology
    • Noyori R., Suzuki M. Organic synthesis of prostaglandins: advancing biology. Science 1993, 259:44-45.
    • (1993) Science , vol.259 , pp. 44-45
    • Noyori, R.1    Suzuki, M.2
  • 70
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 2000, 267:4928-4944.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 72
    • 77957224442 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins with dienone structure promote cross-linking of the chemoresistance-inducing enzyme glutathione transferase P1-1
    • Sánchez-Gómez F.J., Díez-Dacal B., Pajares M.A., Llorca O., Pérez-Sala D. Cyclopentenone prostaglandins with dienone structure promote cross-linking of the chemoresistance-inducing enzyme glutathione transferase P1-1. Mol. Pharmacol. 2010, 78:723-733.
    • (2010) Mol. Pharmacol. , vol.78 , pp. 723-733
    • Sánchez-Gómez, F.J.1    Díez-Dacal, B.2    Pajares, M.A.3    Llorca, O.4    Pérez-Sala, D.5
  • 73
    • 33846003462 scopus 로고    scopus 로고
    • Direct evidence for the covalent modification of glutathione-S-transferase P1-1 by electrophilic prostaglandins: implications for enzyme inactivation and cell survival
    • Sánchez-Gómez F.J., Gayarre J., Avellano M.I., Pérez-Sala D. Direct evidence for the covalent modification of glutathione-S-transferase P1-1 by electrophilic prostaglandins: implications for enzyme inactivation and cell survival. Arch. Biochem. Biophys. 2007, 457:150-159.
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 150-159
    • Sánchez-Gómez, F.J.1    Gayarre, J.2    Avellano, M.I.3    Pérez-Sala, D.4
  • 75
    • 79954416526 scopus 로고    scopus 로고
    • The cytoprotective role of the Keap1-Nrf2 pathway
    • Baird L., Dinkova-Kostova A.T. The cytoprotective role of the Keap1-Nrf2 pathway. Arch. Toxicol. 2011, 85:241-272.
    • (2011) Arch. Toxicol. , vol.85 , pp. 241-272
    • Baird, L.1    Dinkova-Kostova, A.T.2
  • 78
    • 33845357331 scopus 로고    scopus 로고
    • Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles
    • Cassidy P., Edes K., Nelson C., Parsawar K., Fitzpatrick F., Moos P. Thioredoxin reductase is required for the inactivation of tumor suppressor p53 and for apoptosis induced by endogenous electrophiles. Carcinogenesis 2006, 27:2538-2549.
    • (2006) Carcinogenesis , vol.27 , pp. 2538-2549
    • Cassidy, P.1    Edes, K.2    Nelson, C.3    Parsawar, K.4    Fitzpatrick, F.5    Moos, P.6
  • 80
    • 0043237307 scopus 로고    scopus 로고
    • Glutathione S transferase pi indicates chemotherapy resistance in breast cancer
    • Su F., Hu X., Jia W., Gong C., Song E., Hamar P. Glutathione S transferase pi indicates chemotherapy resistance in breast cancer. J. Surg. Res. 2003, 113:102-108.
    • (2003) J. Surg. Res. , vol.113 , pp. 102-108
    • Su, F.1    Hu, X.2    Jia, W.3    Gong, C.4    Song, E.5    Hamar, P.6
  • 82
    • 37149023303 scopus 로고    scopus 로고
    • Anti-inflammatory lipid mediator 15d-PGJ2 inhibits translation through inactivation of eIF4A
    • Kim W.J., Kim J.H., Jang S.K. Anti-inflammatory lipid mediator 15d-PGJ2 inhibits translation through inactivation of eIF4A. EMBO J. 2007, 26:5020-5032.
    • (2007) EMBO J. , vol.26 , pp. 5020-5032
    • Kim, W.J.1    Kim, J.H.2    Jang, S.K.3
  • 83
    • 78149448121 scopus 로고    scopus 로고
    • Alkylation of the tumor suppressor PTEN activates Akt and beta-catenin signaling: a mechanism linking inflammation and oxidative stress with cancer
    • Covey T.M., Edes K., Coombs G.S., Virshup D.M., Fitzpatrick F.A. Alkylation of the tumor suppressor PTEN activates Akt and beta-catenin signaling: a mechanism linking inflammation and oxidative stress with cancer. PLoS One 2010, 5:e13545.
    • (2010) PLoS One , vol.5
    • Covey, T.M.1    Edes, K.2    Coombs, G.S.3    Virshup, D.M.4    Fitzpatrick, F.A.5
  • 84
    • 77958140054 scopus 로고    scopus 로고
    • The Nrf2-Keap1-ARE signaling pathway: the regulation and dual function of Nrf2 in cancer
    • Zhang D.D. The Nrf2-Keap1-ARE signaling pathway: the regulation and dual function of Nrf2 in cancer. Antioxid. Redox Signal. 2010, 13:1623-1626.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1623-1626
    • Zhang, D.D.1
  • 85
    • 79957558400 scopus 로고    scopus 로고
    • Regulation of aldo-keto reductase AKR1B10 gene expression: involvement of transcription factor Nrf2
    • Nishinaka T., Miura T., Okumura M., Nakao F., Nakamura H., Terada T. Regulation of aldo-keto reductase AKR1B10 gene expression: involvement of transcription factor Nrf2. Chem. Biol. Interact. 2011, 191:185-191.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 185-191
    • Nishinaka, T.1    Miura, T.2    Okumura, M.3    Nakao, F.4    Nakamura, H.5    Terada, T.6


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