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Volumn 206, Issue 2, 2005, Pages 224-232

Amyloid deposits in transthyretin-derived amyloidosis: Cleaved transthyretin is associated with distinct amyloid morphology

Author keywords

Amyloidosis; Familial amyloid polyneuropathy; Senile systemic amyloidosis; Transthyretin

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; PREALBUMIN;

EID: 19944365557     PISSN: 00223417     EISSN: None     Source Type: Journal    
DOI: 10.1002/path.1759     Document Type: Article
Times cited : (195)

References (44)
  • 3
    • 0034637031 scopus 로고    scopus 로고
    • Cardiac amyloid in patients with familial amyloid polyneuropathy consists of abundant wild-type transthyretin
    • Yazaki M, Tokuda T, Nakamura A, et al. Cardiac amyloid in patients with familial amyloid polyneuropathy consists of abundant wild-type transthyretin. Biochem Biophys Res Commun 2000; 274: 702-706.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 702-706
    • Yazaki, M.1    Tokuda, T.2    Nakamura, A.3
  • 4
    • 0141815583 scopus 로고    scopus 로고
    • Contribution of wild-type transthyretin to hereditary peripheral nerve amyloid
    • Yazaki M, Liepnieks JJ, Kincaid JC, Benson MD. Contribution of wild-type transthyretin to hereditary peripheral nerve amyloid. Muscle Nerve 2003; 28: 438-442.
    • (2003) Muscle Nerve , vol.28 , pp. 438-442
    • Yazaki, M.1    Liepnieks, J.J.2    Kincaid, J.C.3    Benson, M.D.4
  • 8
    • 0020519870 scopus 로고
    • Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation
    • Cornwell GG 3rd, Murdoch WL, Kyle RA, Westermark P, Pitkänen P. Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation. Am J Med 1983; 75: 618-623.
    • (1983) Am. J. Med. , vol.75 , pp. 618-623
    • Cornwell III, G.G.1    Murdoch, W.L.2    Kyle, R.A.3    Westermark, P.4    Pitkänen, P.5
  • 9
    • 0025753077 scopus 로고
    • Senile systemic amyloidosis: A clinico-pathological study of twelve patients with massive amyloid infiltration
    • Johansson B, Westermark P. Senile systemic amyloidosis: a clinico-pathological study of twelve patients with massive amyloid infiltration. Int J Cardiol 1991; 32: 83-92.
    • (1991) Int. J. Cardiol. , vol.32 , pp. 83-92
    • Johansson, B.1    Westermark, P.2
  • 10
  • 12
    • 0020485070 scopus 로고
    • Cellular origin of prealbumin in the rat
    • Felding P, Fex G. Cellular origin of prealbumin in the rat. Biochim Biophys Acta 1982; 716: 446-449.
    • (1982) Biochim. Biophys. Acta , vol.716 , pp. 446-449
    • Felding, P.1    Fex, G.2
  • 14
    • 0022628925 scopus 로고
    • Transthyretin: A choroid plexus-specific transport protein in human brain. The 1986 S Weir Mitchell award
    • Herbert J, Wilcox JN, Pham KT, et al. Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S Weir Mitchell award. Neurology 1986; 36: 900-911.
    • (1986) Neurology , vol.36 , pp. 900-911
    • Herbert, J.1    Wilcox, J.N.2    Pham, K.T.3
  • 15
    • 0024599423 scopus 로고
    • In situ localization of transthyretin-mRNA in the adult human liver, choroid plexus and pancreatic islets and in endocrine tumors of the pancreas and gut
    • Jacobsson B. In situ localization of transthyretin-mRNA in the adult human liver, choroid plexus and pancreatic islets and in endocrine tumors of the pancreas and gut. Histochemistry 1989; 91: 299-304.
    • (1989) Histochemistry , vol.91 , pp. 299-304
    • Jacobsson, B.1
  • 16
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake CC, Geisow MJ, Oatley SJ, Rerat B, Rerat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 1978; 121: 339-356.
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 17
    • 0034602241 scopus 로고    scopus 로고
    • Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface
    • Liu K, Cho HS, Hoyt DW, et al. Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface. J Mol Biol 2000; 303: 555-565.
    • (2000) J. Mol. Biol. , vol.303 , pp. 555-565
    • Liu, K.1    Cho, H.S.2    Hoyt, D.W.3
  • 18
    • 0037907526 scopus 로고    scopus 로고
    • Why is Leu55 → Pro55 transthyretin variant the most amyloidogenic: Insights from molecular dynamics simulations of transthyretin monomers
    • Yang M, Lei M, Huo S. Why is Leu55 → Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomers. Protein Sci 2003; 12: 1222-1231.
    • (2003) Protein Sci. , vol.12 , pp. 1222-1231
    • Yang, M.1    Lei, M.2    Huo, S.3
  • 19
    • 0032725562 scopus 로고    scopus 로고
    • The tetrameric protein transthyretin dissociates to a non-native monomer in solution. A novel model for amyloidogenesis
    • Quintas A, Saraiva MJ, Brito RM. The tetrameric protein transthyretin dissociates to a non-native monomer in solution. A novel model for amyloidogenesis. J Biol Chem 1999; 274: 32 943-32 949.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32943-32949
    • Quintas, A.1    Saraiva, M.J.2    Brito, R.M.3
  • 20
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A, Vaz DC, Cardoso I, Saraiva MJ, Brito RM. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 2001; 276: 27 207-27 213.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 21
  • 22
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman AR, White JT, Powers ET, Kelly JW. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 2004; 43: 7365-7381.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 23
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • Jiang X, Buxbaum JN, Kelly JW. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci U S A 2001; 98: 14 943-14 948.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 24
    • 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, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 1996; 35: 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 25
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers
    • Lai Z, McCulloch J, Lashuel HA, Kelly JW. Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry 1997; 36: 10 230-10 239.
    • (1997) Biochemistry , vol.36 , pp. 10230-10239
    • Lai, Z.1    McCulloch, J.2    Lashuel, H.A.3    Kelly, J.W.4
  • 26
    • 0023696119 scopus 로고
    • Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin
    • Cornwell GG 3rd, Sletten K, Johansson B, Westermark P. Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem Biophys Res Commun 1988; 154: 648-653.
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 648-653
    • Cornwell III, G.G.1    Sletten, K.2    Johansson, B.3    Westermark, P.4
  • 28
    • 0021909227 scopus 로고
    • Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic polyneuropathy
    • Felding P, Fex G, Westermark P, Olofsson BO, Pitkänen P, Benson L. Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic polyneuropathy. Scand J Immunol 1985; 21: 133-140.
    • (1985) Scand. J. Immunol. , vol.21 , pp. 133-140
    • Felding, P.1    Fex, G.2    Westermark, P.3    Olofsson, B.O.4    Pitkänen, P.5    Benson, L.6
  • 29
    • 0020697241 scopus 로고
    • Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin
    • Pras M, Prelli F, Franklin EC, Frangione B. Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Natl Acad Sci U S A 1983; 80: 539-542.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 539-542
    • Pras, M.1    Prelli, F.2    Franklin, E.C.3    Frangione, B.4
  • 30
    • 0019490518 scopus 로고
    • A variant of prealbumin from amyloid fibrils in familial polyneuropathy of Jewish origin
    • Pras M, Franklin EC, Prelli F, Frangione B. A variant of prealbumin from amyloid fibrils in familial polyneuropathy of Jewish origin. J Exp Med 1981; 154: 989-993.
    • (1981) J. Exp. Med. , vol.154 , pp. 989-993
    • Pras, M.1    Franklin, E.C.2    Prelli, F.3    Frangione, B.4
  • 31
    • 0024560416 scopus 로고
    • Systemic senile amyloidosis. Identification of a new prealbumin (transthyretin) variant in cardiac tissue: Immunologic and biochemical similarity to one form of familial amyloidotic polyneuropathy
    • Gorevic PD, Prelli FC, Wright J, Pras M, Frangione B. Systemic senile amyloidosis. Identification of a new prealbumin (transthyretin) variant in cardiac tissue: immunologic and biochemical similarity to one form of familial amyloidotic polyneuropathy. J Clin Invest 1989; 83: 836-843.
    • (1989) J. Clin. Invest. , vol.83 , pp. 836-843
    • Gorevic, P.D.1    Prelli, F.C.2    Wright, J.3    Pras, M.4    Frangione, B.5
  • 32
    • 0027389112 scopus 로고
    • Modifications of transthyretin in amyloid fibrils: Analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation
    • Thylen C, Wahlqvist J, Haettner E, Sandgren O, Holmgren G, Lundgren E. Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation. EMBO J 1993; 12: 743-748.
    • (1993) EMBO J. , vol.12 , pp. 743-748
    • Thylen, C.1    Wahlqvist, J.2    Haettner, E.3    Sandgren, O.4    Holmgren, G.5    Lundgren, E.6
  • 33
    • 0028801805 scopus 로고
    • Purification and characterization of amyloid-related transthyretin associated with familial amyloidotic cardiomyopathy
    • Hermansen LF, Bergman T, Jörnvall H, Husby G, Ranløv I, Sletten K. Purification and characterization of amyloid-related transthyretin associated with familial amyloidotic cardiomyopathy. Eur J Biochem 1995; 227: 772-779.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 772-779
    • Hermansen, L.F.1    Bergman, T.2    Jörnvall, H.3    Husby, G.4    Ranløv, I.5    Sletten, K.6
  • 34
    • 2042487135 scopus 로고    scopus 로고
    • Analysis of transthyretin (TTR) forms of amyloid fibrils in familial amyloidotic polyneuropathy (Met 30)
    • Ando Y, Ando E, Ohlsson P-I, et al. Analysis of transthyretin (TTR) forms of amyloid fibrils in familial amyloidotic polyneuropathy (Met 30). Amyloid: Int J Exp Clin Invest 1999; 6: 119-123.
    • (1999) Amyloid: Int. J. Exp. Clin. Invest. , vol.6 , pp. 119-123
    • Ando, Y.1    Ando, E.2    Ohlsson, P.-I.3
  • 35
    • 3543107213 scopus 로고    scopus 로고
    • Two different types of amyloid deposits - Apolipoprotein A-IV and transthyretin - In a patient with systemic amyloidosis
    • Bergström J, Murphy CL, Weiss DT, et al. Two different types of amyloid deposits - apolipoprotein A-IV and transthyretin - in a patient with systemic amyloidosis. Lab Invest 2004; 84: 981-988.
    • (2004) Lab. Invest. , vol.84 , pp. 981-988
    • Bergström, J.1    Murphy, C.L.2    Weiss, D.T.3
  • 36
    • 0028260652 scopus 로고
    • Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations
    • Gustavsson Å, Engström U, Westermark P. Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations. Am J Pathol 1994; 144: 1301-1311.
    • (1994) Am. J. Pathol. , vol.144 , pp. 1301-1311
    • Gustavsson, Å.1    Engström, U.2    Westermark, P.3
  • 37
    • 0032877133 scopus 로고    scopus 로고
    • Microextraction and purification techniques applicable to chemical characterization of amyloid proteins in minute amounts in tissue
    • Kaplan B, Hrncic R, Murphy CL, Gallo G, Weiss DT, Solomon A. Microextraction and purification techniques applicable to chemical characterization of amyloid proteins in minute amounts in tissue. Methods Enzymol 1999; 309: 67-81.
    • (1999) Methods Enzymol. , vol.309 , pp. 67-81
    • Kaplan, B.1    Hrncic, R.2    Murphy, C.L.3    Gallo, G.4    Weiss, D.T.5    Solomon, A.6
  • 38
    • 17844409327 scopus 로고    scopus 로고
    • Chemical typing of amyloid protein contained in formalin-fixed paraffin-embedded biopsy specimens
    • Murphy CL, Eulitz M, Hrncic R, et al. Chemical typing of amyloid protein contained in formalin-fixed paraffin-embedded biopsy specimens. Am J Clin Pathol 2001; 116: 135-142.
    • (2001) Am. J. Clin. Pathol. , vol.116 , pp. 135-142
    • Murphy, C.L.1    Eulitz, M.2    Hrncic, R.3
  • 39
    • 0034811004 scopus 로고    scopus 로고
    • Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis
    • Bergström J, Murphy C, Eulitz M, et al. Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis. Biochem Biophys Res Commun 2001; 285: 903-908.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 903-908
    • Bergström, J.1    Murphy, C.2    Eulitz, M.3
  • 40
    • 0036383921 scopus 로고    scopus 로고
    • Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector
    • Hellman U, Bhikhabhai R. Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. Rapid Commun Mass Spectrom 2002; 16: 1851-1859.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 1851-1859
    • Hellman, U.1    Bhikhabhai, R.2
  • 41
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987; 166: 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 44
    • 1242316998 scopus 로고    scopus 로고
    • Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
    • Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Öhman A. Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J Biol Chem 2004; 279: 5699-5707.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Wijmenga, S.S.3    Lundgren, E.4    Öhman, A.5


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