메뉴 건너뛰기




Volumn 20, Issue 8, 2016, Pages 1443-1456

Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2-microglobulin

Author keywords

amyloid cytotoxicity; GM1 ganglioside; membrane bilayers; protein misfolding; systemic amyloidosis

Indexed keywords

AMYLOID PROTEIN; BETA 2 MICROGLOBULIN; CONGO RED; GANGLIOSIDE GM1; QUANTUM DOT; REACTIVE OXYGEN METABOLITE; THIOFLAVINE;

EID: 84979086201     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/jcmm.12833     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0034864986 scopus 로고    scopus 로고
    • Distinct differences in association of MHC class I with endoplasmic reticulum proteins in wild-type, and beta 2-microglobulin- and TAP-deficient cell lines
    • Paulsson KM, Wang P, Anderson PO, et al. Distinct differences in association of MHC class I with endoplasmic reticulum proteins in wild-type, and beta 2-microglobulin- and TAP-deficient cell lines. Int Immunol. 2001; 13: 1063–73.
    • (2001) Int Immunol , vol.13 , pp. 1063-1073
    • Paulsson, K.M.1    Wang, P.2    Anderson, P.O.3
  • 2
    • 0011039325 scopus 로고
    • Three-dimensional structure of beta 2-microglobulin
    • Becker JW, Reeke GN Jr. Three-dimensional structure of beta 2-microglobulin. Proc Natl Acad Sci USA. 1985; 82: 4225–9.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4225-4229
    • Becker, J.W.1    Reeke, G.N.2
  • 3
    • 80053596817 scopus 로고    scopus 로고
    • Understanding the complex mechanisms of beta2-microglobulin amyloid assembly
    • Eichner T, Radford SE. Understanding the complex mechanisms of beta2-microglobulin amyloid assembly. FEBS J. 2011; 278: 3868–83.
    • (2011) FEBS J , vol.278 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 4
    • 84862198496 scopus 로고    scopus 로고
    • Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin
    • Valleix S, Gillmore JD, Bridoux F, et al. Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin. N Engl J Med. 2012; 366: 2276–83.
    • (2012) N Engl J Med , vol.366 , pp. 2276-2283
    • Valleix, S.1    Gillmore, J.D.2    Bridoux, F.3
  • 5
    • 51349128031 scopus 로고    scopus 로고
    • A regulatable switch mediates self-association in an immunoglobulin fold
    • Calabrese MF, Eakin CM, Wang JM, et al. A regulatable switch mediates self-association in an immunoglobulin fold. Nat Struct Mol Biol. 2008; 15: 965–71.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 965-971
    • Calabrese, M.F.1    Eakin, C.M.2    Wang, J.M.3
  • 6
    • 66749133376 scopus 로고    scopus 로고
    • Metal binding sheds light on mechanisms of amyloid assembly
    • Calabrese MF, Miranker AD. Metal binding sheds light on mechanisms of amyloid assembly. Prion. 2009; 3: 1–4.
    • (2009) Prion , vol.3 , pp. 1-4
    • Calabrese, M.F.1    Miranker, A.D.2
  • 7
    • 33745224979 scopus 로고    scopus 로고
    • Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosis
    • Relini A, Canale C, De Stefano S, et al. Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J Biol Chem. 2006; 281: 16521–9.
    • (2006) J Biol Chem , vol.281 , pp. 16521-16529
    • Relini, A.1    Canale, C.2    De Stefano, S.3
  • 8
    • 0346103697 scopus 로고    scopus 로고
    • Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S, Yamaguchi I, Hasegawa K, et al. Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. J Am Soc Nephrol. 2004; 15: 126–33.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 126-133
    • Yamamoto, S.1    Yamaguchi, I.2    Hasegawa, K.3
  • 9
    • 33144471714 scopus 로고    scopus 로고
    • A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH
    • Myers SL, Jones S, Jahn TR, et al. A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH. Biochemistry. 2006; 45: 2311–21.
    • (2006) Biochemistry , vol.45 , pp. 2311-2321
    • Myers, S.L.1    Jones, S.2    Jahn, T.R.3
  • 10
    • 84886655678 scopus 로고    scopus 로고
    • Structure, folding dynamics, and amyloidogenesis of D76N beta2-microglobulin: roles of shear flow, hydrophobic surfaces, and alpha-crystallin
    • Mangione PP, Esposito G, Relini A, et al. Structure, folding dynamics, and amyloidogenesis of D76N beta2-microglobulin: roles of shear flow, hydrophobic surfaces, and alpha-crystallin. J Biol Chem. 2013; 288: 30917–30.
    • (2013) J Biol Chem , vol.288 , pp. 30917-30930
    • Mangione, P.P.1    Esposito, G.2    Relini, A.3
  • 11
    • 84890285330 scopus 로고    scopus 로고
    • Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate beta2-microglobulin amyloid assembly
    • Torbeev VY, Hilvert D. Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate beta2-microglobulin amyloid assembly. Proc Natl Acad Sci USA. 2013; 110: 20051–6.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 20051-20056
    • Torbeev, V.Y.1    Hilvert, D.2
  • 12
    • 60949106895 scopus 로고    scopus 로고
    • A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch
    • Eichner T, Radford SE. A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. J Mol Biol. 2009; 386: 1312–26.
    • (2009) J Mol Biol , vol.386 , pp. 1312-1326
    • Eichner, T.1    Radford, S.E.2
  • 13
    • 77951645923 scopus 로고    scopus 로고
    • Sequence determinants of compaction in intrinsically disordered proteins
    • Marsh JA, Forman-Kay JD. Sequence determinants of compaction in intrinsically disordered proteins. Biophys J. 2010; 98: 2383–90.
    • (2010) Biophys J , vol.98 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 14
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L, Khurana R, Coats A, et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 2001; 40: 6036–46.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3
  • 15
    • 0037112480 scopus 로고    scopus 로고
    • Functional expression of the hyperpolarization-activated, non-selective cation current I(f) in immortalized HL-1 cardiomyocytes
    • Sartiani L, Bochet P, Cerbai E, et al. Functional expression of the hyperpolarization-activated, non-selective cation current I(f) in immortalized HL-1 cardiomyocytes. J Physiol. 2002; 545: 81–92.
    • (2002) J Physiol , vol.545 , pp. 81-92
    • Sartiani, L.1    Bochet, P.2    Cerbai, E.3
  • 16
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods. 1983; 65: 55–63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 17
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli IY, Prager K, Barth E, et al. Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J Biol Chem. 2005; 280: 28110–7.
    • (2005) J Biol Chem , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1    Prager, K.2    Barth, E.3
  • 18
    • 34250184742 scopus 로고    scopus 로고
    • Imaging the lateral diffusion of membrane molecules with quantum dots
    • Bannai H, Levi S, Schweizer C, et al. Imaging the lateral diffusion of membrane molecules with quantum dots. Nat Protoc. 2006; 1: 2628–34.
    • (2006) Nat Protoc , vol.1 , pp. 2628-2634
    • Bannai, H.1    Levi, S.2    Schweizer, C.3
  • 19
    • 26444459812 scopus 로고    scopus 로고
    • Single quantum dot tracking based on perceptual grouping using minimal paths in a spatiotemporal volume
    • Bonneau S, Dahan M, Cohen LD. Single quantum dot tracking based on perceptual grouping using minimal paths in a spatiotemporal volume. IEEE Trans Image Process. 2005; 14: 1384–95.
    • (2005) IEEE Trans Image Process , vol.14 , pp. 1384-1395
    • Bonneau, S.1    Dahan, M.2    Cohen, L.D.3
  • 20
    • 34247857560 scopus 로고    scopus 로고
    • Multiple association states between glycine receptors and gephyrin identified by SPT analysis
    • Ehrensperger MV, Hanus C, Vannier C, et al. Multiple association states between glycine receptors and gephyrin identified by SPT analysis. Biophys J. 2007; 92: 3706–18.
    • (2007) Biophys J , vol.92 , pp. 3706-3718
    • Ehrensperger, M.V.1    Hanus, C.2    Vannier, C.3
  • 21
    • 48249097851 scopus 로고    scopus 로고
    • Plasma membranes are poised for activation of raft phase coalescence at physiological temperature
    • Lingwood D, Ries J, Schwille P, et al. Plasma membranes are poised for activation of raft phase coalescence at physiological temperature. Proc Natl Acad Sci USA. 2008; 105: 10005–10.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10005-10010
    • Lingwood, D.1    Ries, J.2    Schwille, P.3
  • 22
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: applications to membrane dynamics
    • Saxton MJ, Jacobson K. Single-particle tracking: applications to membrane dynamics. Annu Rev Biophys Biomol Struct. 1997; 26: 373–99.
    • (1997) Annu Rev Biophys Biomol Struct , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 23
    • 65349160016 scopus 로고    scopus 로고
    • beta2-Microglobulin is potentially neurotoxic, but the blood brain barrier is likely to protect the brain from its toxicity
    • Giorgetti S, Raimondi S, Cassinelli S, et al. beta2-Microglobulin is potentially neurotoxic, but the blood brain barrier is likely to protect the brain from its toxicity. Nephrol Dial Transplant. 2009; 24: 1176–81.
    • (2009) Nephrol Dial Transplant , vol.24 , pp. 1176-1181
    • Giorgetti, S.1    Raimondi, S.2    Cassinelli, S.3
  • 24
    • 14644435012 scopus 로고    scopus 로고
    • Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates
    • Bucciantini M, Rigacci S, Berti A, et al. Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. FASEB J. 2005; 19: 437–59.
    • (2005) FASEB J , vol.19 , pp. 437-459
    • Bucciantini, M.1    Rigacci, S.2    Berti, A.3
  • 25
    • 84864810728 scopus 로고    scopus 로고
    • Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers
    • Evangelisti E, Cecchi C, Cascella R, et al. Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers. J Cell Sci. 2012; 125: 2416–27.
    • (2012) J Cell Sci , vol.125 , pp. 2416-2427
    • Evangelisti, E.1    Cecchi, C.2    Cascella, R.3
  • 26
    • 84899068704 scopus 로고    scopus 로고
    • Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes
    • Hong S, Ostaszewski BL, Yang T, et al. Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes. Neuron. 2014; 82: 308–19.
    • (2014) Neuron , vol.82 , pp. 308-319
    • Hong, S.1    Ostaszewski, B.L.2    Yang, T.3
  • 27
    • 84856545963 scopus 로고    scopus 로고
    • Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1
    • Bucciantini M, Nosi D, Forzan M, et al. Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1. FASEB J. 2012; 26: 818–31.
    • (2012) FASEB J , vol.26 , pp. 818-831
    • Bucciantini, M.1    Nosi, D.2    Forzan, M.3
  • 28
    • 84876472619 scopus 로고    scopus 로고
    • Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates
    • Calamai M, Pavone FS. Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates. FEBS Lett. 2013; 587: 1385–91.
    • (2013) FEBS Lett , vol.587 , pp. 1385-1391
    • Calamai, M.1    Pavone, F.S.2
  • 29
    • 79952021123 scopus 로고    scopus 로고
    • Biological membranes as protein aggregation matrices and targets of amyloid toxicity
    • Bucciantini M, Cecchi C. Biological membranes as protein aggregation matrices and targets of amyloid toxicity. Methods Mol Biol. 2010; 648: 231–43.
    • (2010) Methods Mol Biol , vol.648 , pp. 231-243
    • Bucciantini, M.1    Cecchi, C.2
  • 30
    • 1642334714 scopus 로고    scopus 로고
    • Membrane properties of binary and ternary systems of ganglioside GM1/dipalmitoylphosphatidylcholine/dioleoylphosphatidylcholine
    • Ohtaa Y, Yokoyama S, Sakaia H, et al. Membrane properties of binary and ternary systems of ganglioside GM1/dipalmitoylphosphatidylcholine/dioleoylphosphatidylcholine. Colloids Surf B. 2004; 34: 147–53.
    • (2004) Colloids Surf B , vol.34 , pp. 147-153
    • Ohtaa, Y.1    Yokoyama, S.2    Sakaia, H.3
  • 31
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding TT, Lee SJ, Rochet JC, et al. Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry. 2002; 41: 10209–17.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3
  • 32
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol. 2007; 8: 101–12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 33
    • 78751560834 scopus 로고    scopus 로고
    • Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils
    • Giorgetti S, Raimondi S, Pagano K, et al. Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils. J Biol Chem. 2011; 286: 2121–31.
    • (2011) J Biol Chem , vol.286 , pp. 2121-2131
    • Giorgetti, S.1    Raimondi, S.2    Pagano, K.3
  • 34
    • 71749089460 scopus 로고    scopus 로고
    • Fibril fragmentation enhances amyloid cytotoxicity
    • Xue WF, Hellewell AL, Gosal WS, et al. Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem. 2009; 284: 34272–82.
    • (2009) J Biol Chem , vol.284 , pp. 34272-34282
    • Xue, W.F.1    Hellewell, A.L.2    Gosal, W.S.3
  • 35
    • 77949278013 scopus 로고    scopus 로고
    • Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters
    • Xue WF, Hellewell AL, Hewitt EW, et al. Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters. Prion. 2010; 4: 20–5.
    • (2010) Prion , vol.4 , pp. 20-25
    • Xue, W.F.1    Hellewell, A.L.2    Hewitt, E.W.3
  • 36
    • 84870947924 scopus 로고    scopus 로고
    • Direct three-dimensional visualization of membrane disruption by amyloid fibrils
    • Milanesi L, Sheynis T, Xue WF, et al. Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proc Natl Acad Sci USA. 2012; 109: 20455–60.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 20455-20460
    • Milanesi, L.1    Sheynis, T.2    Xue, W.F.3
  • 37
    • 33846023647 scopus 로고    scopus 로고
    • Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways
    • Gharibyan AL, Zamotin V, Yanamandra K, et al. Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. J Mol Biol. 2007; 365: 1337–49.
    • (2007) J Mol Biol , vol.365 , pp. 1337-1349
    • Gharibyan, A.L.1    Zamotin, V.2    Yanamandra, K.3
  • 38
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V, Bocharova OV, Bronstein I, et al. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem. 2006; 281: 13828–36.
    • (2006) J Biol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3
  • 39
    • 84893463530 scopus 로고    scopus 로고
    • Polymorphism of hen egg white lysozyme amyloid fibrils influences the cytotoxicity in LLC-PK1 epithelial kidney cells
    • Mocanu MM, Ganea C, Siposova K, et al. Polymorphism of hen egg white lysozyme amyloid fibrils influences the cytotoxicity in LLC-PK1 epithelial kidney cells. Int J Biol Macromol. 2014; 65: 176–87.
    • (2014) Int J Biol Macromol , vol.65 , pp. 176-187
    • Mocanu, M.M.1    Ganea, C.2    Siposova, K.3
  • 40
    • 20944450871 scopus 로고    scopus 로고
    • Raft lipids as common components of human extracellular amyloid fibrils
    • Gellermann GP, Appel TR, Tannert A, et al. Raft lipids as common components of human extracellular amyloid fibrils. Proc Natl Acad Sci USA. 2005; 102: 6297–302.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6297-6302
    • Gellermann, G.P.1    Appel, T.R.2    Tannert, A.3
  • 41
    • 69249209894 scopus 로고    scopus 로고
    • Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts
    • Wakabayashi M, Matsuzaki K. Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts. FEBS Lett. 2009; 583: 2854–8.
    • (2009) FEBS Lett , vol.583 , pp. 2854-2858
    • Wakabayashi, M.1    Matsuzaki, K.2
  • 42
    • 84864810728 scopus 로고    scopus 로고
    • Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers
    • Stefani M. Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers. J Cell Sci. 2012; 125: 2416–27.
    • (2012) J Cell Sci , vol.125 , pp. 2416-2427
    • Stefani, M.1
  • 43
    • 80052273046 scopus 로고    scopus 로고
    • Nanoscale structural and mechanical effects of beta-amyloid (1-42) on polymer cushioned membranes: a combined study by neutron reflectometry and AFM Force Spectroscopy
    • Dante S, Hauss T, Steitz R, et al. Nanoscale structural and mechanical effects of beta-amyloid (1-42) on polymer cushioned membranes: a combined study by neutron reflectometry and AFM Force Spectroscopy. BBA-Biomembranes. 2011; 1808: 2646–55.
    • (2011) BBA-Biomembranes , vol.1808 , pp. 2646-2655
    • Dante, S.1    Hauss, T.2    Steitz, R.3
  • 44
    • 84912536014 scopus 로고    scopus 로고
    • Cholesterol drives Aβ(1–42) interaction with lipid rafts in model membranes
    • Seghezza S, Diaspro A, Canale C, et al. Cholesterol drives Aβ(1–42) interaction with lipid rafts in model membranes. Langmuir. 2014; 30: 13934–41.
    • (2014) Langmuir , vol.30 , pp. 13934-13941
    • Seghezza, S.1    Diaspro, A.2    Canale, C.3
  • 45
    • 84855416611 scopus 로고    scopus 로고
    • Direct measurement of the mechanical properties of lipid phases in supported bilayers
    • Picas L, Rico F, Scheuring S. Direct measurement of the mechanical properties of lipid phases in supported bilayers. Biophys J. 2012; 102: L01–3.
    • (2012) Biophys J , vol.102 , pp. L01-3
    • Picas, L.1    Rico, F.2    Scheuring, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.