메뉴 건너뛰기




Volumn 50, Issue 11, 2011, Pages 1659-1668

Cysteine-3 and cysteine-4 are essential for the thioredoxin-like oxidoreductase and antioxidant activities of Plasmodium falciparum macrophage migration inhibitory factor

Author keywords

Cysteine modification; Free radicals; Hydroxyl radical; Malaria; Oxidative stress; Oxidoreductase; Vicinal thiol

Indexed keywords

ARSENOSOBENZENE; CYANOGEN BROMIDE; CYSTEINE; INSULIN; MACROPHAGE MIGRATION INHIBITION FACTOR; PLASMID DNA; PROTOZOAL DNA; PROTOZOAL PROTEIN; PROTOZOAL RNA; REACTIVE OXYGEN METABOLITE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; THIOREDOXIN REDUCTASE;

EID: 79955608902     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.03.012     Document Type: Article
Times cited : (22)

References (46)
  • 1
    • 0013933261 scopus 로고
    • Mechanism of a reaction in vitro associated with delayed-type hypersensitivity
    • B.R. Bloom, and B. Bennett Mechanism of a reaction in vitro associated with delayed-type hypersensitivity Science 153 1966 80 82
    • (1966) Science , vol.153 , pp. 80-82
    • Bloom, B.R.1    Bennett, B.2
  • 2
    • 0036212743 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (MIF): Mechanisms of action and role in disease
    • DOI 10.1016/S1286-4579(02)01560-5, PII S1286457902015605
    • H. Lue, R. Kleemann, T. Calandra, T. Roger, and J. Bernhagen Macrophage migration inhibitory factor (MIF): mechanisms of action and role in disease Microbes Infect. 4 2002 449 460 (Pubitemid 34270682)
    • (2002) Microbes and Infection , vol.4 , Issue.4 , pp. 449-460
    • Lue, H.1    Kleemann, R.2    Calandra, T.3    Roger, T.4    Bernhagen, J.5
  • 3
    • 24144433455 scopus 로고    scopus 로고
    • Link between macrophage migration inhibitory factor and cellular redox regulation
    • DOI 10.1089/ars.2005.7.1234
    • M. Thiele, and J. Bernhagen Link between macrophage migration inhibitory factor and cellular redox regulation Antioxid. Redox Signal. 7 2005 1234 1248 (Pubitemid 41232520)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.9-10 , pp. 1234-1248
    • Thiele, M.1    Bernhagen, J.2
  • 8
    • 33750904465 scopus 로고    scopus 로고
    • Role of thioredoxin in cell growth through interactions with signaling molecules
    • J. Yoshioka, E.R. Schreiter, and R.T. Lee Role of thioredoxin in cell growth through interactions with signaling molecules Antioxid. Redox Signal. 8 2006 2143 2151 (Pubitemid 46489637)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.11-12 , pp. 2143-2151
    • Yoshioka, J.1    Schreiter, E.R.2    Lee, R.T.3
  • 9
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • W. Trager, and J.B. Jensen Human malaria parasites in continuous culture Science 193 1976 673 675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 10
    • 24644438428 scopus 로고    scopus 로고
    • Clotrimazole inhibits hemoperoxidase of Plasmodium falciparum and induces oxidative stress: Proposed antimalarial mechanism of clotrimazole
    • DOI 10.1074/jbc.M501563200
    • V. Trivedi, P. Chand, K. Srivastava, S.K. Puri, P.R. Maulik, and U. Bandyopadhyay Clotrimazole inhibits hemoperoxidase of Plasmodium falciparum and induces oxidative stress: proposed antimalarial mechanism of clotrimazole J. Biol. Chem. 280 2005 41129 41136 (Pubitemid 41832165)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41129-41136
    • Trivedi, V.1    Chand, P.2    Srivastava, K.3    Puri, S.K.4    Maulik, P.R.5    Bandyopadhyay, U.6
  • 12
    • 0020440925 scopus 로고
    • Efficient extraction and translation of Plasmodium falciparum messenger RNA
    • DOI 10.1016/0166-6851(82)90023-8
    • M. Wallach Efficient extraction and translation of Plasmodium falciparum messenger RNA Mol. Biochem. Parasitol. 6 1982 335 342 (Pubitemid 13210187)
    • (1982) Molecular and Biochemical Parasitology , vol.6 , Issue.6 , pp. 335-342
    • Wallach, M.1
  • 14
    • 33846629425 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum choline kinase by hexadecyltrimethylammonium bromide: A possible antimalarial mechanism
    • DOI 10.1128/AAC.00919-06
    • V. Choubey, P. Maity, M. Guha, S. Kumar, K. Srivastava, S.K. Puri, and U. Bandyopadhyay Inhibition of Plasmodium falciparum choline kinase by hexadecyltrimethylammonium bromide: a possible antimalarial mechanism Antimicrob. Agents Chemother. 51 2007 696 706 (Pubitemid 46185292)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.2 , pp. 696-706
    • Choubey, V.1    Maity, P.2    Guha, M.3    Kumar, S.4    Srivastava, K.5    Puri, S.K.6    Bandyopadhyay, U.7
  • 17
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • A. Holmgren Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide J. Biol. Chem. 254 1979 9627 9632 (Pubitemid 10248727)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.19 , pp. 9627-9632
    • Holmgren, A.1
  • 18
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, and B.A. Wallace Dichroweb: an interactive website for the analysis of protein secondary structure from circular dichroism spectra Bioinformatics 18 2002 211 212 (Pubitemid 34145057)
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 19
    • 0038175547 scopus 로고    scopus 로고
    • A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical
    • DOI 10.1074/jbc.M210328200
    • K. Biswas, U. Bandyopadhyay, I. Chattopadhyay, A. Varadaraj, E. Ali, and R.K. Banerjee A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical J. Biol. Chem. 278 2003 10993 11001 (Pubitemid 36792647)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 10993-11001
    • Biswas, K.1    Bandyopadhyay, U.2    Chattopadhyay, I.3    Varadaraj, A.4    Ali, E.5    Banerjee, R.K.6
  • 20
    • 0032787451 scopus 로고    scopus 로고
    • Heterogeneity of human red blood cell membrane: Co-existence of heavy and light membranes
    • DOI 10.1023/A:1006932010565
    • S.K. Das, and S. Mukherjee Heterogeneity of human red blood cell membrane: co-existence of heavy and light membranes Mol. Cell. Biochem. 196 1999 141 149 (Pubitemid 29338789)
    • (1999) Molecular and Cellular Biochemistry , vol.196 , Issue.1-2 , pp. 141-149
    • Das, S.K.1    Mukherjee, S.2
  • 21
    • 59149086582 scopus 로고    scopus 로고
    • Indomethacin, a non-steroidal anti-inflammatory drug, develops gastropathy by inducing reactive oxygen species-mediated mitochondrial pathology and associated apoptosis in gastric mucosa: A novel role of mitochondrial aconitase oxidation
    • P. Maity, S. Bindu, S. Dey, M. Goyal, A. Alam, C. Pal, K. Mitra, and U. Bandyopadhyay Indomethacin, a non-steroidal anti-inflammatory drug, develops gastropathy by inducing reactive oxygen species-mediated mitochondrial pathology and associated apoptosis in gastric mucosa: a novel role of mitochondrial aconitase oxidation J. Biol. Chem. 284 2009 3058 3068
    • (2009) J. Biol. Chem. , vol.284 , pp. 3058-3068
    • Maity, P.1    Bindu, S.2    Dey, S.3    Goyal, M.4    Alam, A.5    Pal, C.6    Mitra, K.7    Bandyopadhyay, U.8
  • 22
    • 62449189195 scopus 로고    scopus 로고
    • Melatonin reduces indomethacin-induced gastric mucosal cell apoptosis by preventing mitochondrial oxidative stress and the activation of mitochondrial pathway of apoptosis
    • P. Maity, S. Bindu, S. Dey, M. Goyal, A. Alam, C. Pal, R. Reiter, and U. Bandyopadhyay Melatonin reduces indomethacin-induced gastric mucosal cell apoptosis by preventing mitochondrial oxidative stress and the activation of mitochondrial pathway of apoptosis J. Pineal Res. 46 2009 314 323
    • (2009) J. Pineal Res. , vol.46 , pp. 314-323
    • Maity, P.1    Bindu, S.2    Dey, S.3    Goyal, M.4    Alam, A.5    Pal, C.6    Reiter, R.7    Bandyopadhyay, U.8
  • 24
    • 0141697278 scopus 로고    scopus 로고
    • Development and Applications of In-Gel CNBr/Tryptic Digestion Combined with Mass Spectrometry for the Analysis of Membrane Proteins
    • DOI 10.1021/pr0340126
    • T.T. Quach, N. Li, D.P. Richards, J. Zheng, B.O. Keller, and L. Li Development and applications of in-gel CNBr/tryptic digestion combined with mass spectrometry for the analysis of membrane proteins J. Proteome Res. 2 2003 543 552 (Pubitemid 37376849)
    • (2003) Journal of Proteome Research , vol.2 , Issue.5 , pp. 543-552
    • Quach, T.T.T.1    Li, N.2    Richards, D.P.3    Zheng, J.4    Keller, B.O.5    Li, L.6
  • 25
    • 33646467190 scopus 로고    scopus 로고
    • New insights on macrophage migration inhibitory factor: Based on molecular and functional analysis of its homologue of Chinese amphioxus
    • J. Du, Y. Yu, H. Tu, H. Chen, X. Xie, C. Mou, K. Feng, S. Zhang, and A. Xu New insights on macrophage migration inhibitory factor: based on molecular and functional analysis of its homologue of Chinese amphioxus Mol. Immunol. 43 2006 2083 2088
    • (2006) Mol. Immunol. , vol.43 , pp. 2083-2088
    • Du, J.1    Yu, Y.2    Tu, H.3    Chen, H.4    Xie, X.5    Mou, C.6    Feng, K.7    Zhang, S.8    Xu, A.9
  • 26
    • 33846006235 scopus 로고    scopus 로고
    • Characterisation of macrophage migration inhibitory factor from Eimeria species infectious to chickens
    • DOI 10.1016/j.molbiopara.2006.10.020, PII S0166685106003215
    • K.B. Miska, R.H. Fetterer, H.S. Lillehoj, M.C. Jenkins, P.C. Allen, and S.B. Harper Characterisation of macrophage migration inhibitory factor from Eimeria species infectious to chickens Mol. Biochem. Parasitol. 151 2007 173 183 (Pubitemid 46054211)
    • (2007) Molecular and Biochemical Parasitology , vol.151 , Issue.2 , pp. 173-183
    • Miska, K.B.1    Fetterer, R.H.2    Lillehoj, H.S.3    Jenkins, M.C.4    Allen, P.C.5    Harper, S.B.6
  • 27
    • 33751428611 scopus 로고    scopus 로고
    • Haemaphysalis longicornis: Molecular characterization of a homologue of the macrophage migration inhibitory factor from the partially fed ticks
    • DOI 10.1016/j.exppara.2006.07.006, PII S0014489406001664
    • R. Umemiya, T. Hatta, M. Liao, M. Tanaka, J. Zhou, N. Inoue, and K. Fujisaki Haemaphysalis longicornis: molecular characterization of a homologue of the macrophage migration inhibitory factor from the partially fed ticks Exp. Parasitol. 115 2007 135 142 (Pubitemid 44820049)
    • (2007) Experimental Parasitology , vol.115 , Issue.2 , pp. 135-142
    • Umemiya, R.1    Hatta, T.2    Liao, M.3    Tanaka, M.4    Zhou, J.5    Inoue, N.6    Fujisaki, K.7
  • 28
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • G. Bohm, R. Muhr, and R. Jaenicke Quantitative analysis of protein far UV circular dichroism spectra by neural networks Protein Eng. 5 1992 191 195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Bohm, G.1    Muhr, R.2    Jaenicke, R.3
  • 29
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • J.P. Hennessey Jr., and W.C. Johnson Jr. Information content in the circular dichroism of proteins Biochemistry 20 1981 1085 1094
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 30
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • A. Perczel, K. Park, and G.D. Fasman Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide Anal. Biochem. 203 1992 83 93
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 31
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • A. Holmgren Antioxidant function of thioredoxin and glutaredoxin systems Antioxid. Redox Signal. 2 2000 811 820 (Pubitemid 32062330)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.4 , pp. 811-820
    • Holmgren, A.1
  • 32
    • 33845651700 scopus 로고    scopus 로고
    • Apoptosis in liver during malaria: Role of oxidative stress and implication of mitochondrial pathway
    • M. Guha, S. Kumar, V. Choubey, P. Maity, and U. Bandyopadhyay Apoptosis in liver during malaria: role of oxidative stress and implication of mitochondrial pathway FASEB J. 20 2006 1224 1226
    • (2006) FASEB J. , vol.20 , pp. 1224-1226
    • Guha, M.1    Kumar, S.2    Choubey, V.3    Maity, P.4    Bandyopadhyay, U.5
  • 34
    • 0038779198 scopus 로고    scopus 로고
    • Thiol-modifying phenylarsine oxide inhibits guanine nucleotide binding of Rho but not of Rac GTPases
    • DOI 10.1124/mol.63.6.1349
    • R. Gerhard, H. John, K. Aktories, and I. Just Thiol-modifying phenylarsine oxide inhibits guanine nucleotide binding of Rho but not of Rac GTPases Mol. Pharmacol. 63 2003 1349 1355 (Pubitemid 36627230)
    • (2003) Molecular Pharmacology , vol.63 , Issue.6 , pp. 1349-1355
    • Gerhard, R.1    John, H.2    Aktories, K.3    Just, I.4
  • 35
    • 71549161769 scopus 로고    scopus 로고
    • Glutathione reductase and thioredoxin reductase: Novel antioxidant enzymes from Plasmodium berghei
    • G. Kapoor, and H.S. Banyal Glutathione reductase and thioredoxin reductase: novel antioxidant enzymes from Plasmodium berghei Korean J. Parasitol. 47 2009 421 424
    • (2009) Korean J. Parasitol. , vol.47 , pp. 421-424
    • Kapoor, G.1    Banyal, H.S.2
  • 37
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • DOI 10.1016/j.toxlet.2005.03.004, PII S0378427405000883
    • S. Kumar, and U. Bandyopadhyay Free heme toxicity and its detoxification systems in human Toxicol. Lett. 157 2005 175 188 (Pubitemid 40726102)
    • (2005) Toxicology Letters , vol.157 , Issue.3 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 40
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • DOI 10.1074/jbc.272.47.29399
    • H.F. Gilbert Protein disulfide isomerase and assisted protein folding J. Biol. Chem. 272 1997 29399 29402 (Pubitemid 27508016)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29399-29402
    • Gilbert, H.F.1
  • 41
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966 (Pubitemid 19214215)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.24 , pp. 13963-13966
    • Holmgren, A.1
  • 42
    • 0023891822 scopus 로고
    • Human plasma lecithin-cholesterol acyltransferase: The vicinal nature of cysteine 31 and cysteine 184 in the catalytic site
    • M. Jauhiainen, K.J. Stevenson, and P.J. Dolphin Human plasma lecithin-cholesterol acyltransferase: the vicinal nature of cysteine 31 and cysteine 184 in the catalytic site J. Biol. Chem. 263 1988 6525 6533
    • (1988) J. Biol. Chem. , vol.263 , pp. 6525-6533
    • Jauhiainen, M.1    Stevenson, K.J.2    Dolphin, P.J.3
  • 43
    • 0028298024 scopus 로고
    • Protein tyrosine phosphatase substrate specificity: Size and phosphotyrosine positioning requirements in peptide substrates
    • Z.Y. Zhang, D. Maclean, D.J. McNamara, T.K. Sawyer, and J.E. Dixon Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates Biochemistry 33 1994 2285 2290 (Pubitemid 24099629)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2285-2290
    • Zhang, Z.-Y.1    Maclean, D.2    McNamara, D.J.3    Sawyer, T.K.4    Dixon, J.E.5
  • 44
    • 0017847141 scopus 로고
    • Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with mono- and bifunctional arsenoxides
    • DOI 10.1021/bi00604a026
    • K.J. Stevenson, G. Hale, and R.N. Perham Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with mono- and bifunctional arsenoxides Biochemistry 17 1978 2189 2192 (Pubitemid 8341145)
    • (1978) Biochemistry , vol.17 , Issue.11 , pp. 2189-2192
    • Stevenson, K.J.1    Hale, G.2    Perham, R.N.3
  • 46
    • 0034643810 scopus 로고    scopus 로고
    • Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA
    • DOI 10.1021/bi992690t
    • M.R. Redinbo, J.J. Champoux, and W.G. Hol Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA Biochemistry 39 2000 6832 6840 (Pubitemid 30390375)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 6832-6840
    • Redinbo, M.R.1    Champoux, J.J.2    Hol, W.G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.