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Volumn 134, Issue 2, 2005, Pages 183-189

Cholesterol inhibits the lytic activity of melittin in erythrocytes

Author keywords

Cholesterol depletion; Erythrocyte membrane; Hemolysis; Melittin; Methyl cyclodextrin

Indexed keywords

CHOLESTEROL; MELITTIN; METHYL BETA CYCLODEXTRIN; PEPTIDE DERIVATIVE; PHOSPHOLIPID;

EID: 15244356065     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2004.12.011     Document Type: Article
Times cited : (51)

References (39)
  • 1
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • L. Abrami, and F.G. van der Goot Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin J. Cell Biol. 147 1999 175 184
    • (1999) J. Cell Biol. , vol.147 , pp. 175-184
    • Abrami, L.1    Van Der Goot, F.G.2
  • 2
    • 0037417761 scopus 로고    scopus 로고
    • Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis
    • D. Allende, and T.J. McIntosh Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis Biochemistry 42 2003 1101 1108
    • (2003) Biochemistry , vol.42 , pp. 1101-1108
    • Allende, D.1    McIntosh, T.J.2
  • 3
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • in press.
    • Allende, D., Simon, S.A., McIntosh, T.J., 2005. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys. J., in press.
    • (2005) Biophys. J.
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 4
    • 0033016103 scopus 로고    scopus 로고
    • Fluorometric method for the enzymatic determination of cholesterol
    • D.M. Amundson, and M. Zhou Fluorometric method for the enzymatic determination of cholesterol J. Biochem. Biophys. Methods 38 1999 43 52
    • (1999) J. Biochem. Biophys. Methods , vol.38 , pp. 43-52
    • Amundson, D.M.1    Zhou, M.2
  • 5
    • 0030997633 scopus 로고    scopus 로고
    • Solution structure of polypeptide from the N terminus of the HIV protein Nef
    • K.J. Barnham, S.A. Monks, M.G. Hinds, A.A. Azad, and R.S. Norton Solution structure of polypeptide from the N terminus of the HIV protein Nef Biochemistry 36 1997 5970 5980
    • (1997) Biochemistry , vol.36 , pp. 5970-5980
    • Barnham, K.J.1    Monks, S.A.2    Hinds, M.G.3    Azad, A.A.4    Norton, R.S.5
  • 6
    • 0031027375 scopus 로고    scopus 로고
    • Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: A property used for membrane targeting
    • T. Benachir, M. Monette, J. Grenier, and M. Lafleur Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: a property used for membrane targeting Eur. Biophys. J. 25 1997 201 210
    • (1997) Eur. Biophys. J. , vol.25 , pp. 201-210
    • Benachir, T.1    Monette, M.2    Grenier, J.3    Lafleur, M.4
  • 7
    • 0032516731 scopus 로고    scopus 로고
    • Membrane sterol composition modulates the pore forming activity of syringomycin e in human red blood cells
    • K. Blasko, L.V. Schagina, G. Agner, Y.A. Kaulin, and J.Y. Takemoto Membrane sterol composition modulates the pore forming activity of syringomycin E in human red blood cells Biochim. Biophys. Acta 1373 1998 163 169
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 163-169
    • Blasko, K.1    Schagina, L.V.2    Agner, G.3    Kaulin, Y.A.4    Takemoto, J.Y.5
  • 8
    • 0033793871 scopus 로고    scopus 로고
    • Regulation of receptor function by cholesterol
    • K. Burger, G. Gimpl, and F. Fahrenholz Regulation of receptor function by cholesterol Cell. Mol. Life Sci. 57 2000 1577 1592
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1577-1592
    • Burger, K.1    Gimpl, G.2    Fahrenholz, F.3
  • 9
    • 0037120762 scopus 로고    scopus 로고
    • Differential effects of cholesterol on acyl chain order in erythrocyte membranes as a function of depth from the surface: An electron paramagnetic resonance (EPR) spin label study
    • M.B. Cassera, A.M. Silber, and A.M. Gennaro Differential effects of cholesterol on acyl chain order in erythrocyte membranes as a function of depth from the surface: an electron paramagnetic resonance (EPR) spin label study Biophys. Chem. 99 2002 117 127
    • (2002) Biophys. Chem. , vol.99 , pp. 117-127
    • Cassera, M.B.1    Silber, A.M.2    Gennaro, A.M.3
  • 10
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • F.-Y. Chen, M.-T. Lee, and H.W. Huang Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 84 2003 3751 3758
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 11
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrins for manipulating cellular cholesterol content
    • A.E. Christian, M.P. Haynes, M.C. Phillips, and G.H. Rothblat Use of cyclodextrins for manipulating cellular cholesterol content J. Lipid Res. 38 1997 2264 2272
    • (1997) J. Lipid Res. , vol.38 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 12
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • C.E. Dempsey The actions of melittin on membranes Biochim. Biophys. Acta 1031 1990 143 161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 13
    • 0036194867 scopus 로고    scopus 로고
    • Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts
    • M. Gandhavadi, D. Allende, D. Vidal, S.A. Simon, and T.J. McIntosh Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts Biophys. J. 82 2002 1469 1482
    • (2002) Biophys. J. , vol.82 , pp. 1469-1482
    • Gandhavadi, M.1    Allende, D.2    Vidal, D.3    Simon, S.A.4    McIntosh, T.J.5
  • 14
    • 0030704248 scopus 로고    scopus 로고
    • Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: Implications in membrane organization and function
    • A.K. Ghosh, R. Rukmini, and A. Chattopadhyay Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function Biochemistry 36 1997 14291 14305
    • (1997) Biochemistry , vol.36 , pp. 14291-14305
    • Ghosh, A.K.1    Rukmini, R.2    Chattopadhyay, A.3
  • 15
    • 0028823176 scopus 로고
    • The interactions of signal sequences with membranes
    • C. Golding, and P. O'Shea The interactions of signal sequences with membranes Biochem. Soc. Trans. 23 1995 971 976
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 971-976
    • Golding, C.1    O'Shea, P.2
  • 16
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • E. Habermann Bee and wasp venoms Science 177 1972 314 322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 17
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location and lipid perturbations of melittin at the membrane interface
    • K. Hristova, C.E. Dempsey, and S.H. White Structure, location and lipid perturbations of melittin at the membrane interface Biophys. J. 80 2001 801 811
    • (2001) Biophys. J. , vol.80 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 19
    • 0015019307 scopus 로고
    • An accurate and convenient organic phosphorus assay
    • C.W.F. McClare An accurate and convenient organic phosphorus assay Anal. Biochem. 39 1971 527 530
    • (1971) Anal. Biochem. , vol.39 , pp. 527-530
    • McClare, C.W.F.1
  • 20
    • 0031872002 scopus 로고    scopus 로고
    • Effect of cholesterol on molecular order and dynamics in highly polyunsaturated phospholipid bilayers
    • D.C. Mitchell, and B.J. Litman Effect of cholesterol on molecular order and dynamics in highly polyunsaturated phospholipid bilayers Biophys. J. 75 1998 896 908
    • (1998) Biophys. J. , vol.75 , pp. 896-908
    • Mitchell, D.C.1    Litman, B.J.2
  • 21
    • 0025162326 scopus 로고
    • G protein activation: A receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
    • M. Mousli, J.-L. Bueb, C. Bronner, B. Rouot, and Y. Landry G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides Trends Pharmacol. Sci. 11 1990 358 362
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 358-362
    • Mousli, M.1    Bueb, J.-L.2    Bronner, C.3    Rouot, B.4    Landry, Y.5
  • 22
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • S. Munro Lipid rafts: elusive or illusive? Cell 115 2003 377 388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 25
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • M. Rabenstein, and Y.K. Shin A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation Biochemistry 34 1995 13390 13397
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 26
    • 0345376179 scopus 로고    scopus 로고
    • Organization and dynamics of melittin in environments of graded hydration: A fluorescence approach
    • H. Raghuraman, and A. Chattopadhyay Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach Langmuir 19 2003 10332 10341
    • (2003) Langmuir , vol.19 , pp. 10332-10341
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 27
    • 15244358803 scopus 로고    scopus 로고
    • Interaction of melittin with membrane cholesterol: A fluorescence approach
    • H. Raghuraman, and A. Chattopadhyay Interaction of melittin with membrane cholesterol: a fluorescence approach Biophys. J. 87 2004 2419 2432
    • (2004) Biophys. J. , vol.87 , pp. 2419-2432
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 28
    • 0037274871 scopus 로고    scopus 로고
    • Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: An EPR spin label study
    • M.G. Rivas, and A.M. Gennaro Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: an EPR spin label study Chem. Phys. Lipids 122 2003 165 169
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 165-169
    • Rivas, M.G.1    Gennaro, A.M.2
  • 29
    • 0026100432 scopus 로고
    • Characterization of lipid domains in erythrocyte membranes
    • W. Rodgers, and M. Glaser Characterization of lipid domains in erythrocyte membranes Proc. Natl. Acad. Sci. USA 88 1991 1364 1368
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1364-1368
    • Rodgers, W.1    Glaser, M.2
  • 30
    • 0344683171 scopus 로고
    • Improved procedure for the extraction of lipids from human erythrocytes
    • H.G. Rose, and M. Oklander Improved procedure for the extraction of lipids from human erythrocytes J. Lipid Res. 6 1965 428 431
    • (1965) J. Lipid Res. , vol.6 , pp. 428-431
    • Rose, H.G.1    Oklander, M.2
  • 31
    • 0034810547 scopus 로고    scopus 로고
    • Cholesterol organization in membranes at low concentrations: Effects of curvature stress and membrane thickness
    • R. Rukmini, S.S. Rawat, S.S. Biswas, and A. Chattopadhyay Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness Biophys. J. 81 2001 2122 2134
    • (2001) Biophys. J. , vol.81 , pp. 2122-2134
    • Rukmini, R.1    Rawat, S.S.2    Biswas, S.S.3    Chattopadhyay, A.4
  • 32
    • 0035800734 scopus 로고    scopus 로고
    • The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection
    • B.U. Samuel, N. Mohandas, T. Harrison, H. McManus, W. Rosse, M. Reid, and K. Haldar The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection J. Biol. Chem. 276 2001 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
  • 33
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 34
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • K. Simons, and E. Ikonen How cells handle cholesterol Science 290 2000 1721 1725
    • (2000) Science , vol.290 , pp. 1721-1725
    • Simons, K.1    Ikonen, E.2
  • 35
    • 0036789540 scopus 로고    scopus 로고
    • Probing red cell membrane cholesterol movement with cyclodextrin
    • T.L. Steck, J. Ye, and Y. Lange Probing red cell membrane cholesterol movement with cyclodextrin Biophys. J. 83 2002 2118 2125
    • (2002) Biophys. J. , vol.83 , pp. 2118-2125
    • Steck, T.L.1    Ye, J.2    Lange, Y.3
  • 36
    • 0033057716 scopus 로고    scopus 로고
    • Biological activities of C-terminal 15-residue synthetic fragment of melittin: Design of an analog with improved antibacterial activity
    • C. Subbalakshmi, R. Nagaraj, and N. Sitaram Biological activities of C-terminal 15-residue synthetic fragment of melittin: design of an analog with improved antibacterial activity FEBS Lett. 448 1999 62 66
    • (1999) FEBS Lett. , vol.448 , pp. 62-66
    • Subbalakshmi, C.1    Nagaraj, R.2    Sitaram, N.3
  • 39
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • P.L. Yeagle Cholesterol and the cell membrane Biochim. Biophys. Acta 822 1985 267 287
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1


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