메뉴 건너뛰기




Volumn 100, Issue 1, 1999, Pages 61-72

Hemozoin stability and dormant induction of heme oxygenase in hemozoin-fed human monocytes

Author keywords

Heme oxygenase; Hemozoin; Malaria; Monocytes; Phagocytosis

Indexed keywords

CHLOROQUINE; HEME OXYGENASE; HEMOZOIN; METHIONINE; SULFUR 35;

EID: 0032968134     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00031-6     Document Type: Article
Times cited : (33)

References (45)
  • 2
    • 0015071632 scopus 로고
    • The enzymatic degradation of hemoglobin to bile pigments by macrophages
    • Pimstone N.R., Tenhunen R., Seitz P.T., Marver H.S., Schmid R. The enzymatic degradation of hemoglobin to bile pigments by macrophages. J. Exp. Med. 133:1971;1264-1281.
    • (1971) J. Exp. Med. , vol.133 , pp. 1264-1281
    • Pimstone, N.R.1    Tenhunen, R.2    Seitz, P.T.3    Marver, H.S.4    Schmid, R.5
  • 4
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines M.D. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 2:1992;2557-2568.
    • (1992) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 5
    • 0024100201 scopus 로고
    • Regulation of heme oxygenase gene expression
    • Shibahara S. Regulation of heme oxygenase gene expression. Semin. Hematol. 25:1988;370-376.
    • (1988) Semin. Hematol. , vol.25 , pp. 370-376
    • Shibahara, S.1
  • 6
    • 0030764117 scopus 로고    scopus 로고
    • Malarial pigment (haemozoin): A very active 'inert' substance
    • Arese P., Schwarzer E. Malarial pigment (haemozoin): a very active 'inert' substance. Ann. Trop. Med. Parasitol. 91:1997;501-516.
    • (1997) Ann. Trop. Med. Parasitol. , vol.91 , pp. 501-516
    • Arese, P.1    Schwarzer, E.2
  • 7
  • 8
    • 0031021734 scopus 로고    scopus 로고
    • Characterization of the products of the heme detoxification pathway in malarial late trophozoites by X-ray diffraction
    • Bohle D.S., Dinnebier R.E., Madsen S.K., Stephens P.W. Characterization of the products of the heme detoxification pathway in malarial late trophozoites by X-ray diffraction. J. Biol. Chem. 272:1997;713-716.
    • (1997) J. Biol. Chem. , vol.272 , pp. 713-716
    • Bohle, D.S.1    Dinnebier, R.E.2    Madsen, S.K.3    Stephens, P.W.4
  • 10
    • 0026663050 scopus 로고
    • Impairment of macrophage functions after ingestion of Plasmodium falciparum-infected erythrocytes or isolated malarial pigment
    • Schwarzer E., Turrini F., Ulliers D., Giribaldi G., Ginsburg H., Arese P. Impairment of macrophage functions after ingestion of Plasmodium falciparum-infected erythrocytes or isolated malarial pigment. J. Exp. Med. 176:1992;1033-1041.
    • (1992) J. Exp. Med. , vol.176 , pp. 1033-1041
    • Schwarzer, E.1    Turrini, F.2    Ulliers, D.3    Giribaldi, G.4    Ginsburg, H.5    Arese, P.6
  • 11
    • 0027534915 scopus 로고
    • Phagocytosis of P. falciparum malarial pigment hemozoin by human monocytes inactivates monocyte protein kinase C
    • Schwarzer E., Turrini F., Giribaldi G., Arese P. Phagocytosis of P. falciparum malarial pigment hemozoin by human monocytes inactivates monocyte protein kinase C. Biochim. Biophys. Acta. 1181:1993;51-54.
    • (1993) Biochim. Biophys. Acta , vol.1181 , pp. 51-54
    • Schwarzer, E.1    Turrini, F.2    Giribaldi, G.3    Arese, P.4
  • 12
    • 0030598916 scopus 로고    scopus 로고
    • Phagocytosis of malarial pigment hemozoin inhibits NADPH-oxidase activity in human monocyte-derived macrophages
    • Schwarzer E., Arese P. Phagocytosis of malarial pigment hemozoin inhibits NADPH-oxidase activity in human monocyte-derived macrophages. Biochim. Biophys. Acta. 1316:1996;169-175.
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 169-175
    • Schwarzer, E.1    Arese, P.2
  • 13
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R., Marver H.S., Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. USA. 61:1968;748-755.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 14
    • 0017158047 scopus 로고
    • The effect of cobaltous chloride on liver heme metabolism in the rat
    • De Matteis F., Gibbs A.H. The effect of cobaltous chloride on liver heme metabolism in the rat. Ann. Clin. Res. 8(Suppl. 17):1976;193-197.
    • (1976) Ann. Clin. Res , vol.8 , Issue.SUPPL. 17 , pp. 193-197
    • De Matteis, F.1    Gibbs, A.H.2
  • 15
    • 0028077749 scopus 로고
    • A luminescence method for the quantitative determination of phagocytosis of erythrocytes, of malaria-parasitized erythrocytes and of malarial pigment
    • Schwarzer E., Turrini F., Arese P. A luminescence method for the quantitative determination of phagocytosis of erythrocytes, of malaria-parasitized erythrocytes and of malarial pigment. Br. J. Haematol. 88:1994;740-745.
    • (1994) Br. J. Haematol. , vol.88 , pp. 740-745
    • Schwarzer, E.1    Turrini, F.2    Arese, P.3
  • 16
    • 0024272054 scopus 로고
    • Preparation and acidification of lysosomes and lysosomal membranes
    • Schneider D.L., Chin J. Preparation and acidification of lysosomes and lysosomal membranes. Meth. Enzymol. 157:1988;591-601.
    • (1988) Meth. Enzymol. , vol.157 , pp. 591-601
    • Schneider, D.L.1    Chin, J.2
  • 17
    • 0021711079 scopus 로고
    • The oxidation of hemins by microsomal heme oxygenase. Structural requirements for the retention of substrate specificity
    • Tomaro M.L., Frydman R.B., Frydman B., Pandey R.K., Smith K.M. The oxidation of hemins by microsomal heme oxygenase. Structural requirements for the retention of substrate specificity. Biochim. Biophys. Acta. 791:1984;342-349.
    • (1984) Biochim. Biophys. Acta. , vol.791 , pp. 342-349
    • Tomaro, M.L.1    Frydman, R.B.2    Frydman, B.3    Pandey, R.K.4    Smith, K.M.5
  • 18
    • 0003946851 scopus 로고
    • BBA Library, Amsterdam: Elsevier Publishing Company
    • Falk JE. Porphyrins and Metalloporphyrins. BBA Library, Vol 2. Amsterdam: Elsevier Publishing Company, 1964.
    • (1964) Porphyrins and Metalloporphyrins , vol.2
    • Falk, J.E.1
  • 19
    • 0030045312 scopus 로고    scopus 로고
    • Plasmodium hemozoin formation mediated by histidine-rich proteins
    • Sullivan D.J., Gluzman J.Y., Goldberg D.E. Plasmodium hemozoin formation mediated by histidine-rich proteins. Science. 271:1996;219-222.
    • (1996) Science , vol.271 , pp. 219-222
    • Sullivan, D.J.1    Gluzman, J.Y.2    Goldberg, D.E.3
  • 20
    • 0026556492 scopus 로고
    • Endogenous glutathione levels modulate both constitutive and UVA radiation/hydrogen peroxide inducible expression of the human heme oxygenase gene
    • Lautier D., Lüscher P., Tyrrell R.M. Endogenous glutathione levels modulate both constitutive and UVA radiation/hydrogen peroxide inducible expression of the human heme oxygenase gene. Carcinogenesis. 13:1992;227-232.
    • (1992) Carcinogenesis , vol.13 , pp. 227-232
    • Lautier, D.1    Lüscher, P.2    Tyrrell, R.M.3
  • 21
    • 0029915428 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene expression by a glutathione depletor, phorone, mediated through AP-1 activation in rats
    • Oguro T., Hayashi M., Numazawa S., Asakawa K., Yoshida T. Heme oxygenase-1 gene expression by a glutathione depletor, phorone, mediated through AP-1 activation in rats. Biochem. Biophys. Res. Commun. 221:1996;259-265.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 259-265
    • Oguro, T.1    Hayashi, M.2    Numazawa, S.3    Asakawa, K.4    Yoshida, T.5
  • 22
    • 0027673463 scopus 로고
    • Hemoglobin degradation in Plasmodium-infected red blood cells
    • Goldberg D.E. Hemoglobin degradation in Plasmodium-infected red blood cells. Semin. Cell Biol. 4:1993;355-361.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 355-361
    • Goldberg, D.E.1
  • 23
    • 0029013807 scopus 로고
    • The Plasmodium digestive vacuole: Metabolic headquarters and choice drug target
    • Olliaro P.L., Goldberg D.E. The Plasmodium digestive vacuole: Metabolic headquarters and choice drug target. Parasitol. Today. 11:1995;294-297.
    • (1995) Parasitol. Today , vol.11 , pp. 294-297
    • Olliaro, P.L.1    Goldberg, D.E.2
  • 24
    • 0020599554 scopus 로고
    • Assessment of immune phagocytosis of Plasmodium falciparum-infected red blood cells by human monocytes and polymorphonuclear leukocytes. A method for visualizing infected red blood cells ingested by phagocytes
    • Celada A., Cruchaud A., Perrin L.H. Assessment of immune phagocytosis of Plasmodium falciparum-infected red blood cells by human monocytes and polymorphonuclear leukocytes. A method for visualizing infected red blood cells ingested by phagocytes. J. Immunol. Meth. 63:1983;263-271.
    • (1983) J. Immunol. Meth. , vol.63 , pp. 263-271
    • Celada, A.1    Cruchaud, A.2    Perrin, L.H.3
  • 25
    • 0026688902 scopus 로고
    • Phagocytosis of Plasmodium falciparum-infected human red blood cells by human monocytes: Involvement of immune and non-immune determinants and dependence on parasite developmental stage
    • Turrini F., Ginsburg H., Bussolino F., Pescarmona G.P., Serra M.V., Arese P. Phagocytosis of Plasmodium falciparum-infected human red blood cells by human monocytes: Involvement of immune and non-immune determinants and dependence on parasite developmental stage. Blood. 80:1991;801-808.
    • (1991) Blood , vol.80 , pp. 801-808
    • Turrini, F.1    Ginsburg, H.2    Bussolino, F.3    Pescarmona, G.P.4    Serra, M.V.5    Arese, P.6
  • 27
    • 0030591436 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal in human monocytes fed with malarial pigment hemozoin. A possible clue for hemozoin toxicity
    • Schwarzer E., Müller O., Arese P., Siems W.G., Grune T. Increased levels of 4-hydroxynonenal in human monocytes fed with malarial pigment hemozoin. A possible clue for hemozoin toxicity. FEBS Lett. 388:1996;119-122.
    • (1996) FEBS Lett. , vol.388 , pp. 119-122
    • Schwarzer, E.1    Müller, O.2    Arese, P.3    Siems, W.G.4    Grune, T.5
  • 29
    • 0027761831 scopus 로고
    • Reduced microbicidal and anti-tumor activities of human monocytes after ingestion of Plasmodium falciparum-infected red blood cells
    • Fiori P.L., Rappelli P., Mirkarimi S.N., Ginsburg H., Cappuccinelli P., Turrini F. Reduced microbicidal and anti-tumor activities of human monocytes after ingestion of Plasmodium falciparum-infected red blood cells. Parasite Immunol. 15:1993;647-655.
    • (1993) Parasite Immunol. , vol.15 , pp. 647-655
    • Fiori, P.L.1    Rappelli, P.2    Mirkarimi, S.N.3    Ginsburg, H.4    Cappuccinelli, P.5    Turrini, F.6
  • 30
    • 0032036422 scopus 로고    scopus 로고
    • Phagocytosis of malarial pigment, hemozoin, impairs expression of major histocompatibility complex class II antigen, CD 54, and CD11c in human monocytes
    • Schwarzer E., Alessio M., Ulliers D., Arese P. Phagocytosis of malarial pigment, hemozoin, impairs expression of major histocompatibility complex class II antigen, CD 54, and CD11c in human monocytes. Infect. Immun. 66:1998;1601-1606.
    • (1998) Infect. Immun. , vol.66 , pp. 1601-1606
    • Schwarzer, E.1    Alessio, M.2    Ulliers, D.3    Arese, P.4
  • 31
    • 0028090213 scopus 로고
    • Plasmodium falciparum pigment induces monocytes to release high levels of tumor necrosis factor-α And interleukin-1β
    • Pichyangkul S., Saengkrai P., Webster H.K. Plasmodium falciparum pigment induces monocytes to release high levels of tumor necrosis factor-α and interleukin-1β Am. J. Trop. Med. Hyg. 51:1994;430-435.
    • (1994) Am. J. Trop. Med. Hyg. , vol.51 , pp. 430-435
    • Pichyangkul, S.1    Saengkrai, P.2    Webster, H.K.3
  • 32
    • 0031795459 scopus 로고    scopus 로고
    • Neutrophils and monocytes from subjects with the Mediterranean G6PD variant: Effect of Plasmodium falciparum hemozoin on G6PD activity, oxidative burst and cytokine production
    • Mordmüller B., Turrini F., Long H., Kremsner P.G., Arese P. Neutrophils and monocytes from subjects with the Mediterranean G6PD variant: effect of Plasmodium falciparum hemozoin on G6PD activity, oxidative burst and cytokine production. Eur. Cytokine. Netw. 6:1998;239-246.
    • (1998) Eur. Cytokine. Netw. , vol.6 , pp. 239-246
    • Mordmüller, B.1    Turrini, F.2    Long, H.3    Kremsner, P.G.4    Arese, P.5
  • 33
    • 0029089359 scopus 로고
    • Malaria-specific metabolite hemozoin mediates the release of several potent endogenous pyrogens (TNF, MIP-1α, and MIP-1β) in vitro, and altered thermoregulation in vivo
    • Sherry B.A., Alava G., Tracey K.J., Martiney J., Cerami A., Slater A.F.G. Malaria-specific metabolite hemozoin mediates the release of several potent endogenous pyrogens (TNF, MIP-1α, and MIP-1β) in vitro, and altered thermoregulation in vivo. J. Inflammation. 45:1995;85-96.
    • (1995) J. Inflammation , vol.45 , pp. 85-96
    • Sherry, B.A.1    Alava, G.2    Tracey, K.J.3    Martiney, J.4    Cerami, A.5    Slater, A.F.G.6
  • 34
    • 0029073265 scopus 로고
    • Hemozoin differentially modulates the production of interleukin 6 and tumor necrosis factor in murine malaria
    • Prada J., Malinowski J., Müller S., Bienzle U., Kremsner P.G. Hemozoin differentially modulates the production of interleukin 6 and tumor necrosis factor in murine malaria. Eur. Cytokine. Netw. 6:1995;109-112.
    • (1995) Eur. Cytokine. Netw. , vol.6 , pp. 109-112
    • Prada, J.1    Malinowski, J.2    Müller, S.3    Bienzle, U.4    Kremsner, P.G.5
  • 35
    • 0029617970 scopus 로고
    • The heme moiety of malaria pigment (β-hematin) mediates the inhibition of nitric oxide and tumor necrosis factor-α production by lipopolysaccharide stimulated macrophages
    • Taramelli D., Basilico N., Pagani E., Grande R., Monti D., Ghione M., Olliaro P. The heme moiety of malaria pigment (β-hematin) mediates the inhibition of nitric oxide and tumor necrosis factor-α production by lipopolysaccharide stimulated macrophages. Exper. Parasitol. 81:1995;501-511.
    • (1995) Exper. Parasitol. , vol.81 , pp. 501-511
    • Taramelli, D.1    Basilico, N.2    Pagani, E.3    Grande, R.4    Monti, D.5    Ghione, M.6    Olliaro, P.7
  • 36
    • 0002063739 scopus 로고
    • Destruction of erythrocytes
    • G.R. Lee, T.C. Bithell, J. Foerster, J.W. Athens, & J.N. Lukens. Philadelphia: Lea & Febiger
    • Deiss A. Destruction of erythrocytes. Lee G.R., Bithell T.C., Foerster J., Athens J.W., Lukens J.N. Wintrobe's Clinical Hematology. 1993;195-222 Lea & Febiger, Philadelphia.
    • (1993) Wintrobe's Clinical Hematology , pp. 195-222
    • Deiss, A.1
  • 37
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse S.M., Tyrrell R.M. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. USA. 86:1989;99-103.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 38
    • 0025368527 scopus 로고
    • Induction of haem oxygenase as a defence against oxidative stress
    • Stocker R. Induction of haem oxygenase as a defence against oxidative stress. Free. Radic. Res. Commun. 9:1990;101-112.
    • (1990) Free. Radic. Res. Commun. , vol.9 , pp. 101-112
    • Stocker, R.1
  • 40
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile G.F., Basu-Modak S., Waltner C., Tyrrell R.M. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc. Natl. Acad. Sci. USA. 91:1994;2607-2610.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 41
    • 0026514177 scopus 로고
    • Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites
    • Slater A.F.G., Cerami A. Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites. Nature. 355:1992;167-169.
    • (1992) Nature , vol.355 , pp. 167-169
    • Slater, A.F.G.1    Cerami, A.2
  • 42
    • 0026526418 scopus 로고
    • Heme polymerase: Modulation by chloroquine treatment of a rodent malaria
    • Chou A.C., Fitch C.D. Heme polymerase: modulation by chloroquine treatment of a rodent malaria. Life. Sci. 51:1992;2073-2078.
    • (1992) Life. Sci. , vol.51 , pp. 2073-2078
    • Chou, A.C.1    Fitch, C.D.2
  • 44
    • 0019188940 scopus 로고
    • Ferriprotoporphyrin IX fulfills the criteria for identification as the chloroquine receptor of malaria parasites
    • Chou A.C., Chevli R., Fitch C.D. Ferriprotoporphyrin IX fulfills the criteria for identification as the chloroquine receptor of malaria parasites. Biochemistry. 19:1980;1543-1549.
    • (1980) Biochemistry , vol.19 , pp. 1543-1549
    • Chou, A.C.1    Chevli, R.2    Fitch, C.D.3
  • 45
    • 0027315687 scopus 로고
    • Chloroquine: Mechanism of drug action and resistance in Plasmodium falciparum
    • Slater A.F.G. Chloroquine: mechanism of drug action and resistance in Plasmodium falciparum. Pharmac. Ther. 57:1993;203-235.
    • (1993) Pharmac. Ther. , vol.57 , pp. 203-235
    • Slater, A.F.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.