메뉴 건너뛰기




Volumn 44, Issue 25, 2005, Pages 9265-9274

Kinetic stabilization of an oligomeric protein under physiological conditions demonstrated by a lack of subunit exchange: Implications for transthyretin amyloidosis

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; ASSAYS; DISEASES; DISSOCIATION; OLIGOMERS; PHYSIOLOGY; REACTION KINETICS;

EID: 21744452155     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050352o     Document Type: Article
Times cited : (56)

References (38)
  • 1
    • 0034799733 scopus 로고    scopus 로고
    • Transthyretin: A review from a structural perspective
    • Hamilton, J. A., and Benson, M. D. (2001) Transthyretin: a review from a structural perspective, Cell Mol. Life Sci. 58, 1491-1521.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1491-1521
    • Hamilton, J.A.1    Benson, M.D.2
  • 3
    • 0038661338 scopus 로고    scopus 로고
    • D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: A prescription for central nervous system amyloidosis?
    • Hammarstrom, P., Sekijima, Y., White, J. T., Wiseman, R. L., Lim, A., Costello, C. E., Altland, K., Garzuly, F., Budka, H., and Kelly, J. W. (2003) D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? Biochemistry 42, 6656-6663.
    • (2003) Biochemistry , vol.42 , pp. 6656-6663
    • Hammarstrom, P.1    Sekijima, Y.2    White, J.T.3    Wiseman, R.L.4    Lim, A.5    Costello, C.E.6    Altland, K.7    Garzuly, F.8    Budka, H.9    Kelly, J.W.10
  • 4
    • 0344074661 scopus 로고    scopus 로고
    • Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy
    • Plante-Bordeneuve, V., Lalu, T., Misrahi, M., Reilly, M. M., Adams, D., Lacroix, C., and Said, G. (1998) Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy, Neurology 51, 708-714.
    • (1998) Neurology , vol.51 , pp. 708-714
    • Plante-Bordeneuve, V.1    Lalu, T.2    Misrahi, M.3    Reilly, M.M.4    Adams, D.5    Lacroix, C.6    Said, G.7
  • 5
    • 0026612659 scopus 로고
    • Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement
    • Jacobson, D. R., McFarlin, D. E., Kane, I., and Buxbaum, J. N. (1992) Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement, Hum. Genet. 89, 353-356.
    • (1992) Hum. Genet. , vol.89 , pp. 353-356
    • Jacobson, D.R.1    McFarlin, D.E.2    Kane, I.3    Buxbaum, J.N.4
  • 7
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva, M. J. (1995) Transthyretin mutations in health and disease, Hum. Mutat. 5, 191-196.
    • (1995) Hum. Mutat. , vol.5 , pp. 191-196
    • Saraiva, M.J.1
  • 9
    • 0036713015 scopus 로고    scopus 로고
    • Long-term follow-up of survival of liver transplant recipients with familial amyloid polyneuropathy (Portuguese type)
    • Suhr, O. B., Ericzon, B. G., and Friman, S. (2002) Long-term follow-up of survival of liver transplant recipients with familial amyloid polyneuropathy (Portuguese type), Liver Transpl. 8, 787-794.
    • (2002) Liver Transpl. , vol.8 , pp. 787-794
    • Suhr, O.B.1    Ericzon, B.G.2    Friman, S.3
  • 11
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom, P., Jiang, X., Hurshman, A. R., Powers, E. T., and Kelly, J. W. (2002) Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity, Proc. Natl. Acad. Sci., U.S.A. 99, 16427-16432.
    • (2002) Proc. Natl. Acad. Sci., U.S.A. , vol.99 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 12
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon, W., and Kelly, J. W. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro, Biochemistry 31, 8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 13
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai, Z., Colon, W., and Kelly, J. W. (1996) The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid, Biochemistry 35, 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 14
    • 0001189971 scopus 로고
    • A strikingly benign evolution of FAP in an individual compound heterozygote for Two TTR mutations: TTR Met30 and TTR Met119
    • Coelho, T., Carvalho, M., Saraiva, M. J., et al. (1993) A Strikingly Benign Evolution of FAP in an Individual Compound Heterozygote for Two TTR Mutations: TTR Met30 and TTR Met119, J. Rheumatol. 20, 179.
    • (1993) J. Rheumatol. , vol.20 , pp. 179
    • Coelho, T.1    Carvalho, M.2    Saraiva, M.J.3
  • 15
    • 0035964955 scopus 로고    scopus 로고
    • Transsuppression of misfolding in an amyloid disease
    • Hammarstrom, P., Schneider, F., and Kelly, J. W. (2001) Transsuppression of misfolding in an amyloid disease. Science 293, 2459-2462.
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 16
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarstrom, P., Wiseman, R. L., Powers, E. T., and Kelly, J. W. (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics, Science 299, 713-716.
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 17
    • 0242299247 scopus 로고    scopus 로고
    • Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization
    • Green, N. S., Palaninathan, S. K., Sacchettini, J. C., and Kelly, J. W. (2003) Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization, J. Am. Chem. Soc. 125, 13404-13414.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13404-13414
    • Green, N.S.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 18
    • 0346333094 scopus 로고    scopus 로고
    • Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis
    • Adamski-Werner, S. L., Palaninathan, S. K., Sacchettini, J. C., and Kelly, J. W. (2004) Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis, J. Med. Chem. 47, 355-374.
    • (2004) J. Med. Chem. , vol.47 , pp. 355-374
    • Adamski-Werner, S.L.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 22
    • 10644265785 scopus 로고    scopus 로고
    • Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: Rationalizing rodent PCB toxicity
    • Purkey, H. E., Palaninathan, S. K., Kent, K. C., Smith, C., Safe, S. H., Sacchettini, J. C., and Kelly, J. W. (2004) Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: rationalizing rodent PCB toxicity, Chem. Biol. 11, 1719-1728.
    • (2004) Chem. Biol. , vol.11 , pp. 1719-1728
    • Purkey, H.E.1    Palaninathan, S.K.2    Kent, K.C.3    Smith, C.4    Safe, S.H.5    Sacchettini, J.C.6    Kelly, J.W.7
  • 24
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach, N., Deechongkit, S., Jiang, X., Kelly, J. W., and Buxbaum, J. N. (2004) Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture, Proc. Natl. Acad. Sci., U.S.A. 101, 2817-2822.
    • (2004) Proc. Natl. Acad. Sci., U.S.A. , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 25
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • Sousa, M. M., Cardoso, I., Fernandes, R., Guimaraes, A., and Saraiva, M. J. (2001) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates, Am. J. Pathol. 159, 1993-2000.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 26
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel, H. A., Lai, Z., and Kelly, J. W. (1998) Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation, Biochemistry 37, 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 27
    • 0033857583 scopus 로고    scopus 로고
    • Review: TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies
    • Damas, A. M., and Saraiva, M. J. (2000) Review: TTR amyloidosis- structural features leading to protein aggregation and their implications on therapeutic strategies, J. Struct. Biol. 130, 290-299.
    • (2000) J. Struct. Biol. , vol.130 , pp. 290-299
    • Damas, A.M.1    Saraiva, M.J.2
  • 28
    • 0034919395 scopus 로고    scopus 로고
    • Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins
    • Schneider, F., Hammarstrom, P., and Kelly, J. W. (2001) Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins, Protein Sci. 10, 1606-1613.
    • (2001) Protein Sci. , vol.10 , pp. 1606-1613
    • Schneider, F.1    Hammarstrom, P.2    Kelly, J.W.3
  • 29
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • Lashuel, H. A., Wurth, C., Woo, L., and Kelly, J. W. (1999) The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions, Biochemistry 38, 13560-13573.
    • (1999) Biochemistry , vol.38 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 31
    • 14944368141 scopus 로고    scopus 로고
    • Kinetic stabilization of the native state by protein engineering: Implications of transthyretin amyloidogenesis
    • Foss, T. R., Kelker, M. S., Wiseman, R. L., Wilson, I. A., and Kelly, J. W. (2005) Kinetic Stabilization of the Native State by Protein Engineering: Implications of Transthyretin Amyloidogenesis, J. Mol. Biol. 347, 841-854.
    • (2005) J. Mol. Biol. , vol.347 , pp. 841-854
    • Foss, T.R.1    Kelker, M.S.2    Wiseman, R.L.3    Wilson, I.A.4    Kelly, J.W.5
  • 32
  • 34
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt, S., and Freire, E. (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry, Curr. Opin. Struct. Biol. 11, 560-566.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 35
    • 0036277955 scopus 로고    scopus 로고
    • Screening transthyretin amyloid fibril inhibitors: Characterization of novel multiprotein, multiligand complexes by mass spectrometry
    • McCammon, M. G., Scott, D. J., Keetch, C. A., Greene, L. H., Purkey, H. E., Petrassi, H. M., Kelly, J. W., and Robinson, C. V. (2002) Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry, Structure 10, 851-863.
    • (2002) Structure , vol.10 , pp. 851-863
    • McCammon, M.G.1    Scott, D.J.2    Keetch, C.A.3    Greene, L.H.4    Purkey, H.E.5    Petrassi, H.M.6    Kelly, J.W.7    Robinson, C.V.8
  • 36
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • Sacchettini, J. C., and Kelly, J. W. (2002) Therapeutic strategies for human amyloid diseases, Nat. Rev. Drug Discovery 1, 267-275.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 37
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn, L. I., Miller, T. M., and Cleveland, D. W. (2004) Unraveling the mechanisms involved in motor neuron degeneration in ALS, Annu. Rev. Neurosci. 27, 723-749.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 38
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li, S. H., and Li, X. J. (2004) Huntingtin-protein interactions and the pathogenesis of Huntington's disease, Trends Genet. 20, 146-154.
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.