메뉴 건너뛰기




Volumn 51, Issue 23, 2008, Pages 7356-7369

Novel multifunctional acyloxyalkyl ester prodrugs of 5-aminolevulinic acid display improved anticancer activity independent and dependent on photoactivation

Author keywords

[No Author keywords available]

Indexed keywords

1 (BUTYRYLOXY)ETHYL 5 AMINO 4 OXOPENTANOATE; AMINOLEVULINIC ACID; BUTYRIC ACID; BUTYRYLOXYMETHYL 5 AMINO 4 OXOPENTANOATE; ESTER DERIVATIVE; FORMALDEHYDE; HISTONE H2AX; MYC PROTEIN; PIVALIC ACID; PRODRUG; PROTEASOME; PROTEIN P21; PROTOPORPHYRIN; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 57349168030     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm8008794     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 0025862375 scopus 로고
    • Derivatives of butyric acid as potential anti-neoplastic agents
    • Rephaeli, A.; Shaklai, M.; Ruse, M.; Nudelman, A. Derivatives of butyric acid as potential anti-neoplastic agents. Int. J. Cancer 1991, 49, 66-72.
    • (1991) Int. J. Cancer , vol.49 , pp. 66-72
    • Rephaeli, A.1    Shaklai, M.2    Ruse, M.3    Nudelman, A.4
  • 2
    • 0027316830 scopus 로고
    • Rapid alteration of c-myc and c-jun expression in leukemic cells induced to differentiate by a butyric acid prodrug
    • Rabizadeh, E.; Shaklai, M.; Nudelman, A.; Eisenbach, L.; Rephaeli, A. Rapid alteration of c-myc and c-jun expression in leukemic cells induced to differentiate by a butyric acid prodrug. FEBS Lett. 1993, 328, 225-229.
    • (1993) FEBS Lett , vol.328 , pp. 225-229
    • Rabizadeh, E.1    Shaklai, M.2    Nudelman, A.3    Eisenbach, L.4    Rephaeli, A.5
  • 3
    • 0028219470 scopus 로고
    • Comparison between the effect of butyric acid and its prodrug pivaloyloxymethyl butyrate on histones hyperacetylation in an HL-60 leukemic cell line
    • Aviram, A.; Zimrah, Y.; Shaklai, M.; Nudelman, A.; Rephaeli, A. Comparison between the effect of butyric acid and its prodrug pivaloyloxymethyl butyrate on histones hyperacetylation in an HL-60 leukemic cell line. Int. J. Cancer 1994, 56, 906-909.
    • (1994) Int. J. Cancer , vol.56 , pp. 906-909
    • Aviram, A.1    Zimrah, Y.2    Shaklai, M.3    Nudelman, A.4    Rephaeli, A.5
  • 4
    • 33745039080 scopus 로고    scopus 로고
    • Uptake of acyloxyalkyl ester prodrugs of butyric acid into leukemic cells and their intracellular esterasecatalyzed hydrolysis
    • Zimra, Y.; Nudelman, A.; Zhuk, R.; Rabizadeh, E.; Shaklai, M.; Aviram, A.; Rephaeli, A. Uptake of acyloxyalkyl ester prodrugs of butyric acid into leukemic cells and their intracellular esterasecatalyzed hydrolysis. J. Cancer Res. Clin. Oncol. 2000, 123, 152-160.
    • (2000) J. Cancer Res. Clin. Oncol , vol.123 , pp. 152-160
    • Zimra, Y.1    Nudelman, A.2    Zhuk, R.3    Rabizadeh, E.4    Shaklai, M.5    Aviram, A.6    Rephaeli, A.7
  • 6
    • 0036839093 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor AN-9 has selective toxicity to acute leukemia and drug-resistant primary leukemia and cancer cell lines
    • Batova, A.; Shao, L. E.; Diccianni, M. B.; Yu, A. L.; Tanaka, T.; Rephaeli, A.; Nudelman, A.; Yu, J. The histone deacetylase inhibitor AN-9 has selective toxicity to acute leukemia and drug-resistant primary leukemia and cancer cell lines. Blood 2002, 100, 3319-3324.
    • (2002) Blood , vol.100 , pp. 3319-3324
    • Batova, A.1    Shao, L.E.2    Diccianni, M.B.3    Yu, A.L.4    Tanaka, T.5    Rephaeli, A.6    Nudelman, A.7    Yu, J.8
  • 7
    • 0031046409 scopus 로고    scopus 로고
    • An anti-cancer derivative of butyric acid (pivaloyloxymethyl-butyrate) and daunorubicin cooperatively prolong survival of mice inoculated with monocytic leukemia cells
    • Kasukabe, T.; Rephaeli, A.; Honma, Y. An anti-cancer derivative of butyric acid (pivaloyloxymethyl-butyrate) and daunorubicin cooperatively prolong survival of mice inoculated with monocytic leukemia cells. Br. J. Cancer 1997, 75, 850-854.
    • (1997) Br. J. Cancer , vol.75 , pp. 850-854
    • Kasukabe, T.1    Rephaeli, A.2    Honma, Y.3
  • 8
    • 0033819869 scopus 로고    scopus 로고
    • Prodrugs of butyric acid from bench to beside: Synthetic design, mechanism of action, and clinical applications
    • Rephaeli, A.; Zhuk, R.; Nudelman, A. Prodrugs of butyric acid from bench to beside: synthetic design, mechanism of action, and clinical applications. Drug Dev. Res. 2000, 50, 379-391.
    • (2000) Drug Dev. Res , vol.50 , pp. 379-391
    • Rephaeli, A.1    Zhuk, R.2    Nudelman, A.3
  • 9
    • 13944275513 scopus 로고    scopus 로고
    • The role of intracellularly released formaldehyde and butyric acid in the anticancer activity of acyloxyalkyl esters
    • Nudelman, A.; Levovich, I.; Cutts, S. M.; Phillips, D. R.; Rephaeli, A. The role of intracellularly released formaldehyde and butyric acid in the anticancer activity of acyloxyalkyl esters. J. Med. Chem. 2005, 48, 1042-1054.
    • (2005) J. Med. Chem , vol.48 , pp. 1042-1054
    • Nudelman, A.1    Levovich, I.2    Cutts, S.M.3    Phillips, D.R.4    Rephaeli, A.5
  • 10
    • 45849091516 scopus 로고    scopus 로고
    • Formaldehyde-releasing prodrugs specifically affect cancer cells by depletion of intracellular glutathione and augmentation of reactive oxygen species
    • Levovich, I.; Nudelman, A.; Berkovitch, G.; Swift, L.; Cutts, S.; Phillips, D. R.; Rephaeli, A. Formaldehyde-releasing prodrugs specifically affect cancer cells by depletion of intracellular glutathione and augmentation of reactive oxygen species. Cancer Chemother. Pharmacol. 2008, 62, 471-482.
    • (2008) Cancer Chemother. Pharmacol , vol.62 , pp. 471-482
    • Levovich, I.1    Nudelman, A.2    Berkovitch, G.3    Swift, L.4    Cutts, S.5    Phillips, D.R.6    Rephaeli, A.7
  • 11
    • 0000203929 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity
    • Stefan, W.; Rex, M. The heme synthesis and degradation pathways: role in oxidant sensitivity. Free Radical Biol. Med. 2000, 28, 289-309.
    • (2000) Free Radical Biol. Med , vol.28 , pp. 289-309
    • Stefan, W.1    Rex, M.2
  • 12
    • 0019841509 scopus 로고
    • Hemin inhibits ATP-dependent ubiquitin-dependent proteolysis: Role of hemin in regulating ubiquitin conjugate degradation
    • Haas, A. L.; Rose, I. A. Hemin inhibits ATP-dependent ubiquitin-dependent proteolysis: role of hemin in regulating ubiquitin conjugate degradation. Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 6845-6848.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 6845-6848
    • Haas, A.L.1    Rose, I.A.2
  • 13
    • 0019223260 scopus 로고
    • Control of protein degradation in reticulocytes and reticulocyte extracts by hemin
    • Etlinger, J. D.; Goldberg, A. L. Control of protein degradation in reticulocytes and reticulocyte extracts by hemin. J. Biol. Chem. 1980, 255, 4563-4568.
    • (1980) J. Biol. Chem , vol.255 , pp. 4563-4568
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 14
    • 33645689183 scopus 로고    scopus 로고
    • Proteasome inhibition: Novel therapy for multiple myeloma
    • Jonathan, L.; Kaufman, L. Proteasome inhibition: novel therapy for multiple myeloma. Onkologie 2006, 29, 162-168.
    • (2006) Onkologie , vol.29 , pp. 162-168
    • Jonathan, L.1    Kaufman, L.2
  • 15
    • 33747439440 scopus 로고    scopus 로고
    • Study of the mechanisms of uptake of 5-aminolevulinic acid derivatives by PEPT1 and PEPT2 transporters as a tool to improve photodynamic therapy of tumours
    • Rodriguez, L.; Batlle, A.; Di Venosa, G.; MacRobert, A.; Battah, S.; Daniel, H.; Casas, A. Study of the mechanisms of uptake of 5-aminolevulinic acid derivatives by PEPT1 and PEPT2 transporters as a tool to improve photodynamic therapy of tumours. Int. J. Biochem. Cell Biol. 2006, 38, 1530-1539.
    • (2006) Int. J. Biochem. Cell Biol , vol.38 , pp. 1530-1539
    • Rodriguez, L.1    Batlle, A.2    Di Venosa, G.3    MacRobert, A.4    Battah, S.5    Daniel, H.6    Casas, A.7
  • 16
    • 0347360162 scopus 로고    scopus 로고
    • Photodynamic therapy of skin cancer: Controlled drug delivery of 5-ALA and its esters
    • Fonseca, R.; Vianna, L.; Langeb, N.; Guyc, R.; Lopes, M.; Bentleya, B. Photodynamic therapy of skin cancer: controlled drug delivery of 5-ALA and its esters. Adv. Drug Delivery Rev. 2004, 56, 77-94.
    • (2004) Adv. Drug Delivery Rev , vol.56 , pp. 77-94
    • Fonseca, R.1    Vianna, L.2    Langeb, N.3    Guyc, R.4    Lopes, M.5    Bentleya, B.6
  • 17
    • 85022837582 scopus 로고
    • A mild and efficient sonochemical tert-butoxycarbonylation of amines from their salts
    • Einhorn, J.; Einhorn, C.; Luche, J. L. A mild and efficient sonochemical tert-butoxycarbonylation of amines from their salts. Synlett 1991, 37-38.
    • (1991) Synlett , pp. 37-38
    • Einhorn, J.1    Einhorn, C.2    Luche, J.L.3
  • 19
    • 0031906453 scopus 로고    scopus 로고
    • Acetyl chloride-methanol as a convenient reagent for: A) quantitative formation of amine hydrochlorides B), carboxylate ester formation, C) mild removal of N-t-Boc-protective group
    • Nudelman, A.; Bechor, Y.; Falb, E.; Fischer, B.; Wexler, B. A.; Nudelman, A. Acetyl chloride-methanol as a convenient reagent for: A) quantitative formation of amine hydrochlorides B), carboxylate ester formation, C) mild removal of N-t-Boc-protective group. Synth. Commun. 1998, 28, 471-474.
    • (1998) Synth. Commun , vol.28 , pp. 471-474
    • Nudelman, A.1    Bechor, Y.2    Falb, E.3    Fischer, B.4    Wexler, B.A.5    Nudelman, A.6
  • 20
    • 0001037074 scopus 로고    scopus 로고
    • Rasmussen, M.; Leonard, N. J. Synthesis of 3-(2′-deoxy-D- ribofurancsyl)adenine. Application of a new protecting group pivaloyloxymethyl (POM). J. Am. Chem. Soc. 1967, 89, 5439-5445.
    • Rasmussen, M.; Leonard, N. J. Synthesis of 3-(2′-deoxy-D- ribofurancsyl)adenine. Application of a new protecting group pivaloyloxymethyl (POM). J. Am. Chem. Soc. 1967, 89, 5439-5445.
  • 21
    • 0022534447 scopus 로고
    • Preparation of 1-acyloxyethyl esters of 7-[2-(2-aminothiazol-4-yl)acetamido]-3-[[[1-(2-dimethylaminoethyl)- 1H-tetrazol-5-yl]thio]-methyl]ceph-3-em-4-carboxylic acid (Cefotiam) and their oral absorption in mice
    • Yoshimura, Y.; Hamaguchi, N.; Yashiki, T. Preparation of 1-acyloxyethyl esters of 7-[2-(2-aminothiazol-4-yl)acetamido]-3-[[[1-(2-dimethylaminoethyl)- 1H-tetrazol-5-yl]thio]-methyl]ceph-3-em-4-carboxylic acid (Cefotiam) and their oral absorption in mice. J. Antibiot. 1986, 39, 1329-1342.
    • (1986) J. Antibiot , vol.39 , pp. 1329-1342
    • Yoshimura, Y.1    Hamaguchi, N.2    Yashiki, T.3
  • 23
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • Chou, T. C. Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol. Rev. 2006, 58, 621-681.
    • (2006) Pharmacol. Rev , vol.58 , pp. 621-681
    • Chou, T.C.1
  • 24
    • 33645721277 scopus 로고    scopus 로고
    • Modifications of intracellular levels of glutathione-dependent form-aldehyde dehydrogenase alters glutathione homeostasis and root development
    • Espunia, M. C.; Diaz, M.; Morenoa-romero, J.; Martinez, M. C. Modifications of intracellular levels of glutathione-dependent form-aldehyde dehydrogenase alters glutathione homeostasis and root development. Plant, Cell Environ. 2006, 29, 1002-1111.
    • (2006) Plant, Cell Environ , vol.29 , pp. 1002-1111
    • Espunia, M.C.1    Diaz, M.2    Morenoa-romero, J.3    Martinez, M.C.4
  • 25
    • 0024422072 scopus 로고
    • Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
    • Koivusalo, M.; Baumann, M.; Lasse, U. Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase. FEBS Lett. 1989, 257, 105-109.
    • (1989) FEBS Lett , vol.257 , pp. 105-109
    • Koivusalo, M.1    Baumann, M.2    Lasse, U.3
  • 26
    • 0025442850 scopus 로고
    • Photodynamic therapy with endogenous protoporphyrin IX: Basic principles and present clinical experience
    • Kennedy, J.; Pottier, R.; Pross, G. Photodynamic therapy with endogenous protoporphyrin IX: Basic principles and present clinical experience. J. Photochem. Photobiol. B 1990, 6, 143-148.
    • (1990) J. Photochem. Photobiol. B , vol.6 , pp. 143-148
    • Kennedy, J.1    Pottier, R.2    Pross, G.3
  • 27
    • 33947356281 scopus 로고    scopus 로고
    • Bortezomib-mediated 26S proteasome inhibition causes cell-cycle arrest and induces apoptosis in CD-30+ anaplastic large cell lymphoma
    • Bonvini, P.; Zorzi, E.; Basso, G.; Rosolen, A. Bortezomib-mediated 26S proteasome inhibition causes cell-cycle arrest and induces apoptosis in CD-30+ anaplastic large cell lymphoma. Leukemia 2007, 21, 838-842.
    • (2007) Leukemia , vol.21 , pp. 838-842
    • Bonvini, P.1    Zorzi, E.2    Basso, G.3    Rosolen, A.4
  • 28
    • 26844452967 scopus 로고    scopus 로고
    • Preclinical evaluation of the proteasome inhibitor bortezomib in cancer therapy
    • Boccadoro, M.; Morgan, G.; Cavenagh, J. Preclinical evaluation of the proteasome inhibitor bortezomib in cancer therapy. Cancer Cell 2005, 5, 1-9.
    • (2005) Cancer Cell , vol.5 , pp. 1-9
    • Boccadoro, M.1    Morgan, G.2    Cavenagh, J.3
  • 29
    • 0035006792 scopus 로고    scopus 로고
    • Proteasome inhibition in oxidative stress neurotoxicity: Implications for heat shock proteins
    • Ding, Q.; Keller, J. N. Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins. J. Neurochem. 2001, 77, 1010-1017.
    • (2001) J. Neurochem , vol.77 , pp. 1010-1017
    • Ding, Q.1    Keller, J.N.2
  • 30
    • 21344464730 scopus 로고    scopus 로고
    • HDAC inhibition prevents NF-kappa B activation by suppressing proteasome activity: Down-regulation of proteasome subunit expression stabilizes I kappa B alpha
    • Place, R. F.; Noonan, E. J.; Giardina, C. HDAC inhibition prevents NF-kappa B activation by suppressing proteasome activity: down-regulation of proteasome subunit expression stabilizes I kappa B alpha. Biochem. Pharmacol. 2005, 70, 394-406.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 394-406
    • Place, R.F.1    Noonan, E.J.2    Giardina, C.3
  • 31
    • 33846707942 scopus 로고    scopus 로고
    • Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B
    • Chen, J.; Ghazawi, F. M.; Bakkar, W.; Li, Q. Valproic acid and butyrate induce apoptosis in human cancer cells through inhibition of gene expression of Akt/protein kinase B. Mol. Cancer 2006, 5, 71-82.
    • (2006) Mol. Cancer , vol.5 , pp. 71-82
    • Chen, J.1    Ghazawi, F.M.2    Bakkar, W.3    Li, Q.4
  • 32
    • 0034844509 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex
    • Almond, J. B.; Snowden, R. T.; Hunter, A.; Dinsdale, D.; Cain, K.; Cohen, G. M. Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex. Leukemia 2001, 15, 1388-1397.
    • (2001) Leukemia , vol.15 , pp. 1388-1397
    • Almond, J.B.1    Snowden, R.T.2    Hunter, A.3    Dinsdale, D.4    Cain, K.5    Cohen, G.M.6
  • 33
    • 33749635130 scopus 로고    scopus 로고
    • A small-molecule c-Myc inhibitor, 10058-F4, induces cell-cycle arrest, apoptosis, and myeloid differentiation of human acute myeloid leukemia
    • Huang, M. J.; Cheng, Y. C.; Liu, C R.; Lin, S.; Liu, H. E. A small-molecule c-Myc inhibitor, 10058-F4, induces cell-cycle arrest, apoptosis, and myeloid differentiation of human acute myeloid leukemia. Exp. Hematol. 2006, 34, 1480-1489.
    • (2006) Exp. Hematol , vol.34 , pp. 1480-1489
    • Huang, M.J.1    Cheng, Y.C.2    Liu, C.R.3    Lin, S.4    Liu, H.E.5
  • 34
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou, E. P.; Pilch, D. R.; Orr, A. H.; Ivanova, V. S.; Bonner, W. M. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 1998, 273, 5858-5868.
    • (1998) J. Biol. Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 35
    • 33750909999 scopus 로고    scopus 로고
    • Reactive oxygen species-induced activation of the MAP kinase signaling pathways
    • McCubrey, J. A.; Lahair, M. M.; Franklin, R. A. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxid. Redox Signaling 2006, 8, 1775-1789.
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 1775-1789
    • McCubrey, J.A.1    Lahair, M.M.2    Franklin, R.A.3
  • 36
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian, E.; Karin, M. AP-1 in cell proliferation and survival. Oncogene 2001, 20, 2390-2400.
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 37
    • 36148944490 scopus 로고    scopus 로고
    • Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against pre-clinical models of multiple myeloma
    • Kuhn, D.; Chen, Q.; Voorhees, P.; Strader, J.; Shenk, K.; Sun, C.; Demo, S.; Bennett, M.; Leeuwen, F.; Chanan-Khan, A.; Orlowski, R. Z. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against pre-clinical models of multiple myeloma. Blood 2007, 100, 3281-3290.
    • (2007) Blood , vol.100 , pp. 3281-3290
    • Kuhn, D.1    Chen, Q.2    Voorhees, P.3    Strader, J.4    Shenk, K.5    Sun, C.6    Demo, S.7    Bennett, M.8    Leeuwen, F.9    Chanan-Khan, A.10    Orlowski, R.Z.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.