메뉴 건너뛰기




Volumn 185, Issue 11, 2015, Pages 3039-3052

Serum Pantetheinase/Vanin Levels regulate erythrocyte homeostasis and severity of malaria

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE AMINOTRANSFERASE; ALKALINE PHOSPHATASE; ASPARTATE AMINOTRANSFERASE; CATALASE; CRYOPYRIN; ENZYME; GAMMA INTERFERON; GAMMA INTERFERON INDUCIBLE PROTEIN 10; GLUTATHIONE TRANSFERASE; LACTATE DEHYDROGENASE; PANTETHEINASE; PANTOTHENIC ACID; PEROXIREDOXIN 2; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; AMIDASE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN;

EID: 84945269807     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2015.07.011     Document Type: Article
Times cited : (16)

References (53)
  • 1
    • 0018337347 scopus 로고
    • Purification and properties of pantetheinase from horse kidney
    • S. Dupre, and D. Cavallini Purification and properties of pantetheinase from horse kidney Methods Enzymol 62 1979 262 267
    • (1979) Methods Enzymol , vol.62 , pp. 262-267
    • Dupre, S.1    Cavallini, D.2
  • 4
    • 84905860807 scopus 로고    scopus 로고
    • Role of the Vnn1 pantetheinase in tissue tolerance to stress
    • P. Naquet, G. Pitari, S. Dupre, and F. Galland Role of the Vnn1 pantetheinase in tissue tolerance to stress Biochem Soc Trans 42 2014 1094 1100
    • (2014) Biochem Soc Trans , vol.42 , pp. 1094-1100
    • Naquet, P.1    Pitari, G.2    Dupre, S.3    Galland, F.4
  • 5
    • 0033752791 scopus 로고    scopus 로고
    • Cysteamine, the most potent ulcerogenic drug known so far, powerfully activates carbonic anhydrase I, II and IV: In vitro and in vivo studies
    • I. Puscas, M. Coltau, A. Maghiar, and G. Domuta Cysteamine, the most potent ulcerogenic drug known so far, powerfully activates carbonic anhydrase I, II and IV: in vitro and in vivo studies Exp Toxicol Pathol 52 2000 431 435
    • (2000) Exp Toxicol Pathol , vol.52 , pp. 431-435
    • Puscas, I.1    Coltau, M.2    Maghiar, A.3    Domuta, G.4
  • 6
    • 0023226012 scopus 로고
    • Development of cysteamine-induced ultrastructural surface changes on duodenal mucosa
    • D.C. Pfeiffer, C.J. Pfeiffer, and S. Szabo Development of cysteamine-induced ultrastructural surface changes on duodenal mucosa Lab Invest 56 1987 444 450
    • (1987) Lab Invest , vol.56 , pp. 444-450
    • Pfeiffer, D.C.1    Pfeiffer, C.J.2    Szabo, S.3
  • 7
    • 34447558473 scopus 로고    scopus 로고
    • Cellular thiol pools are responsible for sequestration of cytotoxic reactive aldehydes: Central role of free cysteine and cysteamine
    • P.L. Wood, M.A. Khan, and J.R. Moskal Cellular thiol pools are responsible for sequestration of cytotoxic reactive aldehydes: central role of free cysteine and cysteamine Brain Res 1158 2007 158 163
    • (2007) Brain Res , vol.1158 , pp. 158-163
    • Wood, P.L.1    Khan, M.A.2    Moskal, J.R.3
  • 8
    • 0023222921 scopus 로고
    • Gastric mucosal protection by agents altering gastric mucosal sulfhydryls: Role of endogenous prostaglandins
    • S.J. Konturek, T. Brzozowski, I. Piastucki, T. Radecki, D. Dupuy, and S. Szabo Gastric mucosal protection by agents altering gastric mucosal sulfhydryls: role of endogenous prostaglandins Digestion 37 1987 67 71
    • (1987) Digestion , vol.37 , pp. 67-71
    • Konturek, S.J.1    Brzozowski, T.2    Piastucki, I.3    Radecki, T.4    Dupuy, D.5    Szabo, S.6
  • 9
    • 33845888547 scopus 로고    scopus 로고
    • Vanin-1 licenses inflammatory mediator production by gut epithelial cells and controls colitis by antagonizing peroxisome proliferator-activated receptor gamma activity
    • C. Berruyer, L. Pouyet, V. Millet, F.M. Martin, A. LeGoffic, A. Canonici, S. Garcia, C. Bagnis, P. Naquet, and F. Galland Vanin-1 licenses inflammatory mediator production by gut epithelial cells and controls colitis by antagonizing peroxisome proliferator-activated receptor gamma activity J Exp Med 203 2006 2817 2827
    • (2006) J Exp Med , vol.203 , pp. 2817-2827
    • Berruyer, C.1    Pouyet, L.2    Millet, V.3    Martin, F.M.4    LeGoffic, A.5    Canonici, A.6    Garcia, S.7    Bagnis, C.8    Naquet, P.9    Galland, F.10
  • 10
    • 1642275597 scopus 로고    scopus 로고
    • Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher glutathione stores
    • F. Martin, M.F. Penet, F. Malergue, H. Lepidi, A. Dessein, F. Galland, M. de Reggi, P. Naquet, and B. Gharib Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher glutathione stores J Clin Invest 113 2004 591 597
    • (2004) J Clin Invest , vol.113 , pp. 591-597
    • Martin, F.1    Penet, M.F.2    Malergue, F.3    Lepidi, H.4    Dessein, A.5    Galland, F.6    De Reggi, M.7    Naquet, P.8    Gharib, B.9
  • 11
    • 0017652199 scopus 로고
    • Inhibition of gamma-glutamylcysteine synthetase by cystamine: An approach to a therapy of 5-oxoprolinuria (pyroglutamic aciduria)
    • O.W. Griffith, A. Larsson, and A. Meister Inhibition of gamma-glutamylcysteine synthetase by cystamine: an approach to a therapy of 5-oxoprolinuria (pyroglutamic aciduria) Biochem Biophys Res Commun 79 1977 919 925
    • (1977) Biochem Biophys Res Commun , vol.79 , pp. 919-925
    • Griffith, O.W.1    Larsson, A.2    Meister, A.3
  • 12
    • 44749094011 scopus 로고    scopus 로고
    • Mouse vanin-1 is cytoprotective for islet beta cells and regulates the development of type 1 diabetes
    • C. Roisin-Bouffay, R. Castellano, R. Valero, L. Chasson, F. Galland, and P. Naquet Mouse vanin-1 is cytoprotective for islet beta cells and regulates the development of type 1 diabetes Diabetologia 51 2008 1192 1201
    • (2008) Diabetologia , vol.51 , pp. 1192-1201
    • Roisin-Bouffay, C.1    Castellano, R.2    Valero, R.3    Chasson, L.4    Galland, F.5    Naquet, P.6
  • 13
    • 40349098207 scopus 로고    scopus 로고
    • Persistent Coxiella burnetii infection in mice overexpressing IL-10: An efficient model for chronic Q fever pathogenesis
    • S. Meghari, Y. Bechah, C. Capo, H. Lepidi, D. Raoult, P.J. Murray, and J.L. Mege Persistent Coxiella burnetii infection in mice overexpressing IL-10: an efficient model for chronic Q fever pathogenesis PLoS Pathogens 4 2008 e23
    • (2008) PLoS Pathogens , vol.4 , pp. e23
    • Meghari, S.1    Bechah, Y.2    Capo, C.3    Lepidi, H.4    Raoult, D.5    Murray, P.J.6    Mege, J.L.7
  • 14
    • 33947388797 scopus 로고    scopus 로고
    • Complex genetic control of susceptibility to malaria: Positional cloning of the Char9 locus
    • G. Min-Oo, A. Fortin, G. Pitari, M. Tam, M.M. Stevenson, and P. Gros Complex genetic control of susceptibility to malaria: positional cloning of the Char9 locus J Exp Med 204 2007 511 524
    • (2007) J Exp Med , vol.204 , pp. 511-524
    • Min-Oo, G.1    Fortin, A.2    Pitari, G.3    Tam, M.4    Stevenson, M.M.5    Gros, P.6
  • 19
    • 46449103811 scopus 로고    scopus 로고
    • Peroxiredoxin 2 and peroxide metabolism in the erythrocyte
    • F.M. Low, M.B. Hampton, and C.C. Winterbourn Peroxiredoxin 2 and peroxide metabolism in the erythrocyte Antioxid Redox Signal 10 2008 1621 1630
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1621-1630
    • Low, F.M.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 20
    • 0023600030 scopus 로고
    • Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical
    • C.C. Winterbourn, and A. Stern Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical J Clin Invest 80 1987 1486 1491
    • (1987) J Clin Invest , vol.80 , pp. 1486-1491
    • Winterbourn, C.C.1    Stern, A.2
  • 22
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • N. Mohandas, and P.G. Gallagher Red cell membrane: past, present, and future Blood 112 2008 3939 3948
    • (2008) Blood , vol.112 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 23
    • 38049162296 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency: A historical perspective
    • E. Beutler Glucose-6-phosphate dehydrogenase deficiency: a historical perspective Blood 111 2008 16 24
    • (2008) Blood , vol.111 , pp. 16-24
    • Beutler, E.1
  • 24
    • 74149084415 scopus 로고    scopus 로고
    • The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism
    • R.M. Johnson, Y.S. Ho, D.Y. Yu, F.A. Kuypers, Y. Ravindranath, and G.W. Goyette The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism Free Radic Biol Med 48 2010 519 525
    • (2010) Free Radic Biol Med , vol.48 , pp. 519-525
    • Johnson, R.M.1    Ho, Y.S.2    Yu, D.Y.3    Kuypers, F.A.4    Ravindranath, Y.5    Goyette, G.W.6
  • 27
    • 84866627944 scopus 로고    scopus 로고
    • Thioredoxin and glutathione systems in Plasmodium falciparum
    • E. Jortzik, and K. Becker Thioredoxin and glutathione systems in Plasmodium falciparum Int J Med Microbiol 302 2012 187 194
    • (2012) Int J Med Microbiol , vol.302 , pp. 187-194
    • Jortzik, E.1    Becker, K.2
  • 30
    • 0025884353 scopus 로고
    • Comparison of two simple methods for determining malaria parasite density
    • B.M. Greenwood, and J.R. Armstrong Comparison of two simple methods for determining malaria parasite density Trans R Soc Trop Med Hyg 85 1991 186 188
    • (1991) Trans R Soc Trop Med Hyg , vol.85 , pp. 186-188
    • Greenwood, B.M.1    Armstrong, J.R.2
  • 31
    • 0029717668 scopus 로고    scopus 로고
    • Detection and identification of the four malaria parasite species infecting humans by PCR amplification
    • G. Snounou Detection and identification of the four malaria parasite species infecting humans by PCR amplification Methods Mol Biol 50 1996 263 291
    • (1996) Methods Mol Biol , vol.50 , pp. 263-291
    • Snounou, G.1
  • 33
    • 0033797642 scopus 로고    scopus 로고
    • The origin of red cell fluorescence caused by hydrogen peroxide treatment
    • E. Nagababu, F.J. Chrest, and J.M. Rifkind The origin of red cell fluorescence caused by hydrogen peroxide treatment Free Radic Biol Med 29 2000 659 663
    • (2000) Free Radic Biol Med , vol.29 , pp. 659-663
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 35
    • 67650895865 scopus 로고    scopus 로고
    • Quantitative analysis of mechanisms that govern red blood cell age structure and dynamics during anaemia
    • N.J. Savill, W. Chadwick, and S.E. Reece Quantitative analysis of mechanisms that govern red blood cell age structure and dynamics during anaemia PLoS Comput Biol 5 2009 e1000416
    • (2009) PLoS Comput Biol , vol.5 , pp. e1000416
    • Savill, N.J.1    Chadwick, W.2    Reece, S.E.3
  • 36
    • 77953768762 scopus 로고    scopus 로고
    • AMPKalpha1 deletion shortens erythrocyte life span in mice: Role of oxidative stress
    • S. Wang, G.L. Dale, P. Song, B. Viollet, and M.H. Zou AMPKalpha1 deletion shortens erythrocyte life span in mice: role of oxidative stress J Biol Chem 285 2010 19976 19985
    • (2010) J Biol Chem , vol.285 , pp. 19976-19985
    • Wang, S.1    Dale, G.L.2    Song, P.3    Viollet, B.4    Zou, M.H.5
  • 38
    • 11144225843 scopus 로고    scopus 로고
    • ABCA1 gene deletion protects against cerebral malaria: Potential pathogenic role of microparticles in neuropathology
    • V. Combes, N. Coltel, M. Alibert, M. van Eck, C. Raymond, I. Juhan-Vague, G.E. Grau, and G. Chimini ABCA1 gene deletion protects against cerebral malaria: potential pathogenic role of microparticles in neuropathology Am J Pathol 166 2005 295 302
    • (2005) Am J Pathol , vol.166 , pp. 295-302
    • Combes, V.1    Coltel, N.2    Alibert, M.3    Van Eck, M.4    Raymond, C.5    Juhan-Vague, I.6    Grau, G.E.7    Chimini, G.8
  • 39
    • 31544479249 scopus 로고    scopus 로고
    • Severe malarial anemia of low parasite burden in rodent models results from accelerated clearance of uninfected erythrocytes
    • K.J. Evans, D.S. Hansen, N. van Rooijen, L.A. Buckingham, and L. Schofield Severe malarial anemia of low parasite burden in rodent models results from accelerated clearance of uninfected erythrocytes Blood 107 2006 1192 1199
    • (2006) Blood , vol.107 , pp. 1192-1199
    • Evans, K.J.1    Hansen, D.S.2    Van Rooijen, N.3    Buckingham, L.A.4    Schofield, L.5
  • 41
    • 15244352173 scopus 로고    scopus 로고
    • Increased expression of the Abcg2 transporter during erythroid maturation plays a role in decreasing cellular protoporphyrin IX levels
    • S. Zhou, Y. Zong, P.A. Ney, G. Nair, C.F. Stewart, and B.P. Sorrentino Increased expression of the Abcg2 transporter during erythroid maturation plays a role in decreasing cellular protoporphyrin IX levels Blood 105 2005 2571 2576
    • (2005) Blood , vol.105 , pp. 2571-2576
    • Zhou, S.1    Zong, Y.2    Ney, P.A.3    Nair, G.4    Stewart, C.F.5    Sorrentino, B.P.6
  • 42
    • 35348831178 scopus 로고    scopus 로고
    • Age-dependent increase in green autofluorescence of blood erythrocytes
    • S. Khandelwal, and R.K. Saxena Age-dependent increase in green autofluorescence of blood erythrocytes J Biosci 32 2007 1139 1145
    • (2007) J Biosci , vol.32 , pp. 1139-1145
    • Khandelwal, S.1    Saxena, R.K.2
  • 43
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • E. Nagababu, and J.M. Rifkind Heme degradation by reactive oxygen species Antioxid Redox Signal 6 2004 967 978
    • (2004) Antioxid Redox Signal , vol.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 44
    • 0022855189 scopus 로고
    • Porphyria: Genetic and acquired
    • D.J. Cripps Porphyria: genetic and acquired IARC Sci Publ 1986 549 566
    • (1986) IARC Sci Publ , pp. 549-566
    • Cripps, D.J.1
  • 46
    • 77951813369 scopus 로고    scopus 로고
    • Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells
    • C.S. Cho, S. Lee, G.T. Lee, H.A. Woo, E.J. Choi, and S.G. Rhee Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells Antioxid Redox Signal 12 2010 1235 1246
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1235-1246
    • Cho, C.S.1    Lee, S.2    Lee, G.T.3    Woo, H.A.4    Choi, E.J.5    Rhee, S.G.6
  • 47
    • 73549114427 scopus 로고    scopus 로고
    • Role of the membrane in the formation of heme degradation products in red blood cells
    • E. Nagababu, J.G. Mohanty, S. Bhamidipaty, G.R. Ostera, and J.M. Rifkind Role of the membrane in the formation of heme degradation products in red blood cells Life Sci 86 2010 133 138
    • (2010) Life Sci , vol.86 , pp. 133-138
    • Nagababu, E.1    Mohanty, J.G.2    Bhamidipaty, S.3    Ostera, G.R.4    Rifkind, J.M.5
  • 48
    • 27844579180 scopus 로고    scopus 로고
    • Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes
    • P. Arese, F. Turrini, and E. Schwarzer Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes Cell Physiol Biochem 16 2005 133 146
    • (2005) Cell Physiol Biochem , vol.16 , pp. 133-146
    • Arese, P.1    Turrini, F.2    Schwarzer, E.3
  • 53
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • M.V. Karpuj, M.W. Becher, J.E. Springer, D. Chabas, S. Youssef, R. Pedotti, D. Mitchell, and L. Steinman Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine Nat Med 8 2002 143 149
    • (2002) Nat Med , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.