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Volumn 48, Issue 19, 2009, Pages 4198-4208

The toxicity of prion protein fragment PrP(106-126) is not mediated by membrane permeabilization as shown by a M112W substitution

Author keywords

[No Author keywords available]

Indexed keywords

ISOFORM; MEMBRANE PERMEABILIZATION; MEMBRANE PORES; PEPTIDE-MEMBRANE INTERACTIONS; PHYSIOLOGICAL CONDITION; PORE FORMATION; POST-TRANSLATIONAL MODIFICATIONS; PRION DISEASE; PRION PROTEIN; TOXIC EFFECT;

EID: 66049086991     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900009d     Document Type: Article
Times cited : (29)

References (49)
  • 2
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002. (Pubitemid 23086050)
    • (1993) Biochemistry , vol.32 , Issue.8 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 3
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. (1991) Molecular biology of prion diseases. Science 252, 1515-1522 (Pubitemid 21917065)
    • (1991) Science , vol.252 , Issue.5012 , pp. 1515-1522
    • Prusiner, S.B.1
  • 6
    • 15544379325 scopus 로고    scopus 로고
    • Aggregation and fibrillization of prions in lipid membranes
    • Kazlauskaite, J., and Pinheiro, T. J. (2005) Aggregation and fibrillization of prions in lipid membranes. Biochem. Soc. Symp. 211-222
    • (2005) Biochem. Soc. Symp. , pp. 211-222
    • Kazlauskaite, J.1    Pinheiro, T.J.2
  • 7
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • DOI 10.1074/jbc.272.10.6324
    • Naslavsky, N., Stein,R., Yanai, A., Friedlander,G., and Taraboulos, A. (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272, 6324-6331 (Pubitemid 27118107)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 9
    • 0032213349 scopus 로고    scopus 로고
    • Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line
    • DOI 10.1002/(SICI)1097-4547(19981101)54:3<341::AID-JNR5>3.0.CO;2-G
    • Florio, T., Thellung, S., Amico, C., Robello, M., Salmona, M., Bugiani, O., Tagliavini, F., Forloni, G., and Schettini, G. (1998) Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line. J. Neurosci. Res. 54, 341-352 (Pubitemid 28493944)
    • (1998) Journal of Neuroscience Research , vol.54 , Issue.3 , pp. 341-352
    • Florio, T.1    Thellung, S.2    Amico, C.3    Robello, M.4    Salmona, M.5    Bugiani, O.6    Tagliavini, F.7    Forloni, G.8    Schettini, G.9
  • 11
    • 10644226077 scopus 로고    scopus 로고
    • The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species
    • DOI 10.1016/j.mcn.2004.09.006, PII S1044743104002192
    • Fioriti, L., Quaglio, E., Massignan, T., Colombo, L., Stewart, R. S., Salmona, M., Harris, D. A., Forloni, G., and Chiesa, R. (2005) The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species. Mol. Cell. Neurosci. 28, 165-176 (Pubitemid 39656020)
    • (2005) Molecular and Cellular Neuroscience , vol.28 , Issue.1 , pp. 165-176
    • Fioriti, L.1    Quaglio, E.2    Massignan, T.3    Colombo, L.4    Stewart, R.S.5    Salmona, M.6    Harris, D.A.7    Forloni, G.8    Chiesa, R.9
  • 13
    • 0033774525 scopus 로고    scopus 로고
    • Prion peptide fragment PrP [106-126] forms distinct cation channel types
    • Kourie, J. I., and Culverson, A. (2000) Prion peptide fragment PrP [106-126] forms distinct cation channel types. J. Neurosci. Res. 62, 120-133
    • (2000) J. Neurosci. Res. , vol.62 , pp. 120-133
    • Kourie, J.I.1    Culverson, A.2
  • 14
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • DOI 10.1074/jbc.272.1.44
    • Lin, M. C., Mirzabekov, T., and Kagan, B. L. (1997) Channel formation by a neurotoxic prion protein fragment. J. Biol. Chem. 272, 44-47 (Pubitemid 27021122)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.1 , pp. 44-47
    • Lin, M.-C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 15
    • 34248994582 scopus 로고    scopus 로고
    • PrP106-126 amide causes the semi-penetrated poration in the supported lipid bilayers
    • DOI 10.1016/j.bbamem.2007.03.003, PII S0005273607000752
    • Zhong, J., Zheng, W., Huang, L., Hong, Y., Wang, L., Qiu, Y., and Sha, Y. (2007) PrP106-126 amide causes the semi-penetrated poration in the supported lipid bilayers. Biochim. Biophys. Acta 1768, 1420-1429 (Pubitemid 46795477)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.6 , pp. 1420-1429
    • Zhong, J.1    Zheng, W.2    Huang, L.3    Hong, Y.4    Wang, L.5    Qiu, Y.6    Sha, Y.7
  • 16
    • 50349090857 scopus 로고    scopus 로고
    • PrP(106-126) does not interact with membranes under physiological conditions
    • Henriques, S. T., Pattenden, L. K., Aguilar, M. I., and Castanho, M. A. (2008) PrP(106-126) does not interact with membranes under physiological conditions. Biophys. J. 95, 1877-1889
    • (2008) Biophys. J. , vol.95 , pp. 1877-1889
    • Henriques, S.T.1    Pattenden, L.K.2    Aguilar, M.I.3    Castanho, M.A.4
  • 18
    • 18944361896 scopus 로고    scopus 로고
    • Environmental factors that enhance the action of the cell penetrating peptide pep-1: A spectroscopic study using lipidic vesicles
    • DOI 10.1016/j.bbamem.2004.11.017, PII S0005273605000544
    • Henriques, S. T., and Castanho,M.A. (2005) Environmental factors that enhance the action of the cell penetrating peptide pep-1 A spectroscopic study using lipidic vesicles. Biochim. Biophys. Acta 1669, 75-86. (Pubitemid 40704724)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1669 , Issue.2 , pp. 75-86
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 19
    • 0029738097 scopus 로고    scopus 로고
    • Teaching light scattering spectroscopy: The dimension and shape of tobacco mosaic virus
    • Santos, N. C., and Castanho,M. A. (1996) Teaching light scattering spectroscopy: The dimension and shape of tobacco mosaic virus. Biophys. J. 71, 1641-1650
    • (1996) Biophys. J. , vol.71 , pp. 1641-1650
    • Santos, N.C.1    Castanho, M.A.2
  • 21
    • 0038392423 scopus 로고    scopus 로고
    • Quantifying molecular partition into model systems of biomembranes: An emphasis on optical spectroscopic methods
    • DOI 10.1016/S0005-2736(03)00112-3
    • Santos, N. C., Prieto, M., and Castanho, M. A. (2003) Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods. Biochim. Biophys. Acta 1612, 123-135 (Pubitemid 36629567)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1612 , Issue.2 , pp. 123-135
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.R.B.3
  • 23
    • 0031958516 scopus 로고    scopus 로고
    • Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide
    • Cladera, J., and O'Shea, P. (1998) Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide. Biophys. J. 74, 2434-2442
    • (1998) Biophys. J. , vol.74 , pp. 2434-2442
    • Cladera, J.1    O'Shea, P.2
  • 24
    • 0034746677 scopus 로고    scopus 로고
    • The dipole potential of phospholipid membranes and methods for its detection
    • Clarke, R. J. (2001) The dipole potential of phospholipid membranes and methods for its detection. Adv. Colloid Interface Sci. 89-90, 263-281
    • (2001) Adv. Colloid Interface Sci. , vol.89-90 , pp. 263-281
    • Clarke, R.J.1
  • 25
    • 0032974758 scopus 로고    scopus 로고
    • Effect of gramicidin A on the dipole potential of phospholipid membranes
    • Shapovalov, V. L., Kotova, E.A., Rokitskaya, T. I., and Antonenko, Y. N. (1999) Effect of gramicidin A on the dipole potential of phospholipid membranes. Biophys. J. 77, 299-305.
    • (1999) Biophys. J. , vol.77 , pp. 299-305
    • Shapovalov, V.L.1    Kotova, E.A.2    Rokitskaya, T.I.3    Antonenko, Y.N.4
  • 26
    • 3343017389 scopus 로고    scopus 로고
    • Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles
    • DOI 10.1021/bi036325k
    • Henriques, S. T., and Castanho, M. A. (2004) Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide pep-1 in lipidic vesicles. Biochemistry 43, 9716-9724 (Pubitemid 38993821)
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9716-9724
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 27
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • DOI 10.1016/S0968-0004(00)01626-1, PII S0968000400016261
    • Killian, J. A., and von Heijne, G. (2000) How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25, 429-434 (Pubitemid 30662410)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.9 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 28
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • DOI 10.1016/j.bbamem.2004.08.004, PII S0005273604002056, Lipid-Protein Interactions
    • Seelig, J. (2004) Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 1666, 40-50. (Pubitemid 39425197)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 40-50
    • Seelig, J.1
  • 29
    • 0035715969 scopus 로고    scopus 로고
    • Measurement of the affinity of melittin for zwitterionic and anionic membranes using immobilized lipid biosensors
    • DOI 10.1034/j.1399-3011.2001.10974.x
    • Lee, T. H., Mozsolits, H., and Aguilar, M. I. (2001) Measurement of the affinity of melittin for zwitterionic and anionic membranes using immobilized lipid biosensors. J. Pept. Res. 58, 464-476 (Pubitemid 34169374)
    • (2001) Journal of Peptide Research , vol.58 , Issue.6 , pp. 464-476
    • Lee, T.-H.1    Mozsolits, H.2    Aguilar, M.-I.3
  • 30
    • 0037129950 scopus 로고    scopus 로고
    • 1a) carboxyl terminus to anionic lipids
    • DOI 10.1021/bi0121813
    • Mozsolits, H., Unabia, S., Ahmad, A., Morton, C. J., Thomas, W. G., and Aguilar, M. I. (2002) Electrostatic and hydrophobic forces tether the proximal region of the angiotensin II receptor (AT1A) carboxyl terminus to anionic lipids. Biochemistry 41, 7830-7840 (Pubitemid 34627810)
    • (2002) Biochemistry , vol.41 , Issue.24 , pp. 7830-7840
    • Mozsolits, H.1    Unabia, S.2    Ahmad, A.3    Morton, C.J.4    Thomas, W.G.5    Aguilar, M.-I.6
  • 31
    • 0035795730 scopus 로고    scopus 로고
    • Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance
    • DOI 10.1016/S0005-2736(01)00303-0, PII S0005273601003030
    • Mozsolits, H., Wirth, H. J., Werkmeister, J., and Aguilar, M. I. (2001) Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. Biochim. Biophys. Acta 1512, 64-76. (Pubitemid 32381023)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.1 , pp. 64-76
    • Mozsolits, H.1    Wirth, H.-J.2    Werkmeister, J.3    Aguilar, M.-I.4
  • 32
    • 50349090857 scopus 로고    scopus 로고
    • PrP(106-126) does not interact with membranes in physiological conditions
    • submitted for publication
    • Henriques, S. T., Pattenden, L. K., Aguilar, M. I., and Castanho, M. A. R. B. ((2008) ) PrP(106-126) does not interact with membranes in physiological conditions. Biophys. J., submitted for publication.
    • (2008) Biophys. J.
    • Henriques, S.T.1    Pattenden, L.K.2    Aguilar, M.I.3    Castanho, M.A.R.B.4
  • 33
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • DOI 10.1016/S0304-4157(98)00021-5, PII S0304415798000215
    • White, S. H., and Wimley, W. C. (1998) Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta 1376, 339-352 (Pubitemid 28517884)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 34
    • 8844228894 scopus 로고    scopus 로고
    • HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers. Putative correlation with improved efficiency
    • Veiga, A. S., Santos, N. C., Loura, L. M., Fedorov, A., and Castanho, M. A. (2004) HIV fusion inhibitor peptide T-1249 is able to insert or adsorb to lipidic bilayers. Putative correlation with improved efficiency. J. Am. Chem. Soc. 126, 14758-14763
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14758-14763
    • Veiga, A.S.1    Santos, N.C.2    Loura, L.M.3    Fedorov, A.4    Castanho, M.A.5
  • 35
    • 34047249400 scopus 로고    scopus 로고
    • Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation
    • Melo, M. N., and Castanho, M. A. (2007) Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation. Biochim. Biophys. Acta 1768, 1277-1290
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1277-1290
    • Melo, M.N.1    Castanho, M.A.2
  • 36
    • 33744925900 scopus 로고    scopus 로고
    • Prion disease: Exponential growth requires membrane binding
    • Cox, D. L., Sing, R. R., and Yang, S. (2006) Prion disease: Exponential growth requires membrane binding. Biophys. J. 90, L77-9.
    • (2006) Biophys. J. , vol.90
    • Cox, D.L.1    Sing, R.R.2    Yang, S.3
  • 38
    • 0035950434 scopus 로고    scopus 로고
    • Mechanisms of prion-induced modifications in membrane transport properties: Implications for signal transduction and neurotoxicity
    • Kourie, J. I. (2001) Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicity. Chem. Biol. Interact. 138, 1-26.
    • (2001) Chem. Biol. Interact. , vol.138 , pp. 1-26
    • Kourie, J.I.1
  • 39
    • 35348849675 scopus 로고    scopus 로고
    • Clustered negative charges on the lipid membrane surface induce β-sheet formation of prion protein fragment 106-126
    • DOI 10.1021/bi700939j
    • Miura, T., Yoda, M., Takaku, N., Hirose, T., and Takeuchi, H. (2007) Clustered negative charges on the lipid membrane surface induce beta-sheet formation of prion protein fragment 106-126. Biochemistry 46, 11589-11597 (Pubitemid 47585504)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11589-11597
    • Miura, T.1    Yoda, M.2    Takaku, N.3    Hirose, T.4    Takeuchi, H.5
  • 41
    • 0032859326 scopus 로고    scopus 로고
    • Neurotoxicity of prion peptide 106-126 not confirmed
    • DOI 10.1016/S0014-5793(99)01123-0, PII S0014579399011230
    • Kunz, B., Sandmeier, E., and Christen, P. (1999) Neurotoxicity of prion peptide 106-126 not confirmed. FEBS Lett. 458, 65-68 (Pubitemid 29415673)
    • (1999) FEBS Letters , vol.458 , Issue.1 , pp. 65-68
    • Kunz, B.1    Sandmeier, E.2    Christen, P.3
  • 42
    • 0034595577 scopus 로고    scopus 로고
    • Reported channel formation by prion protein fragment 106-126 in planar lipid bilayers cannot be reproduced [2]
    • DOI 10.1016/S0014-5793(00)01603-3, PII S0014579300016033
    • Manunta, M., Kunz, B., Sandmeier, E., Christen, P., and Schindler, H. (2000) Reported channel formation by prion protein fragment 106-126 in planar lipid bilayers cannot be reproduced. FEBS Lett. 474, 255-256 (Pubitemid 30330845)
    • (2000) FEBS Letters , vol.474 , Issue.2-3 , pp. 255-256
    • Manunta, M.1    Kunz, B.2    Sandmeier, E.3    Christen, P.4    Schindler, H.5
  • 43
    • 0042572540 scopus 로고    scopus 로고
    • Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides
    • DOI 10.1021/bi034338s
    • Jin, Y., Mozsolits, H., Hammer, J., Zmuda, E., Zhu, F., Zhang, Y., Aguilar, M. I., and Blazyk, J. (2003) Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides. Biochemistry 42, 9395-9405 (Pubitemid 36959247)
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9395-9405
    • Jin, Y.1    Mozsolits, H.2    Hammer, J.3    Zmuda, E.4    Zhu, F.5    Zhang, Y.6    Aguilar, M.I.7    Blazyk, J.8
  • 44
  • 45
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid β-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • DOI 10.1021/bi0255874
    • Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., and Matsuzaki, K. (2002) Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 41, 7385-7390 (Pubitemid 34602456)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.-I.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 47
    • 33645290776 scopus 로고    scopus 로고
    • The prion protein and lipid rafts
    • Taylor, D. R., and Hooper, N. M. (2006) The prion protein and lipid rafts. Mol. Membr. Biol. 23, 89-99.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 89-99
    • Taylor, D.R.1    Hooper, N.M.2
  • 48
    • 4344632252 scopus 로고    scopus 로고
    • PrP(C) association with lipid rafts in the early secretory pathway stabilizes its cellular conformation
    • Sarnataro, D., Campana, V., Paladino, S., Stornaiuolo, M., Nitsch, L., and Zurzolo, C. (2004) PrP(C) association with lipid rafts in the early secretory pathway stabilizes its cellular conformation. Mol. Biol. Cell 15, 4031-4042
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4031-4042
    • Sarnataro, D.1    Campana, V.2    Paladino, S.3    Stornaiuolo, M.4    Nitsch, L.5    Zurzolo, C.6
  • 49
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M. N., Ferre, R., and Castanho, M. A. (2009) Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7, 245-250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3


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