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Volumn 15, Issue 12, 1999, Pages 488-491

Calcium homeostasis and signaling in the blood-stage malaria parasite

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALCIUM BINDING PROTEIN; CALMODULIN; PROTEIN KINASE;

EID: 0033485874     PISSN: 01694758     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-4758(99)01571-9     Document Type: Review
Times cited : (57)

References (56)
  • 1
    • 0014381540 scopus 로고
    • 2+ content of human erythrocytes
    • 2+ content of human erythrocytes. J. Physiol. 199:1968;367-381.
    • (1968) J. Physiol. , vol.199 , pp. 367-381
    • Harrison, D.G.1    Long, C.2
  • 2
    • 0015101181 scopus 로고
    • The binding of calcium ions by erythrocytes and ghost cell membranes
    • Long C., Mouat B. The binding of calcium ions by erythrocytes and ghost cell membranes. Biochem. J. 123:1971;829-836.
    • (1971) Biochem. J. , vol.123 , pp. 829-836
    • Long, C.1    Mouat, B.2
  • 3
    • 0019302689 scopus 로고
    • Factors affecting the ability of isolated Plasmodium knowlesi merozoites to attach to and invade erythrocytes
    • Johnson J.G.et al. Factors affecting the ability of isolated Plasmodium knowlesi merozoites to attach to and invade erythrocytes. Parasitology. 80:1980;539-550.
    • (1980) Parasitology , vol.80 , pp. 539-550
    • Johnson, J.G.1
  • 4
    • 0025130869 scopus 로고
    • Role of calcium and erythrocyte cytoskeleton phosphorylation in the invasion of Plasmodium falciparum
    • Wasserman M.J.et al. Role of calcium and erythrocyte cytoskeleton phosphorylation in the invasion of Plasmodium falciparum. Parasitol. Res. 76:1990;681-688.
    • (1990) Parasitol. Res. , vol.76 , pp. 681-688
    • Wasserman, M.J.1
  • 5
    • 0023507296 scopus 로고
    • Role of calmodulin in Plasmodium falciparum: Implications for erythrocyte invasion by the merozoite
    • Matsumoto Y.et al. Role of calmodulin in Plasmodium falciparum: implications for erythrocyte invasion by the merozoite. Eur. J. Cell Biol. 45:1987;36-43.
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 36-43
    • Matsumoto, Y.1
  • 6
    • 0026571564 scopus 로고
    • The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum
    • McCallum-Deigthon N., Holder A.A. The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum. Mol. Biochem. Parasitol. 50:1992;317-324.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 317-324
    • McCallum-Deigthon, N.1    Holder, A.A.2
  • 7
    • 0021030104 scopus 로고
    • A cytoplasmic requirement of red cells for invasion by malarial parasites
    • Dluzewski A.R.et al. A cytoplasmic requirement of red cells for invasion by malarial parasites. Mol. Biochem. Parasitol. 9:1983;145-160.
    • (1983) Mol. Biochem. Parasitol. , vol.9 , pp. 145-160
    • Dluzewski, A.R.1
  • 8
    • 0242481218 scopus 로고    scopus 로고
    • Intraerythrocytic calcium chelators inhibit the invasion of P. falciparum
    • Wasserman M., Chaparro J. Intraerythrocytic calcium chelators inhibit the invasion of P. falciparum. Parasitol. Res. 82:1996;102-107.
    • (1996) Parasitol. Res. , vol.82 , pp. 102-107
    • Wasserman, M.1    Chaparro, J.2
  • 9
    • 0020645789 scopus 로고
    • 2+ uptake by mouse erythrocytes in malarial Plasmodium berghei infection
    • 2+ uptake by mouse erythrocytes in malarial Plasmodium berghei infection. Mol. Biochem. Parasitol. 7:1983;227-235.
    • (1983) Mol. Biochem. Parasitol. , vol.7 , pp. 227-235
    • Krungkrai, J.1    Yuthavong, Y.2
  • 10
    • 0020313839 scopus 로고
    • Calcium transport of Plasmodium chabaudi-infected erythrocytes
    • Tanabe K.et al. Calcium transport of Plasmodium chabaudi-infected erythrocytes. J. Cell Biol. 93:1982;680-684.
    • (1982) J. Cell Biol. , vol.93 , pp. 680-684
    • Tanabe, K.1
  • 11
    • 0022388038 scopus 로고
    • Membrane structure and function of malaria parasites and the infected erythrocyte
    • Sherman I.W. Membrane structure and function of malaria parasites and the infected erythrocyte. Parasitology. 91:1985;609-645.
    • (1985) Parasitology , vol.91 , pp. 609-645
    • Sherman, I.W.1
  • 12
    • 0024495679 scopus 로고
    • Rapid clearance of Plasmodium yoelli-infected erythrocytes after exposure to the ionophore A23187
    • Tanabe K., Doi S. Rapid clearance of Plasmodium yoelli-infected erythrocytes after exposure to the ionophore A23187. Comp. Biochem. Physiol. 92:1989;85-89.
    • (1989) Comp. Biochem. Physiol. , vol.92 , pp. 85-89
    • Tanabe, K.1    Doi, S.2
  • 13
    • 0029945188 scopus 로고    scopus 로고
    • 2+ entry into Plasmodium falciparum-infected blood cells
    • 2+ entry into Plasmodium falciparum-infected blood cells. Am. J. Trop. Med. Hyg. 54:1996;464-470.
    • (1996) Am. J. Trop. Med. Hyg. , vol.54 , pp. 464-470
    • Desai, S.A.1
  • 14
    • 0027194909 scopus 로고
    • Cytosolic free calcium in Plasmodium falciparum-infected erythrocytes and the effect of verapamil: A cytometric study
    • Adovelande J.et al. Cytosolic free calcium in Plasmodium falciparum-infected erythrocytes and the effect of verapamil: a cytometric study. Exp. Parasitol. 76:1993;247-258.
    • (1993) Exp. Parasitol. , vol.76 , pp. 247-258
    • Adovelande, J.1
  • 15
    • 0024524808 scopus 로고
    • 2+ and calmodulin modulators
    • 2+ and calmodulin modulators. J. Protozool. 36:1989;139-143.
    • (1989) J. Protozool. , vol.36 , pp. 139-143
    • Tanabe, K.1
  • 16
    • 0027416648 scopus 로고
    • Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxy terminus with the EF-hand calcium-binding proteins
    • Zhao Y.et al. Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxy terminus with the EF-hand calcium-binding proteins. J. Biol. Chem. 268:1993;4347-4354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4347-4354
    • Zhao, Y.1
  • 17
    • 0028121976 scopus 로고
    • Plasmodium falciparum calcium dependent protein kinase phosphorylates proteins of host erythrocyte membrane
    • Zhao Y.et al. Plasmodium falciparum calcium dependent protein kinase phosphorylates proteins of host erythrocyte membrane. Mol. Biochem. Parasitol. 66:1994;329-343.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 329-343
    • Zhao, Y.1
  • 18
    • 0028296130 scopus 로고
    • Calcium-binding properties of a calcium dependent protein kinase from Plasmodium falciparum and the significance of individual calcium binding sites for kinase activation
    • Zhao Y.et al. Calcium-binding properties of a calcium dependent protein kinase from Plasmodium falciparum and the significance of individual calcium binding sites for kinase activation. Biochemistry. 33:1994;3714-3721.
    • (1994) Biochemistry , vol.33 , pp. 3714-3721
    • Zhao, Y.1
  • 19
    • 0030806327 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a second protein kinase of Plasmodium falciparum
    • Farber P.M.et al. Molecular cloning and characterization of a second protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol. 87:1997;211-216.
    • (1997) Mol. Biochem. Parasitol. , vol.87 , pp. 211-216
    • Farber, P.M.1
  • 21
    • 0025148986 scopus 로고
    • 2+ ATPase of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+ ATPase of rabbit skeletal muscle sarcoplasmic reticulum. J. Cell Sci. 97:1990;487-495.
    • (1990) J. Cell Sci. , vol.97 , pp. 487-495
    • Murakami, K.1
  • 22
    • 0027252663 scopus 로고
    • 2+ ATPases
    • 2+ ATPases. J. Cell Sci. 104:1993;1129-1136.
    • (1993) J. Cell Sci. , vol.104 , pp. 1129-1136
    • Kimura, M.1
  • 23
    • 0029069735 scopus 로고
    • 2+-ATPases
    • 2+-ATPases. Gene. 158:1995;133-137.
    • (1995) Gene , vol.158 , pp. 133-137
    • Trottein, F.1
  • 24
    • 0028889183 scopus 로고
    • Molecular cloning and sequence of two novel P-type adenosinetriphosphatases from P. falciparum
    • Trottein F., Cowman A.F. Molecular cloning and sequence of two novel P-type adenosinetriphosphatases from P. falciparum. Eur. J. Biochem. 227:1995;214-225.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 214-225
    • Trottein, F.1    Cowman, A.F.2
  • 25
    • 0029941312 scopus 로고
    • Analysis of a cation-transporting ATPase of Plasmodium falciparum
    • Dyer M.et al. Analysis of a cation-transporting ATPase of Plasmodium falciparum. Mol. Biochem. Parasitol. 78:1994;1-12.
    • (1994) Mol. Biochem. Parasitol. , vol.78 , pp. 1-12
    • Dyer, M.1
  • 26
    • 0026081676 scopus 로고
    • The structure of calmodulin gene of Plasmodium falciparum
    • Robson K.J.H., Jennings M.W. The structure of calmodulin gene of Plasmodium falciparum. Mol. Biochem. Parasitol. 46:1991;19-34.
    • (1991) Mol. Biochem. Parasitol. , vol.46 , pp. 19-34
    • Robson, K.J.H.1    Jennings, M.W.2
  • 27
    • 0023432272 scopus 로고
    • Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): Implications for drug design
    • Scheibel L.W.et al. Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): implications for drug design. Proc. Natl. Acad. Sci. U. S. A. 84:1987;7310-7314.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7310-7314
    • Scheibel, L.W.1
  • 28
    • 0020689512 scopus 로고
    • Transport of ions in erythrocytes infected by Plasmodia
    • Tanabe K.et al. Transport of ions in erythrocytes infected by Plasmodia. Ciba Found. Symp. 94:1983;64-73.
    • (1983) Ciba Found. Symp. , vol.94 , pp. 64-73
    • Tanabe, K.1
  • 29
    • 0026699150 scopus 로고
    • A novel 40 kDa membrane-associated EF-hand calcium-binding protein in Plasmodium falciparum
    • Rawlings D.J., Kaslow D.C. A novel 40 kDa membrane-associated EF-hand calcium-binding protein in Plasmodium falciparum. J. Biol. Chem. 267:1992;3976-3982.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3976-3982
    • Rawlings, D.J.1    Kaslow, D.C.2
  • 30
    • 0009498131 scopus 로고
    • Calcium homeostasis in intact lymphocytes: Cytoplasmic free calcium monitored with a new intracellularly trapped fluorescent indicator
    • Tsien R.Y.et al. Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new intracellularly trapped fluorescent indicator. J. Cell Biol. 260:1982;3440-3450.
    • (1982) J. Cell Biol. , vol.260 , pp. 3440-3450
    • Tsien, R.Y.1
  • 31
    • 0029955417 scopus 로고    scopus 로고
    • Calcium homeostasis in intraerythrocytic malaria parasites
    • Garcia C.R.S.et al. Calcium homeostasis in intraerythrocytic malaria parasites. Eur. J. Cell Biol. 71:1996;409-413.
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 409-413
    • Garcia, C.R.S.1
  • 32
    • 0031283090 scopus 로고    scopus 로고
    • 2+ transport activity associated with a non-mitochondrial calcium pool in the rodent malaria parasite P. chabaudi
    • 2+ transport activity associated with a non-mitochondrial calcium pool in the rodent malaria parasite P. chabaudi. Biochem. Mol. Biol. Int. 42:1997;919-925.
    • (1997) Biochem. Mol. Biol. Int. , vol.42 , pp. 919-925
    • Passos, A.P.D.1    Garcia, C.R.S.2
  • 33
    • 0030775595 scopus 로고    scopus 로고
    • Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple EF-hand motifs in asexual stages of Plasmodium falciparum
    • La Greca N.et al. Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple EF-hand motifs in asexual stages of Plasmodium falciparum. Mol. Biochem. Parasitol. 89:1997;283-293.
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 283-293
    • La Greca, N.1
  • 34
    • 0029045358 scopus 로고
    • 2+ binding protein with multiple EF-hand motifs
    • 2+ binding protein with multiple EF-hand motifs. J. Biochem. 117:1995;1113-1119.
    • (1995) J. Biochem. , vol.117 , pp. 1113-1119
    • Ozawa, M.1
  • 35
    • 0028339802 scopus 로고
    • The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif
    • Weis K.et al. The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J. Biol. Chem. 269:1994;19142-19150.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19142-19150
    • Weis, K.1
  • 36
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan T.et al. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74:1994;595-636.
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1
  • 37
    • 0031837255 scopus 로고    scopus 로고
    • Acidic calcium pools in intraerythrocytic malaria parasites
    • Garcia C.R.S.et al. Acidic calcium pools in intraerythrocytic malaria parasites. Eur. J. Cell Biol. 76:1998;133-138.
    • (1998) Eur. J. Cell Biol. , vol.76 , pp. 133-138
    • Garcia, C.R.S.1
  • 38
    • 0026514177 scopus 로고
    • Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites
    • Slater 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, F.G.1    Cerami, A.2
  • 39
    • 0028947372 scopus 로고
    • Malarial haemozoin/β-haematin supports haem polymerization in the absence of protein
    • Dorn A.et al. Malarial haemozoin/β-haematin supports haem polymerization in the absence of protein. Nature. 374:1995;269-271.
    • (1995) Nature , vol.374 , pp. 269-271
    • Dorn, A.1
  • 40
    • 0028979316 scopus 로고
    • 2+ storage in acidocalcisomes of T. cruzi
    • 2+ storage in acidocalcisomes of T. cruzi. Biochem. J. 310:1995;1005-1012.
    • (1995) Biochem. J. , vol.310 , pp. 1005-1012
    • DoCampo, R.1
  • 41
    • 0009538123 scopus 로고    scopus 로고
    • 2+ content and expression of acidocalcisome calcium pump are elevated in intracellular forms of T. cruzi
    • 2+ content and expression of acidocalcisome calcium pump are elevated in intracellular forms of T. cruzi. J. Biol. Chem. 272:1996;9464-9473.
    • (1996) J. Biol. Chem. , vol.272 , pp. 9464-9473
    • Lu, H.G.1
  • 42
    • 0029935038 scopus 로고    scopus 로고
    • 2+ release from acidocalcisomes of Trypanosoma brucei
    • 2+ release from acidocalcisomes of Trypanosoma brucei. Biochem. J. 315:1996;260-270.
    • (1996) Biochem. J. , vol.315 , pp. 260-270
    • Vercesi, A.E.1    DoCampo, R.2
  • 43
    • 0028171327 scopus 로고
    • + exchange in acidic vacuoles of T. brucei
    • + exchange in acidic vacuoles of T. brucei. Biochem. J. 304:1994;227-233.
    • (1994) Biochem. J. , vol.304 , pp. 227-233
    • Vercesi, A.E.1
  • 44
    • 0029671128 scopus 로고
    • Acidocalcisomes in Toxoplasma gondii tachyzoites
    • Moreno S.N.J., Zhong L. Acidocalcisomes in Toxoplasma gondii tachyzoites. Biochem. J. 313:1993;655-659.
    • (1993) Biochem. J. , vol.313 , pp. 655-659
    • Moreno, S.N.J.1    Zhong, L.2
  • 45
    • 0023664149 scopus 로고
    • 2+ from vacuolar membrane vesicles of oat roots
    • 2+ from vacuolar membrane vesicles of oat roots. J. Biol. Chem. 262:1987;3944-3946.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3944-3946
    • Schumaker, K.S.1    Sze, H.2
  • 47
    • 0020630774 scopus 로고
    • Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Ohsumi Y., Anraku A. Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem. 258:1985;5614-5617.
    • (1985) J. Biol. Chem. , vol.258 , pp. 5614-5617
    • Ohsumi, Y.1    Anraku, A.2
  • 48
    • 0023504658 scopus 로고
    • 2+ uptake in EGTA-treated bovine spermatozoa
    • 2+ uptake in EGTA-treated bovine spermatozoa. Eur. J. Biochem. 169:1987;417-422.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 417-422
    • Rigone, F.1
  • 49
    • 0025919762 scopus 로고
    • 2+ pools in PC12 cells
    • 2+ pools in PC12 cells. J. Biol. Chem. 266:1991;20159-20167.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20159-20167
    • Fasolato, C.1
  • 50
    • 0024327334 scopus 로고
    • 2+ pools in rat pancreatic acinar cells
    • 2+ pools in rat pancreatic acinar cells. J. Membr. Biol. 109:1989;173-186.
    • (1989) J. Membr. Biol. , vol.109 , pp. 173-186
    • Thévenod, F.M.1
  • 51
    • 0040982083 scopus 로고    scopus 로고
    • A plastid of probable green algal origin in apicomplexan parasites
    • Kohller S.et al. A plastid of probable green algal origin in apicomplexan parasites. Science. 275:1997;1485-1489.
    • (1997) Science , vol.275 , pp. 1485-1489
    • Kohller, S.1
  • 53
    • 0028260815 scopus 로고
    • Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte
    • Martin S.K.et al. Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte. J. Parasitol. 80:1994;371-378.
    • (1994) J. Parasitol. , vol.80 , pp. 371-378
    • Martin, S.K.1
  • 54
    • 0032492553 scopus 로고    scopus 로고
    • 2+ release from chloroquine-sensitive and insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi
    • 2+ release from chloroquine-sensitive and insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi. Biochem. Biophys. Res. Commun. 245:1998;155-160.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 155-160
    • Passos, A.P.D.1    Garcia, C.R.S.2
  • 55
    • 0025866878 scopus 로고
    • Direct access to serum macromolecules by intraerythrocytic malaria parasites
    • Pouvelle B.et al. Direct access to serum macromolecules by intraerythrocytic malaria parasites. Nature. 353:1991;73-75.
    • (1991) Nature , vol.353 , pp. 73-75
    • Pouvelle, B.1
  • 56
    • 0030953287 scopus 로고    scopus 로고
    • A membrane network for nutrient import in red cells infected with the malaria parasite
    • Lauer S.A.et al. A membrane network for nutrient import in red cells infected with the malaria parasite. Science. 276:1997;1122-1125.
    • (1997) Science , vol.276 , pp. 1122-1125
    • Lauer, S.A.1


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