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Volumn 154, Issue 6, 2013, Pages 501-504

Synergy of ferrous ion on 5-aminolevulinic acid-mediated growth inhibition of Plasmodium falciparum

Author keywords

5 aminolevulinic acid (ALA); Haem synthesis; Malaria; Plasmodium falciparum

Indexed keywords

ACYL CARRIER PROTEIN; AMINOLEVULINIC ACID; COPROPORPHYRIN; COPROPORPHYRIN 3; FERROUS ION; HEME; UNCLASSIFIED DRUG;

EID: 84890491304     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvt096     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow, R.W., Guerra, C.A., Noor, A.M., Myint, H.Y., and Hay, S.I. (2005) The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 434, 214-217
    • (2005) Nature , vol.434 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 2
    • 32944458099 scopus 로고    scopus 로고
    • Invasion of red blood cells by malaria parasites
    • Cowman, A.F. and Crabb, B.S. (2006) Invasion of red blood cells by malaria parasites. Cell 124, 755-766
    • (2006) Cell , vol.124 , pp. 755-766
    • Cowman, A.F.1    Crabb, B.S.2
  • 4
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia, N. and Padmanaban, G. (1992) de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem. Biophys. Res. Commun. 187, 744-750
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 5
    • 84868310578 scopus 로고    scopus 로고
    • Direct tests of enzymatic heme degradation by the malaria parasite Plasmodium falciparum
    • Sigala, P.A., Crowley, J.R., Hsieh, S., Henderson, J.P., and Goldberg, D.E. (2012) Direct tests of enzymatic heme degradation by the malaria parasite Plasmodium falciparum. J. Biol. Chem. 287, 37793-37807
    • (2012) J. Biol. Chem. , vol.287 , pp. 37793-37807
    • Sigala, P.A.1    Crowley, J.R.2    Hsieh, S.3    Henderson, J.P.4    Goldberg, D.E.5
  • 7
    • 84883378968 scopus 로고    scopus 로고
    • Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection
    • Nagaraj, V.A., Sundaram, B., Varadarajan, N.M., Subramani, P.A., Kalappa, D.M., Ghosh, S.K., and Padmanaban, G. (2013) Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection. PLoS Pathog. 9, e1003522
    • (2013) PLoS Pathog , vol.9
    • Nagaraj, V.A.1    Sundaram, B.2    Varadarajan, N.M.3    Subramani, P.A.4    Kalappa, D.M.5    Ghosh, S.K.6    Padmanaban, G.7
  • 8
    • 84875057433 scopus 로고    scopus 로고
    • Make it, take it, or leave it: Heme metabolism of parasites
    • Korený, L., Oborńk, M., and Lukes, J. (2013) Make it, take it, or leave it: Heme metabolism of parasites. PLoS Pathog. 9, e1003088
    • (2013) PLoS Pathog. , vol.9
    • Korený, L.1    Oborńk, M.2    Lukes, J.3
  • 9
    • 84890475029 scopus 로고    scopus 로고
    • The metabolic roles of the endosymbiotic organelles of Toxoplasma and Plasmodium spp
    • Sheiner, L., Vaidya, A.B., and McFadden, G.I. (2013) The metabolic roles of the endosymbiotic organelles of Toxoplasma and Plasmodium spp. Curr. Opin. Microbiol. 16, 452-458
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 452-458
    • Sheiner, L.1    Vaidya, A.B.2    McFadden, G.I.3
  • 15
    • 0008414465 scopus 로고
    • The succinate glycine cycle. I. The mechanism of pyrrole synthesis
    • Shemin, D., Russell, C.S., and Abramsky, T. (1955) The succinate-glycine cycle. I. The mechanism of pyrrole synthesis. J. Biol. Chem. 215, 613-626
    • (1955) J. Biol. Chem. , vol.215 , pp. 613-626
    • Shemin, D.1    Russell, C.S.2    Abramsky, T.3
  • 16
    • 80052399645 scopus 로고    scopus 로고
    • Roles of porphyrin and iron metabolisms in the d-aminolevulinic acid (ALA)-induced accumulation of protoporphyrin and photodamage of tumor cells
    • Ohgari, Y., Miyata, Y., Miyagi, T., Gotoh, S., Ohta, T., Kataoka, T., Furuyama, K., and Taketani, S. (2011) Roles of porphyrin and iron metabolisms in the d-aminolevulinic acid (ALA)-induced accumulation of protoporphyrin and photodamage of tumor cells. Photochem. Photobiol. 87, 1138-1145
    • (2011) Photochem. Photobiol. , vol.87 , pp. 1138-1145
    • Ohgari, Y.1    Miyata, Y.2    Miyagi, T.3    Gotoh, S.4    Ohta, T.5    Kataoka, T.6    Furuyama, K.7    Taketani, S.8
  • 17
    • 3042803773 scopus 로고    scopus 로고
    • Inactivation of Plasmodium falciparum by photodynamic excitation of heme-cycle intermediates derived from delta-aminolevulinic acid
    • Smith, T.G. and Kain, K.C. (2004) Inactivation of Plasmodium falciparum by photodynamic excitation of heme-cycle intermediates derived from delta-aminolevulinic acid. J. Infect. Dis. 190, 184-191
    • (2004) J. Infect. Dis. , vol.190 , pp. 184-191
    • Smith, T.G.1    Kain, K.C.2
  • 18
    • 71949108405 scopus 로고    scopus 로고
    • Mechanism of cell death by 5-aminolevulinic acidbased photodynamic action and its enhancement by ferrochelatase inhibitors in human histiocytic lymphoma cell line U937
    • Amo, T., Kawanishi, N., Uchida, M., Fujita, H., Oyanagi, E., Utsumi, T., Ogino, T., Inoue, K., Shuin, T., Utsumi, K., and Sasaki, J. (2009) Mechanism of cell death by 5-aminolevulinic acidbased photodynamic action and its enhancement by ferrochelatase inhibitors in human histiocytic lymphoma cell line U937. Cell. Biochem. Funct. 27, 503-515
    • (2009) Cell. Biochem. Funct. , vol.27 , pp. 503-515
    • Amo, T.1    Kawanishi, N.2    Uchida, M.3    Fujita, H.4    Oyanagi, E.5    Utsumi, T.6    Ogino, T.7    Inoue, K.8    Shuin, T.9    Utsumi, K.10    Sasaki, J.11
  • 19
    • 28244496572 scopus 로고    scopus 로고
    • Mechanisms involved in delta-aminolevulinic acid (ALA)-induced photosensitivity of tumor cells: Relation of ferrochelatase and uptake of ALA to the accumulation of protoporphyrin
    • Ohgari, Y., Nakayasu, Y., Kitajima, S., Sawamoto, M., Mori, H., Shimokawa, O., Matsui, H., and Taketani, S. (2005) Mechanisms involved in delta-aminolevulinic acid (ALA)-induced photosensitivity of tumor cells: Relation of ferrochelatase and uptake of ALA to the accumulation of protoporphyrin. Biochem. Pharmacol. 71, 42-49
    • (2005) Biochem. Pharmacol. , vol.71 , pp. 42-49
    • Ohgari, Y.1    Nakayasu, Y.2    Kitajima, S.3    Sawamoto, M.4    Mori, H.5    Shimokawa, O.6    Matsui, H.7    Taketani, S.8
  • 21
    • 12444318635 scopus 로고    scopus 로고
    • Delta-aminolevulinic acid-based photodynamic therapy for acne on the body
    • Kimura, M., Itoh, Y., Tokuoka, Y., and Kawashima, N. (2004) Delta-aminolevulinic acid-based photodynamic therapy for acne on the body. J. Dermatol. 31, 956-960
    • (2004) J. Dermatol. , vol.31 , pp. 956-960
    • Kimura, M.1    Itoh, Y.2    Tokuoka, Y.3    Kawashima, N.4
  • 22
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W. and Jensen, J.B. (1976) Human malaria parasites in continuous culture. Science 193, 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 23
    • 49549107080 scopus 로고    scopus 로고
    • Nrf2-dependent induction of human ABC transporter ABCG2 and heme oxygenase-1 in HepG2 cells by photoactivation of porphyrins: Biochemical implications for cancer cell response to photodynamic therapy
    • Hagiya, Y., Adachi, T., Ogura, S., An, R., Tamura, A., Nakagawa, H., Okura, I., Mochizuki, T., and Ishikawa, T. (2008) Nrf2-dependent induction of human ABC transporter ABCG2 and heme oxygenase-1 in HepG2 cells by photoactivation of porphyrins: Biochemical implications for cancer cell response to photodynamic therapy. J. Exp. Ther. Oncol. 7, 153-167
    • (2008) J. Exp. Ther. Oncol. , vol.7 , pp. 153-167
    • Hagiya, Y.1    Adachi, T.2    Ogura, S.3    An, R.4    Tamura, A.5    Nakagawa, H.6    Okura, I.7    Mochizuki, T.8    Ishikawa, T.9
  • 24
    • 1642431647 scopus 로고    scopus 로고
    • The use of DsRED in single- and dual-color fluorescence labeling of mitochondrial and plastid organelles in Plasmodium falciparum
    • Sato, S. and Wilson, R.J. (2004) The use of DsRED in single- and dual-color fluorescence labeling of mitochondrial and plastid organelles in Plasmodium falciparum. Mol. Biochem. Parasitol. 134, 175-179
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 175-179
    • Sato, S.1    Wilson, R.J.2
  • 27
    • 0142240277 scopus 로고    scopus 로고
    • Zinc protoporphyrin IX binds heme crystals to inhibit the process of crystallization in Plasmodium falciparum
    • Iyer, J.K., Shi, L., Shankar, A.H., and Sullivan, D.J. (2003) Zinc protoporphyrin IX binds heme crystals to inhibit the process of crystallization in Plasmodium falciparum. Mol. Med. 9, 175-182
    • (2003) Mol. Med. , vol.9 , pp. 175-182
    • Iyer, J.K.1    Shi, L.2    Shankar, A.H.3    Sullivan, D.J.4
  • 29
    • 0021045327 scopus 로고
    • On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism
    • Samuni, A., Aronovitch, J., Godinger, D., Chevion, M., and Czapski, G. (1983) On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism. Eur. J. Biochem. 137, 119-124
    • (1983) Eur. J. Biochem. , vol.137 , pp. 119-124
    • Samuni, A.1    Aronovitch, J.2    Godinger, D.3    Chevion, M.4    Czapski, G.5
  • 31
    • 43049104537 scopus 로고    scopus 로고
    • Interaction between artemisinin and heme. A Density Functional Theory study of structures and interaction energies
    • Araú jo, J.Q., Carneiro, J.W., de Araujo, M.T., Leite, F.H., and Taranto, A.G. (2008) Interaction between artemisinin and heme. A Density Functional Theory study of structures and interaction energies. Bioorg. Med. Chem. 16, 5021-5029
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 5021-5029
    • Araú Jo, J.Q.1    Carneiro, J.W.2    De Araujo, M.T.3    Leite, F.H.4    Taranto, A.G.5
  • 32
    • 77955907263 scopus 로고    scopus 로고
    • Metabolic pathways in the apicoplast of apicomplexa
    • Seeber, F. and Soldati-Favre, D. (2010) Metabolic pathways in the apicoplast of apicomplexa. Int. Rev. Cell. Mol. Biol. 281, 161-228
    • (2010) Int. Rev. Cell. Mol. Biol. , vol.281 , pp. 161-228
    • Seeber, F.1    Soldati-Favre, D.2


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