메뉴 건너뛰기




Volumn 23, Issue 1, 2006, Pages 81-88

Lipid rafts and malaria parasite infection of erythrocytes (review)

Author keywords

Detergent resistant membranes; Erythrocyte; Lipid rafts; Malaria; Signaling; Vacuole formation

Indexed keywords

ALPHA GLOBIN; AQUAPORIN 1; BETA 2 ADRENERGIC RECEPTOR; BETA GLOBIN; CD59 ANTIGEN; DECAY ACCELERATING FACTOR; DETERGENT; DUFFY BINDING PROTEIN; ERYTHROCYTE BAND 3 PROTEIN; FLOTILLIN 1; FLOTILLIN 2; GLUCOSE TRANSPORTER 1; GUANINE NUCLEOTIDE BINDING PROTEIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 3; MEMBRANE PROTEIN; PEROXIREDOXIN; PROTEIN S100B; SCRAMBLASE; STIMULATORY GUANINE NUCLEOTIDE BINDING PROTEIN; STOMATIN; UNCLASSIFIED DRUG;

EID: 33645290220     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687860500473440     Document Type: Review
Times cited : (59)

References (58)
  • 4
    • 0034307484 scopus 로고    scopus 로고
    • A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages
    • Bannister LH, Hopkins JM, Fowler RE, Krishna S, Mitchell GH. A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages. Parasitol Today 2000;16:427-433.
    • (2000) Parasitol Today , vol.16 , pp. 427-433
    • Bannister, L.H.1    Hopkins, J.M.2    Fowler, R.E.3    Krishna, S.4    Mitchell, G.H.5
  • 6
    • 0037020192 scopus 로고    scopus 로고
    • The Plasmodium falciparum genome: A blueprint for erythrocyte adhesion
    • Cowman AF, Crabb B. The Plasmodium falciparum genome: a blueprint for erythrocyte adhesion. Science 2002;298:126-128.
    • (2002) Science , vol.298 , pp. 126-128
    • Cowman, A.F.1    Crabb, B.2
  • 7
    • 0035096004 scopus 로고    scopus 로고
    • Molecular insights into receptors used by malaria parasites for erythrocyte invasion
    • Chitnis CE. Molecular insights into receptors used by malaria parasites for erythrocyte invasion. Curr Opin Hematol 2001;8:85-91.
    • (2001) Curr Opin Hematol , vol.8 , pp. 85-91
    • Chitnis, C.E.1
  • 8
    • 0028122878 scopus 로고
    • Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum
    • Sim BK, Chitnis CE, Wasniowska K, Hadley TJ, Miller LH. Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science 1994;264:1941-1944.
    • (1994) Science , vol.264 , pp. 1941-1944
    • Sim, B.K.1    Chitnis, C.E.2    Wasniowska, K.3    Hadley, T.J.4    Miller, L.H.5
  • 9
    • 0035400286 scopus 로고    scopus 로고
    • Uptake and hydrolysis of sphingomyelin analogues in Plasmodium falciparum-infected red cells
    • Lauer SA, Chatterjee S, Haldar K. Uptake and hydrolysis of sphingomyelin analogues in Plasmodium falciparum-infected red cells. Mol Biochem Parasitol 2001;115:275-281.
    • (2001) Mol Biochem Parasitol , vol.115 , pp. 275-281
    • Lauer, S.A.1    Chatterjee, S.2    Haldar, K.3
  • 10
    • 0035800734 scopus 로고    scopus 로고
    • The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection
    • Samuel BU, Mohandas N, Harrison T, McManus H, Rosse W, Reid M, Haldar K. The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection. J Biol Chem 2001;276:29319-29329.
    • (2001) J Biol Chem , vol.276 , pp. 29319-29329
    • Samuel, B.U.1    Mohandas, N.2    Harrison, T.3    McManus, H.4    Rosse, W.5    Reid, M.6    Haldar, K.7
  • 13
    • 0024380375 scopus 로고
    • Membrane assembly and remodelling during reticulocyte maturation
    • Chasis JA, Prenant M, Leung A, Mohandas N. Membrane assembly and remodelling during reticulocyte maturation. Blood 1989;74:1112-1120.
    • (1989) Blood , vol.74 , pp. 1112-1120
    • Chasis, J.A.1    Prenant, M.2    Leung, A.3    Mohandas, N.4
  • 14
    • 0022021094 scopus 로고
    • Red cell membrane biology - Introduction
    • Schrier SL. Red cell membrane biology - introduction. Clin Haematol 1985;14:1-12.
    • (1985) Clin Haematol , vol.14 , pp. 1-12
    • Schrier, S.L.1
  • 15
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D, London E. Functions of lipid rafts in biological membranes. Ann Rev Cell Dev Biol 1998;14:111-136.
    • (1998) Ann Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.1    London, E.2
  • 16
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T, Kurzchalia TV. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 1998;394:802-804.
    • (1998) Nature , vol.394 , pp. 802-804
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 17
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997;387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 18
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in sub micron domains at the cell surface
    • Varma R, Mayor S. GPI-anchored proteins are organized in sub micron domains at the cell surface. Nature 1998;394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 19
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown DA, London E. Structure and origin of ordered lipid domains in biological membranes. J Membr Biol 1998;164:103-114.
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 20
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed SN, Brown DA, London E. On the origin of sphingolipid/cholesterol- rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry 1997;36:10944-10953.
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 21
    • 0036530302 scopus 로고    scopus 로고
    • Ca(++)-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin
    • Salzer U, Hinterdorfer P, Hunger U, Borken C, Prohaska R. Ca(++)-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin. Blood 2002;99:2569-2577.
    • (2002) Blood , vol.99 , pp. 2569-2577
    • Salzer, U.1    Hinterdorfer, P.2    Hunger, U.3    Borken, C.4    Prohaska, R.5
  • 22
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salzer U, Prohaska R. Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 2001;97:1141-1143.
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 24
    • 0032030679 scopus 로고    scopus 로고
    • In vitro incorporation of GPI-anchored proteins into human erythrocytes and their fate in the membrane
    • Civenni G, Test ST, Brodbeck U, Butikofer P. In vitro incorporation of GPI-anchored proteins into human erythrocytes and their fate in the membrane. Blood 1998;91:1784-1792.
    • (1998) Blood , vol.91 , pp. 1784-1792
    • Civenni, G.1    Test, S.T.2    Brodbeck, U.3    Butikofer, P.4
  • 25
    • 0038204140 scopus 로고    scopus 로고
    • New and old integral proteins of the human erythrocyte membrane
    • author reply 3751-3753
    • Minetti G, Ciana A. New and old integral proteins of the human erythrocyte membrane. Blood 2003;101:3751; author reply 3751-3753.
    • (2003) Blood , vol.101 , pp. 3751
    • Minetti, G.1    Ciana, A.2
  • 26
    • 22244473990 scopus 로고    scopus 로고
    • Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton
    • Ciana A, Balduini C, Minetti G. Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton. J Biosci 2005;30:317-328.
    • (2005) J Biosci , vol.30 , pp. 317-328
    • Ciana, A.1    Balduini, C.2    Minetti, G.3
  • 27
    • 0037274871 scopus 로고    scopus 로고
    • Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: An EPR spin label study
    • Rivas MG, Gennaro AM. Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: an EPR spin label study. Chem Phys Lipids 2003;122:165-169.
    • (2003) Chem Phys Lipids , vol.122 , pp. 165-169
    • Rivas, M.G.1    Gennaro, A.M.2
  • 28
    • 0030953111 scopus 로고    scopus 로고
    • Paroxysmal nocturnal hemoglobinuria as a molecular disease
    • Rosse WF. Paroxysmal nocturnal hemoglobinuria as a molecular disease. Medicine 1997;76:63-93.
    • (1997) Medicine , vol.76 , pp. 63-93
    • Rosse, W.F.1
  • 30
    • 0036771552 scopus 로고    scopus 로고
    • Detergent-resistant erythrocyte membrane rafts are modified by a Plasmodium falciparum infection
    • Nagao E, Seydel KB, Dvorak JA. Detergent-resistant erythrocyte membrane rafts are modified by a Plasmodium falciparum infection. Exp Parasitol 2002;102:57-59.
    • (2002) Exp Parasitol , vol.102 , pp. 57-59
    • Nagao, E.1    Seydel, K.B.2    Dvorak, J.A.3
  • 31
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S, Brown DA, Linder ME. Lipid-dependent targeting of G proteins into rafts. J Biol Chem 2000;275:2191-2198.
    • (2000) J Biol Chem , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 32
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linded proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP. Signal transducing molecules and glycosyl-phosphatidylinositol-linded proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 1993;122:789-807.
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 33
    • 0030970954 scopus 로고    scopus 로고
    • Erythrocyte signal transduction pathways and their possible functions
    • Minetti G, Low PS. Erythrocyte signal transduction pathways and their possible functions. Curr Opin Hematol 1997;4:116-121.
    • (1997) Curr Opin Hematol , vol.4 , pp. 116-121
    • Minetti, G.1    Low, P.S.2
  • 34
    • 0026349646 scopus 로고
    • Heterogeneity of guanine nucleotide binding proteins in human red blood cell membranes
    • De Flora A, Damonte G, Sdraffa A, Franco L, Benatti U. Heterogeneity of guanine nucleotide binding proteins in human red blood cell membranes. Adv Exp Med Biol 1991;307:161-171.
    • (1991) Adv Exp Med Biol , vol.307 , pp. 161-171
    • De Flora, A.1    Damonte, G.2    Sdraffa, A.3    Franco, L.4    Benatti, U.5
  • 35
    • 0029783929 scopus 로고    scopus 로고
    • Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences
    • Johnson GJ, Leis LA, Dunlop PC. Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences. Biochem J 1996;318 (Pt 3):1023-1031.
    • (1996) Biochem J , vol.318 , Issue.3 PART , pp. 1023-1031
    • Johnson, G.J.1    Leis, L.A.2    Dunlop, P.C.3
  • 36
    • 0024456950 scopus 로고
    • The G alpha z gene product in human erythrocytes. Identification as a 41-kilodalton protein
    • Premont RT, Buku A, Iyengar R. The G alpha z gene product in human erythrocytes. Identification as a 41-kilodalton protein. J Biol Chem 1989;264:14960-14964.
    • (1989) J Biol Chem , vol.264 , pp. 14960-14964
    • Premont, R.T.1    Buku, A.2    Iyengar, R.3
  • 37
    • 0027469831 scopus 로고
    • Identification of G alpha 11 as the phospholipase C-activating G-protein of turkey erythrocytes
    • Maurice DH, Waldo GL, Morris AJ, Nicholas RA, Harden TK. Identification of G alpha 11 as the phospholipase C-activating G-protein of turkey erythrocytes. Biochem J 1993;290 (Pt 3):765-770.
    • (1993) Biochem J , vol.290 , Issue.3 PART , pp. 765-770
    • Maurice, D.H.1    Waldo, G.L.2    Morris, A.J.3    Nicholas, R.A.4    Harden, T.K.5
  • 38
    • 0028172764 scopus 로고
    • The turkey erythrocyte beta-adrenergic receptor couples to both adenylate cyclase and phospholipase C via distinct G-protein alpha subunits
    • James SR, Vaziri C, Walker TR, Milligan G, Downes CP. The turkey erythrocyte beta-adrenergic receptor couples to both adenylate cyclase and phospholipase C via distinct G-protein alpha subunits. Biochem J 1994;304 (Pt 2):359-364.
    • (1994) Biochem J , vol.304 , Issue.2 PART , pp. 359-364
    • James, S.R.1    Vaziri, C.2    Walker, T.R.3    Milligan, G.4    Downes, C.P.5
  • 39
    • 0041506933 scopus 로고    scopus 로고
    • Pharmacology and physiology of human adrenergic receptor polymorphisms
    • Small KM, McGraw DW, Liggett SB. Pharmacology and physiology of human adrenergic receptor polymorphisms. Annu Rev Pharmacol Toxicol 2003;43:381-411.
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 381-411
    • Small, K.M.1    McGraw, D.W.2    Liggett, S.B.3
  • 40
    • 0033134810 scopus 로고    scopus 로고
    • Beta-adrenergic agonists regulate cell membrane fluctuations of human erythrocytes
    • Tuvia S, Moses A, Gulayev N, Levin S, Korenstein R. Beta-adrenergic agonists regulate cell membrane fluctuations of human erythrocytes. J Physiol 1999;516:781-792.
    • (1999) J Physiol , vol.516 , pp. 781-792
    • Tuvia, S.1    Moses, A.2    Gulayev, N.3    Levin, S.4    Korenstein, R.5
  • 42
    • 0016695533 scopus 로고
    • The effect of catecholamines and prostaglandins upon human and rat erythrocytes
    • Rasmussen H, Lake W, Allen JE. The effect of catecholamines and prostaglandins upon human and rat erythrocytes. Biochim Biophys Acta 1975;411:63-73.
    • (1975) Biochim Biophys Acta , vol.411 , pp. 63-73
    • Rasmussen, H.1    Lake, W.2    Allen, J.E.3
  • 43
    • 0015244729 scopus 로고
    • Human red blood cells: Prostaglandin E2, epinephrine, and isoproterenol alter deformability
    • Allen JE, Rasmussen H. Human red blood cells: prostaglandin E2, epinephrine, and isoproterenol alter deformability. Science 1971;174:512-514.
    • (1971) Science , vol.174 , pp. 512-514
    • Allen, J.E.1    Rasmussen, H.2
  • 44
    • 0027493507 scopus 로고
    • Glucagon and noradrenaline reduce erythrocyte deformability
    • Valensi P, Gaudey F, Parries J, Attali JR. Glucagon and noradrenaline reduce erythrocyte deformability. Metabolism 1993;42:1169-1172.
    • (1993) Metabolism , vol.42 , pp. 1169-1172
    • Valensi, P.1    Gaudey, F.2    Parries, J.3    Attali, J.R.4
  • 45
    • 0022838882 scopus 로고
    • Effect of parathyroid hormone and uremia on erythrocyte deformability
    • Bogin E, Earon Y, Blum M. Effect of parathyroid hormone and uremia on erythrocyte deformability. Clin Chim Acta 1986;161:293-299.
    • (1986) Clin Chim Acta , vol.161 , pp. 293-299
    • Bogin, E.1    Earon, Y.2    Blum, M.3
  • 46
    • 0015951923 scopus 로고
    • A functional acetylcholine receptor in the human erythrocyte
    • Huestis WH, McConnell HM. A functional acetylcholine receptor in the human erythrocyte. Biochem Biophys Res Commun 1974;57:726-732.
    • (1974) Biochem Biophys Res Commun , vol.57 , pp. 726-732
    • Huestis, W.H.1    McConnell, H.M.2
  • 48
    • 4544273781 scopus 로고    scopus 로고
    • Epinephrine acts through erythroid signaling pathways to activate sickle cell adhesion to endothelium via LW-alphavbeta3 interactions
    • Zennadi R, Hines PC, De Castro LM, Cartron JP, Parise LV, Telen MJ. Epinephrine acts through erythroid signaling pathways to activate sickle cell adhesion to endothelium via LW-alphavbeta3 interactions. Blood 2004;104:3774-3781.
    • (2004) Blood , vol.104 , pp. 3774-3781
    • Zennadi, R.1    Hines, P.C.2    De Castro, L.M.3    Cartron, J.P.4    Parise, L.V.5    Telen, M.J.6
  • 50
    • 0035039037 scopus 로고    scopus 로고
    • Co-stimulation and counter-stimulation: Lipid raft clustering controls TCR signaling and functional outcomes
    • Miceli MC, Moran M, Chung CD, Patel VP, Low T, Zinnanti W. Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes. Semin Immunol 2001;13:115-128.
    • (2001) Semin Immunol , vol.13 , pp. 115-128
    • Miceli, M.C.1    Moran, M.2    Chung, C.D.3    Patel, V.P.4    Low, T.5    Zinnanti, W.6
  • 51
    • 4444236958 scopus 로고    scopus 로고
    • Control of immune responses by trafficking cell surface proteins, vesicles and lipid rafts to and from the immunological synapse
    • Taner SB, Onfelt B, Pirinen NJ, McCann FE, Magee AI, Davis DM. Control of immune responses by trafficking cell surface proteins, vesicles and lipid rafts to and from the immunological synapse. Traffic 2004;5:651-661.
    • (2004) Traffic , vol.5 , pp. 651-661
    • Taner, S.B.1    Onfelt, B.2    Pirinen, N.J.3    McCann, F.E.4    Magee, A.I.5    Davis, D.M.6
  • 52
    • 0348111350 scopus 로고    scopus 로고
    • Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites, a role for microbial raft proteins in apicomplexan vacuole biogenesis
    • Hiller NL, Akompong T, Morrow JS, Holder AA, Haldar K. Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites, A role for microbial raft proteins in apicomplexan vacuole biogenesis. J Biol Chem 2003;278:48413-48421.
    • (2003) J Biol Chem , vol.278 , pp. 48413-48421
    • Hiller, N.L.1    Akompong, T.2    Morrow, J.S.3    Holder, A.A.4    Haldar, K.5
  • 53
    • 0033617415 scopus 로고    scopus 로고
    • Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
    • Volonte D, Galbiati F, Li S, Nishiyama K, Okamoto T, Lisanti MP. Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe. J Biol Chem 1999;274:12702-12709.
    • (1999) J Biol Chem , vol.274 , pp. 12702-12709
    • Volonte, D.1    Galbiati, F.2    Li, S.3    Nishiyama, K.4    Okamoto, T.5    Lisanti, M.P.6
  • 54
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: Rafts, worms and anaesthetics
    • Morrow IC, Parton RG. Flotillins and the PHB domain protein family: rafts, worms and anaesthetics. Traffic 2005;6:725-740.
    • (2005) Traffic , vol.6 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 55
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson RG, Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 2002;296:1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 56
    • 0032578034 scopus 로고    scopus 로고
    • Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes
    • Tuvia S, Levin S, Bitler A, Korenstein R. Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes. J Cell Biol 1998;141:1551-1561.
    • (1998) J Cell Biol , vol.141 , pp. 1551-1561
    • Tuvia, S.1    Levin, S.2    Bitler, A.3    Korenstein, R.4
  • 57
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPAses in cell biology
    • Etienne-Manneville S, Hall A. Rho GTPAses in cell biology. Nature 2002;240:629-635.
    • (2002) Nature , vol.240 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.