메뉴 건너뛰기




Volumn 8, Issue 1, 2009, Pages

Chloroquine reduces arylsulphatase B activity and increases chondroitin-4-sulphate: Implications for mechanisms of action and resistance

Author keywords

[No Author keywords available]

Indexed keywords

ARYLSULFATASE; ARYLSULPHATASE B; CHLOROQUINE; CHONDROITIN 4 SULFATE; GLYCOSAMINOGLYCAN; UNCLASSIFIED DRUG; ANTIMALARIAL AGENT; CHONDROITIN SULFATE; ENZYME INHIBITOR;

EID: 76749112961     PISSN: None     EISSN: 14752875     Source Type: Journal    
DOI: 10.1186/1475-2875-8-303     Document Type: Article
Times cited : (20)

References (23)
  • 1
    • 0031081447 scopus 로고    scopus 로고
    • Chondroitin sulfate A as an adherence receptor for Plasmodium falciparum-infected erythrocytes
    • 10.1016/S0169-4758(96)10081-8. 15275126
    • Chondroitin sulfate A as an adherence receptor for Plasmodium falciparum-infected erythrocytes. SJ Rogerson GV Brown, Parasitol Today 1997 13 70 75 10.1016/S0169-4758(96)10081-8 15275126
    • (1997) Parasitol Today , vol.13 , pp. 70-75
    • Rogerson, S.J.1    Brown, G.V.2
  • 2
    • 0031842404 scopus 로고    scopus 로고
    • Inhibition of binding of malaria-infected erythrocytes by a tetradecasaccharide fraction from chondroitin sulfate A
    • 9632611
    • Inhibition of binding of malaria-infected erythrocytes by a tetradecasaccharide fraction from chondroitin sulfate A. JG Beeson W Chai SJ Rogerson AM Lawson GV Brown, Infect Immun 1998 66 3397 3402 9632611
    • (1998) Infect Immun , vol.66 , pp. 3397-3402
    • Beeson, J.G.1    Chai, W.2    Rogerson, S.J.3    Lawson, A.M.4    Brown, G.V.5
  • 3
    • 34447338059 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycan but not hyaluronic acid is the receptor for the adherence of Plasmodium falciparum-infected erythrocytes in human placenta, and infected red blood cell adherence up-regulates the receptor expression
    • 10.2353/ajpath.2007.061238. 17525266
    • Chondroitin sulfate proteoglycan but not hyaluronic acid is the receptor for the adherence of Plasmodium falciparum-infected erythrocytes in human placenta, and infected red blood cell adherence up-regulates the receptor expression. A Muthusamy RN Achur M Valiyaveettil JJ Botti DW Taylor RF Leke DC Gowda, Am J Pathol 2007 170 1989 2000 10.2353/ajpath.2007.061238 17525266
    • (2007) Am J Pathol , vol.170 , pp. 1989-2000
    • Muthusamy, A.1    Achur, R.N.2    Valiyaveettil, M.3    Botti, J.J.4    Taylor, D.W.5    Leke, R.F.6    Gowda, D.C.7
  • 4
    • 33845932552 scopus 로고    scopus 로고
    • Rat spongiotrophoblast-specific protein is predominantly a unique low sulfated chondroitin sulfate proteoglycan
    • 10.1074/jbc.M605841200. 16954212
    • Rat spongiotrophoblast-specific protein is predominantly a unique low sulfated chondroitin sulfate proteoglycan. RN Achur ST Agbor-Enoh DC Gowda, J Biol Chem 2006 281 32327 32334 10.1074/jbc.M605841200 16954212
    • (2006) J Biol Chem , vol.281 , pp. 32327-32334
    • Achur, R.N.1    Agbor-Enoh, S.T.2    Gowda, D.C.3
  • 5
    • 34547931107 scopus 로고    scopus 로고
    • Structural basis for binding of Plasmodium falciparum erythrocyte membrane protein 1 to chondroitin sulfate and placental tissue and the influence of protein polymorphisms on binding specificity
    • 10.1074/jbc.M700231200. 17562715
    • Structural basis for binding of Plasmodium falciparum erythrocyte membrane protein 1 to chondroitin sulfate and placental tissue and the influence of protein polymorphisms on binding specificity. JG Beeson KT Andrews M Boyle MF Duffy EK Choong TJ Byrne JM Chesson AM Lawson W Chai, J Biol Chem 2007 282 22426 22436 10.1074/jbc.M700231200 17562715
    • (2007) J Biol Chem , vol.282 , pp. 22426-22436
    • Beeson, J.G.1    Andrews, K.T.2    Boyle, M.3    Duffy, M.F.4    Choong, E.K.5    Byrne, T.J.6    Chesson, J.M.7    Lawson, A.M.8    Chai, W.9
  • 6
    • 33646022245 scopus 로고    scopus 로고
    • Plasmodium falciparum: Chondroitin sulfate A is the major receptor for adhesion of parasitized erythrocytes in the placenta
    • 10.1016/j.exppara.2005.12.003. 16430888
    • Plasmodium falciparum: Chondroitin sulfate A is the major receptor for adhesion of parasitized erythrocytes in the placenta. M Fried GJ Domingo CD Gowda TK Mutabingwa PE Duffy, Exp Parasitol 2006 113 36 42 10.1016/j.exppara. 2005.12.003 16430888
    • (2006) Exp Parasitol , vol.113 , pp. 36-42
    • Fried, M.1    Domingo, G.J.2    Gowda, C.D.3    Mutabingwa, T.K.4    Duffy, P.E.5
  • 7
    • 4444235642 scopus 로고    scopus 로고
    • Plasmodium falciparum: Adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains
    • 10.1016/j.exppara.2004.05.003. 15363944
    • Plasmodium falciparum: adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains. A Muthusamy RN Achur M Valiyaveettil DC Gowda, Exp Parasitol 2004 107 183 188 10.1016/j.exppara.2004.05.003 15363944
    • (2004) Exp Parasitol , vol.107 , pp. 183-188
    • Muthusamy, A.1    Achur, R.N.2    Valiyaveettil, M.3    Gowda, D.C.4
  • 8
    • 0034704147 scopus 로고    scopus 로고
    • Characterization of proteoglycans of human placenta and identification of unique chondroitin sulfate proteoglycans of the intervillous spaces that mediate the adherence of Plasmodium falciparum-infected erythrocytes to the placenta
    • 10.1074/jbc.M006398200. 11005814
    • Characterization of proteoglycans of human placenta and identification of unique chondroitin sulfate proteoglycans of the intervillous spaces that mediate the adherence of Plasmodium falciparum-infected erythrocytes to the placenta. RN Achur M Valiyaveettil A Alkhalil CF Ockenhouse DC Gowda, J Biol Chem 2000 275 40344 40356 10.1074/jbc.M006398200 11005814
    • (2000) J Biol Chem , vol.275 , pp. 40344-40356
    • Achur, R.N.1    Valiyaveettil, M.2    Alkhalil, A.3    Ockenhouse, C.F.4    Gowda, D.C.5
  • 9
    • 0034704065 scopus 로고    scopus 로고
    • Structural requirements for the adherence of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate proteoglycans of human placenta
    • 10.1074/jbc.M006399200. 11005815
    • Structural requirements for the adherence of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate proteoglycans of human placenta. A Alkhalil RN Achur M Valiyaveettil CF Ockenhouse DC Gowda, J Biol Chem 2000 275 40357 40364 10.1074/jbc.M006399200 11005815
    • (2000) J Biol Chem , vol.275 , pp. 40357-40364
    • Alkhalil, A.1    Achur, R.N.2    Valiyaveettil, M.3    Ockenhouse, C.F.4    Gowda, D.C.5
  • 10
    • 0037838883 scopus 로고    scopus 로고
    • The low sulfated chondroitin sulfate proteoglycans of human placenta have sulfate group-clustered domains that can efficiently bind Plasmodium falciparum-infected erythrocytes
    • 10.1074/jbc.M211015200. 12517756
    • The low sulfated chondroitin sulfate proteoglycans of human placenta have sulfate group-clustered domains that can efficiently bind Plasmodium falciparum-infected erythrocytes. RN Achur M Valiyaveettil DC Gowda, J Biol Chem 2003 278 11705 11713 10.1074/jbc.M211015200 12517756
    • (2003) J Biol Chem , vol.278 , pp. 11705-11713
    • Achur, R.N.1    Valiyaveettil, M.2    Gowda, D.C.3
  • 11
    • 2442676739 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes adhere both in the intervillous space and on the villous surface of human placenta by binding to the low-sulfated chondroitin sulfate proteoglycan receptor
    • 15161637
    • Plasmodium falciparum-infected erythrocytes adhere both in the intervillous space and on the villous surface of human placenta by binding to the low-sulfated chondroitin sulfate proteoglycan receptor. A Muthusamy RN Achur VP Bhavanandan GG Fouda DW Taylor DC Gowda, Am J Pathol 2004 164 2013 2025 15161637
    • (2004) Am J Pathol , vol.164 , pp. 2013-2025
    • Muthusamy, A.1    Achur, R.N.2    Bhavanandan, V.P.3    Fouda, G.G.4    Taylor, D.W.5    Gowda, D.C.6
  • 12
    • 41549117509 scopus 로고    scopus 로고
    • Binding affinity of Plasmodium falciparum-infected erythrocytes from infected placentas and laboratory selected strains to chondroitin 4-sulfate
    • 10.1016/j.molbiopara.2008.02.002. 18359524
    • Binding affinity of Plasmodium falciparum-infected erythrocytes from infected placentas and laboratory selected strains to chondroitin 4-sulfate. RN Achur A Muthusamy SV Madhunapantula DC Gowda, Mol Biochem Parasitol 2008 159 79 84 10.1016/j.molbiopara.2008.02.002 18359524
    • (2008) Mol Biochem Parasitol , vol.159 , pp. 79-84
    • Achur, R.N.1    Muthusamy, A.2    Madhunapantula, S.V.3    Gowda, D.C.4
  • 13
    • 33947705107 scopus 로고    scopus 로고
    • Increased arylsulfatase B activity in cystic fibrosis cells following correction of CFTR
    • 10.1016/j.cca.2007.01.021. 17324393
    • Increased arylsulfatase B activity in cystic fibrosis cells following correction of CFTR. S Bhattacharyya JK Tobacman, Clin Chim Acta 2007 380 122 127 10.1016/j.cca.2007.01.021 17324393
    • (2007) Clin Chim Acta , vol.380 , pp. 122-127
    • Bhattacharyya, S.1    Tobacman, J.K.2
  • 14
    • 44349103674 scopus 로고    scopus 로고
    • Distinct effects of N-acetylgalactosamine-4-sulfatase and galactose-6-sulfatase expression on chondroitin sulfates
    • 10.1074/jbc.M707967200. 18285341
    • Distinct effects of N-acetylgalactosamine-4-sulfatase and galactose-6-sulfatase expression on chondroitin sulfates. S Bhattacharyya K Kotlo S Shukla RS Danziger JK Tobacman, J Biol Chem 2008 283 9523 9530 10.1074/jbc.M707967200 18285341
    • (2008) J Biol Chem , vol.283 , pp. 9523-9530
    • Bhattacharyya, S.1    Kotlo, K.2    Shukla, S.3    Danziger, R.S.4    Tobacman, J.K.5
  • 16
    • 68049133153 scopus 로고    scopus 로고
    • Arylsulfatase B regulates colonic epithelial cell migration by effects on MMP9 expression and RhoA activation
    • 10.1007/s10585-009-9253-z. 19306108
    • Arylsulfatase B regulates colonic epithelial cell migration by effects on MMP9 expression and RhoA activation. S Bhattacharyya JK Tobacman, Clin Exp Metastasis 2009 26 535 545 10.1007/s10585-009-9253-z 19306108
    • (2009) Clin Exp Metastasis , vol.26 , pp. 535-545
    • Bhattacharyya, S.1    Tobacman, J.K.2
  • 17
    • 33751441226 scopus 로고    scopus 로고
    • Steroid sulfatase, arylsulfatases A and B, galactose 6-sulfatase, and iduronate sulfatase in mammary cells and effects of sulfated and non-sulfated estrogens on sulfatase activity
    • 10.1016/j.jsbmb.2006.08.002. 17064891
    • Steroid sulfatase, arylsulfatases A and B, galactose 6-sulfatase, and iduronate sulfatase in mammary cells and effects of sulfated and non-sulfated estrogens on sulfatase activity. S Bhattacharyya JK Tobacman, J Steroid Biochem Mol Biol 2006 103 20 34 10.1016/j.jsbmb.2006.08.002 17064891
    • (2006) J Steroid Biochem Mol Biol , vol.103 , pp. 20-34
    • Bhattacharyya, S.1    Tobacman, J.K.2
  • 18
    • 66349123838 scopus 로고    scopus 로고
    • Quantification of heparan sulfate and heparin disaccharides using ion-pairing, reversed-phase, microflow, high performance liquid chromatography coupled with electrospray ionization trap mass spectrometry
    • 10.1021/ac9001707. 19402671
    • Quantification of heparan sulfate and heparin disaccharides using ion-pairing, reversed-phase, microflow, high performance liquid chromatography coupled with electrospray ionization trap mass spectrometry. Z Zhang J Xie H Liu J Liu RJ Linhardt, Anal Chem 2009 81 4349 4355 10.1021/ac9001707 19402671
    • (2009) Anal Chem , vol.81 , pp. 4349-4355
    • Zhang, Z.1    Xie, J.2    Liu, H.3    Liu, J.4    Linhardt, R.J.5
  • 19
    • 33745219671 scopus 로고    scopus 로고
    • Placental chondroitin sulfate A-binding malarial isolates evade innate phagocytic clearance
    • 10.1086/504721. 16741892
    • Placental chondroitin sulfate A-binding malarial isolates evade innate phagocytic clearance. L Serghides SN Patel K Ayi KC Kain, J Infect Dis 2006 194 133 139 10.1086/504721 16741892
    • (2006) J Infect Dis , vol.194 , pp. 133-139
    • Serghides, L.1    Patel, S.N.2    Ayi, K.3    Kain, K.C.4
  • 21
    • 0023272746 scopus 로고    scopus 로고
    • A ferriprotoporphyrin IX-chloroquine complex promotes membrane phospholipid peroxidation
    • 10.1016/0014-5793(87)80299-5. 3666151
    • A ferriprotoporphyrin IX-chloroquine complex promotes membrane phospholipid peroxidation. Y Sugioka M Suzuki K Sugioka M Nakano, FEBS Letters 223 251 254 10.1016/0014-5793(87)80299-5 3666151
    • FEBS Letters , vol.223 , pp. 251-254
    • Sugioka, Y.1    Suzuki, M.2    Sugioka, K.3    Nakano, M.4
  • 22
    • 0023105195 scopus 로고
    • The basis of antimalarial action: Non-weak base effects of chloroquine on acid vesicle pH
    • 2435182
    • The basis of antimalarial action: non-weak base effects of chloroquine on acid vesicle pH. DJ Krogstad PH Schlesinger, Am J Trop Med Hyg 1987 36 213 210 2435182
    • (1987) Am J Trop Med Hyg , vol.36 , pp. 213-210
    • Krogstad, D.J.1    Schlesinger, P.H.2
  • 23
    • 34247864147 scopus 로고    scopus 로고
    • Chemotherapy of protozoal infections: Malaria
    • New York, NY, USA: McGraw-Hill Companies, Inc Brunton LL, Lazo JS, Parker KL 11
    • Chemotherapy of Protozoal Infections: Malaria. TA Shapiro DE Goldberg, Goodman and Gillman's Pharmacological Basis of Therapeutics New York, NY, USA: McGraw-Hill Companies, Inc, Brunton LL, Lazo JS, Parker KL, 11 2008 Chaper 39 1021 1048
    • (2008) Goodman and Gillman's Pharmacological Basis of Therapeutics , vol.39 , pp. 1021-1048
    • Shapiro, T.A.1    Goldberg, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.