메뉴 건너뛰기




Volumn 27, Issue 5, 2015, Pages 303-323

The diversity of mechanisms influenced by transthyretin in neurobiology: Development, disease and endocrine disruption

Author keywords

Amyloid; Choroid plexus; Endocrine disruption; Evolution of function; Thyroid hormones; Transthyretin

Indexed keywords

APOLIPOPROTEIN A1; ENDOCRINE DISRUPTOR; NEUROPEPTIDE Y; PREALBUMIN; THYROID HORMONE; DNA; RETINOL BINDING PROTEIN;

EID: 84928034050     PISSN: 09538194     EISSN: 13652826     Source Type: Journal    
DOI: 10.1111/jne.12271     Document Type: Review
Times cited : (71)

References (222)
  • 1
    • 0001921555 scopus 로고
    • Electrophoretic study of the blood protein response in tuberculosis
    • Seibert FB, Nelson JW. Electrophoretic study of the blood protein response in tuberculosis. J Biol Chem 1942; 143: 29-38.
    • (1942) J Biol Chem , vol.143 , pp. 29-38
    • Seibert, F.B.1    Nelson, J.W.2
  • 2
    • 0001435965 scopus 로고
    • An electrophoretic study of the protein components in cerebrospinal fluid and their relationship to the serum proteins
    • Kabat EA, Moore DH, Landow H. An electrophoretic study of the protein components in cerebrospinal fluid and their relationship to the serum proteins. J Clin Invest 1942; 21: 571-577.
    • (1942) J Clin Invest , vol.21 , pp. 571-577
    • Kabat, E.A.1    Moore, D.H.2    Landow, H.3
  • 3
    • 0000532662 scopus 로고
    • Pre-albumin: a thyroxinebinding protein of human plasma
    • Ingbar SH. Pre-albumin: a thyroxinebinding protein of human plasma. Endocrinology 1958; 63: 256-259.
    • (1958) Endocrinology , vol.63 , pp. 256-259
    • Ingbar, S.H.1
  • 4
    • 0014690587 scopus 로고
    • The interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex
    • Raz A, Goodman DS. The interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex. J Biol Chem 1969; 244: 3230-3237.
    • (1969) J Biol Chem , vol.244 , pp. 3230-3237
    • Raz, A.1    Goodman, D.S.2
  • 5
    • 84918671290 scopus 로고
    • (NC-IUB) and IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Newsletter 1981
    • Nomenclature Committee of IUB.
    • Nomenclature Committee of IUB. (NC-IUB) and IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Newsletter 1981. Eur J Biochem 1981; 256: 12-14.
    • (1981) Eur J Biochem , vol.256 , pp. 12-14
  • 6
    • 0014017099 scopus 로고
    • Crystallization of prealbumin from human serum
    • Haupt H, Heide K. Crystallization of prealbumin from human serum. Experientia 1966; 22: 449-451.
    • (1966) Experientia , vol.22 , pp. 449-451
    • Haupt, H.1    Heide, K.2
  • 7
    • 0017824077 scopus 로고
    • Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
    • 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 A. 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
  • 8
    • 0016140360 scopus 로고
    • Structure of human plasma prealbumin at 2.5 A resolution: a preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding
    • Blake CCF, Geisow MJ, Swan IDA, Rerat C, Rerat B. Structure of human plasma prealbumin at 2.5 A resolution: a preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol 1974; 88: 1-12.
    • (1974) J Mol Biol , vol.88 , pp. 1-12
    • Blake, C.C.F.1    Geisow, M.J.2    Swan, I.D.A.3    Rerat, C.4    Rerat, B.5
  • 9
    • 0017754889 scopus 로고
    • Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?
    • Blake CC, Oatley SJ. Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor? Nature 1977; 268: 115-120.
    • (1977) Nature , vol.268 , pp. 115-120
    • Blake, C.C.1    Oatley, S.J.2
  • 11
    • 0030484635 scopus 로고    scopus 로고
    • Structures of human transthyretin complexed with thyroxine at 2.0 A resolution and 3′,5′-dinitro-N-acetyl-l-thyronine at 2.2 A resolution
    • Wojtczak A, Cody V, Luft JR, Pangborn W. Structures of human transthyretin complexed with thyroxine at 2.0 A resolution and 3′, 5′-dinitro-N-acetyl-l-thyronine at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr 1996; 52: 758-765.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 758-765
    • Wojtczak, A.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4
  • 12
    • 0035755698 scopus 로고    scopus 로고
    • Structural basis of negative cooperativity in transthyretin
    • Neumann P, Cody V, Wojtczak A. Structural basis of negative cooperativity in transthyretin. Acta Biochim Pol 2001; 48: 867-875.
    • (2001) Acta Biochim Pol , vol.48 , pp. 867-875
    • Neumann, P.1    Cody, V.2    Wojtczak, A.3
  • 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, 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
  • 14
    • 0036919608 scopus 로고    scopus 로고
    • Three-dimensional structure of the transthyretin-retinol-binding protein complex
    • Monaco HL. Three-dimensional structure of the transthyretin-retinol-binding protein complex. Clin Chem Lab Med 2002; 40: 1229-1236.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1229-1236
    • Monaco, H.L.1
  • 15
    • 0036910522 scopus 로고    scopus 로고
    • Hepatic synthesis, maturation and complex formation between retinol-binding protein and transthyretin
    • Gaetani S, Bellovino D, Apreda M, Devirgiliis C. Hepatic synthesis, maturation and complex formation between retinol-binding protein and transthyretin. Clin Chem Lab Med 2002; 40: 1211-1220.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1211-1220
    • Gaetani, S.1    Bellovino, D.2    Apreda, M.3    Devirgiliis, C.4
  • 16
    • 2942741033 scopus 로고    scopus 로고
    • High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine
    • Eneqvist T, Lundberg E, Karlsson A, Huang S, Santos CR, Power DM, Sauer-Eriksson AE. High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine. J Biol Chem 2004; 279: 26411-26416.
    • (2004) J Biol Chem , vol.279 , pp. 26411-26416
    • Eneqvist, T.1    Lundberg, E.2    Karlsson, A.3    Huang, S.4    Santos, C.R.5    Power, D.M.6    Sauer-Eriksson, A.E.7
  • 18
    • 0035756499 scopus 로고    scopus 로고
    • Complex of rat transthyretin with tetraiodothyroacetic acid refined at 2.1 and 1.8 A resolution
    • Muziol T, Cody V, Luft JR, Pangborn W, Wojtczak A. Complex of rat transthyretin with tetraiodothyroacetic acid refined at 2.1 and 1.8 A resolution. Acta Biochim Pol 2001; 48: 877-884.
    • (2001) Acta Biochim Pol , vol.48 , pp. 877-884
    • Muziol, T.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4    Wojtczak, A.5
  • 19
    • 33847320656 scopus 로고    scopus 로고
    • Cell and molecular biology of transthyretin and thyroid hormones
    • Richardson SJ. Cell and molecular biology of transthyretin and thyroid hormones. Int Rev Cytol 2007; 258: 137-193.
    • (2007) Int Rev Cytol , vol.258 , pp. 137-193
    • Richardson, S.J.1
  • 20
    • 0030977515 scopus 로고    scopus 로고
    • Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1)
    • Aldred AR, Prapunpoj P, Schreiber G. Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1). Eur J Biochem 1997; 246: 401-409.
    • (1997) Eur J Biochem , vol.246 , pp. 401-409
    • Aldred, A.R.1    Prapunpoj, P.2    Schreiber, G.3
  • 21
    • 0007824822 scopus 로고    scopus 로고
    • Evolution of thyroid hormone binding by transthyretins in birds and mammals
    • Chang L, Munro SL, Richardson SJ, Schreiber G. Evolution of thyroid hormone binding by transthyretins in birds and mammals. Eur J Biochem 1999; 259: 534-542.
    • (1999) Eur J Biochem , vol.259 , pp. 534-542
    • Chang, L.1    Munro, S.L.2    Richardson, S.J.3    Schreiber, G.4
  • 22
    • 33747438335 scopus 로고    scopus 로고
    • Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3
    • Prapunpoj P, Leelawatwatana L, Schreiber G, Richardson SJ. Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3. FEBS J 2006; 273: 4013-4023.
    • (2006) FEBS J , vol.273 , pp. 4013-4023
    • Prapunpoj, P.1    Leelawatwatana, L.2    Schreiber, G.3    Richardson, S.J.4
  • 23
    • 0018744359 scopus 로고
    • Relationship of receptor affinity to the modulation of thyroid hormone nuclear receptor levels and growth hormone synthesis by l-triiodothyronine and iodothyronine analogues in cultured GH1 cells
    • Samuels HH, Stanley F, Casanova J. Relationship of receptor affinity to the modulation of thyroid hormone nuclear receptor levels and growth hormone synthesis by l-triiodothyronine and iodothyronine analogues in cultured GH1 cells. J Clin Invest 1979; 63: 1229-1240.
    • (1979) J Clin Invest , vol.63 , pp. 1229-1240
    • Samuels, H.H.1    Stanley, F.2    Casanova, J.3
  • 24
    • 84869100945 scopus 로고    scopus 로고
    • Iodothyronine deiodinase structure and function: from ascidians to humans
    • Darras VM, Van Herck SL. Iodothyronine deiodinase structure and function: from ascidians to humans. J Endocrinol 2012; 215: 189-206.
    • (2012) J Endocrinol , vol.215 , pp. 189-206
    • Darras, V.M.1    Van Herck, S.L.2
  • 25
    • 0021802634 scopus 로고
    • Concentrations of thyroxine and 3,5,3′-triiodothyronine at 34 different sites in euthyroid rats as determined by an isotopic equilibrium technique
    • van Doorn J, Roelfsema F, van der Heide D. Concentrations of thyroxine and 3, 5, 3′-triiodothyronine at 34 different sites in euthyroid rats as determined by an isotopic equilibrium technique. Endocrinology 1985; 117: 1201-1208.
    • (1985) Endocrinology , vol.117 , pp. 1201-1208
    • van Doorn, J.1    Roelfsema, F.2    van der Heide, D.3
  • 26
    • 0025011704 scopus 로고
    • Congenital hypothyroidism, as studied in rats. Crucial role of maternal thyroxine but not of 3,5,3′-triiodothyronine in the protection of the fetal brain
    • Calvo R, Obregon MJ, Ruiz de Ona C, Escobar del Rey F, Morreale de Escobar G. Congenital hypothyroidism, as studied in rats. Crucial role of maternal thyroxine but not of 3, 5, 3′-triiodothyronine in the protection of the fetal brain. J Clin Invest 1990; 86: 889-899.
    • (1990) J Clin Invest , vol.86 , pp. 889-899
    • Calvo, R.1    Obregon, M.J.2    Ruiz de Ona, C.3    Escobar del Rey, F.4    Morreale de Escobar, G.5
  • 27
    • 0036801304 scopus 로고    scopus 로고
    • The evolutionary and integrative roles of transthyretin in thyroid hormone homeostasis
    • Schreiber G. The evolutionary and integrative roles of transthyretin in thyroid hormone homeostasis. J Endocrinol 2002; 175: 61-73.
    • (2002) J Endocrinol , vol.175 , pp. 61-73
    • Schreiber, G.1
  • 28
    • 0034892914 scopus 로고    scopus 로고
    • Plasma membrane transport of thyroid hormones and its role in thyroid hormone metabolism and bioavailability
    • Hennemann G, Docter R, Friesema EC, de Jong M, Krenning EP, Visser TJ. Plasma membrane transport of thyroid hormones and its role in thyroid hormone metabolism and bioavailability. Endocr Rev 2001; 22: 451-476.
    • (2001) Endocr Rev , vol.22 , pp. 451-476
    • Hennemann, G.1    Docter, R.2    Friesema, E.C.3    de Jong, M.4    Krenning, E.P.5    Visser, T.J.6
  • 29
    • 0023229118 scopus 로고
    • Thyroid hormone-binding proteins in plasma facilitate uniform distribution of thyroxine within tissues: a perfused rat liver study
    • Mendel CM, Weisiger RA, Jones AL, Cavalieri RR. Thyroid hormone-binding proteins in plasma facilitate uniform distribution of thyroxine within tissues: a perfused rat liver study. Endocrinology 1987; 120: 1742-1749.
    • (1987) Endocrinology , vol.120 , pp. 1742-1749
    • Mendel, C.M.1    Weisiger, R.A.2    Jones, A.L.3    Cavalieri, R.R.4
  • 30
    • 0030945339 scopus 로고    scopus 로고
    • The evolution of gene expression, structure and function of transthyretin
    • Schreiber G, Richardson SJ. The evolution of gene expression, structure and function of transthyretin. Comp Biochem Physiol B Biochem Mol Biol 1997; 116: 137-160.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.116 , pp. 137-160
    • Schreiber, G.1    Richardson, S.J.2
  • 33
    • 0035020343 scopus 로고    scopus 로고
    • Re-evaluation of the thyroxine binding to human plasma lipoproteins using three techniques
    • Benvenga S, Lapa D, Trimarchi F. Re-evaluation of the thyroxine binding to human plasma lipoproteins using three techniques. J Endocrinol Invest 2001; 24: RC16-RC18.
    • (2001) J Endocrinol Invest , vol.24 , pp. RC16-RC18
    • Benvenga, S.1    Lapa, D.2    Trimarchi, F.3
  • 34
    • 0025647127 scopus 로고
    • Thyroxine uptake by perfused rat liver. No evidence for facilitation by five different thyroxine-binding proteins
    • Mendel CM, Weisiger RA. Thyroxine uptake by perfused rat liver. No evidence for facilitation by five different thyroxine-binding proteins. J Clin Invest 1990; 86: 1840-1847.
    • (1990) J Clin Invest , vol.86 , pp. 1840-1847
    • Mendel, C.M.1    Weisiger, R.A.2
  • 35
    • 0024430817 scopus 로고
    • The free hormone hypothesis - a physiologically based mathematical-model
    • Mendel CM. The free hormone hypothesis - a physiologically based mathematical-model. Endocr Rev 1989; 10: 232-274.
    • (1989) Endocr Rev , vol.10 , pp. 232-274
    • Mendel, C.M.1
  • 36
    • 0036919227 scopus 로고    scopus 로고
    • Transthyretin from discovery to now
    • Robbins J. Transthyretin from discovery to now. Clin Chem Lab Med 2002; 40: 1183-1190.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1183-1190
    • Robbins, J.1
  • 37
    • 0025264751 scopus 로고
    • The hepatic biosynthesis of rat thyroxine binding globulin (TBG): demonstration, ontogenesis, and up-regulation in experimental hypothyroidism
    • Vranckx R, Rouaze M, Savu L, Nunez EA, Beaumont C, Flink IL. The hepatic biosynthesis of rat thyroxine binding globulin (TBG): demonstration, ontogenesis, and up-regulation in experimental hypothyroidism. Biochem Biophys Res Commun 1990; 167: 317-322.
    • (1990) Biochem Biophys Res Commun , vol.167 , pp. 317-322
    • Vranckx, R.1    Rouaze, M.2    Savu, L.3    Nunez, E.A.4    Beaumont, C.5    Flink, I.L.6
  • 38
    • 0025109632 scopus 로고
    • Characterization of a major development-regulated serum thyroxine-binding globulin in the euthyroid mouse
    • Vranckx R, Savu L, Maya M, Nunez EA. Characterization of a major development-regulated serum thyroxine-binding globulin in the euthyroid mouse. Biochem J 1990; 271: 373-379.
    • (1990) Biochem J , vol.271 , pp. 373-379
    • Vranckx, R.1    Savu, L.2    Maya, M.3    Nunez, E.A.4
  • 40
    • 0021996005 scopus 로고
    • Rat transthyretin (prealbumin) - molecular-cloning, nucleotide-sequence, and gene-expression in liver and brain
    • Dickson PW, Howlett GJ, Schreiber G. Rat transthyretin (prealbumin) - molecular-cloning, nucleotide-sequence, and gene-expression in liver and brain. J Biol Chem 1985; 260: 8214-8219.
    • (1985) J Biol Chem , vol.260 , pp. 8214-8219
    • Dickson, P.W.1    Howlett, G.J.2    Schreiber, G.3
  • 41
    • 0025013276 scopus 로고
    • Plasma protein synthesis and secretion in the visceral yolk sac of the fetal rat: gene expression, protein synthesis and secretion
    • Thomas T, Southwell BR, Schreiber G, Jaworowski A. Plasma protein synthesis and secretion in the visceral yolk sac of the fetal rat: gene expression, protein synthesis and secretion. Placenta 1990; 11: 413-430.
    • (1990) Placenta , vol.11 , pp. 413-430
    • Thomas, T.1    Southwell, B.R.2    Schreiber, G.3    Jaworowski, A.4
  • 42
    • 0023240265 scopus 로고
    • Synthesis of retinol-binding protein and transthyretin in yolk sac and fetus in the rat
    • Sklan D, Ross AC. Synthesis of retinol-binding protein and transthyretin in yolk sac and fetus in the rat. J Nutr 1987; 117: 436-442.
    • (1987) J Nutr , vol.117 , pp. 436-442
    • Sklan, D.1    Ross, A.C.2
  • 44
    • 0028331788 scopus 로고
    • Synthesis and secretion of retinol-binding protein and transthyretin by cultured retinal pigment epithelium
    • Ong DE, Davis JT, O'Day WT, Bok D. Synthesis and secretion of retinol-binding protein and transthyretin by cultured retinal pigment epithelium. Biochemistry 1994; 33: 1835-1842.
    • (1994) Biochemistry , vol.33 , pp. 1835-1842
    • Ong, D.E.1    Davis, J.T.2    O'Day, W.T.3    Bok, D.4
  • 45
    • 0021835636 scopus 로고
    • Plasma and cellular retinoid-binding proteins and transthyretin (prealbumin) are all localized in the islets of langerhans in the rat
    • Kato M, Kato K, Blaner WS, Chertow BS, Goodman DS. Plasma and cellular retinoid-binding proteins and transthyretin (prealbumin) are all localized in the islets of langerhans in the rat. Proc Natl Acad Sci USA 1985; 82: 2488-2492.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2488-2492
    • Kato, M.1    Kato, K.2    Blaner, W.S.3    Chertow, B.S.4    Goodman, D.S.5
  • 46
    • 0027946187 scopus 로고
    • An in vivo study of the effect of 5-HT and sympathetic nerves on transferrin and transthyretin mRNA expression in rat choroid plexus and meninges
    • Blay P, Nilsson C, Hansson S, Owman C, Aldred AR, Schreiber G. An in vivo study of the effect of 5-HT and sympathetic nerves on transferrin and transthyretin mRNA expression in rat choroid plexus and meninges. Brain Res 1994; 662: 148-154.
    • (1994) Brain Res , vol.662 , pp. 148-154
    • Blay, P.1    Nilsson, C.2    Hansson, S.3    Owman, C.4    Aldred, A.R.5    Schreiber, G.6
  • 47
    • 0028870058 scopus 로고
    • Molecular analysis of the expression of transthyretin in intestine and liver from trisomy 18 fetuses
    • Loughna S, Bennett P, Moore G. Molecular analysis of the expression of transthyretin in intestine and liver from trisomy 18 fetuses. Hum Genet 1995; 95: 89-95.
    • (1995) Hum Genet , vol.95 , pp. 89-95
    • Loughna, S.1    Bennett, P.2    Moore, G.3
  • 48
    • 77955708997 scopus 로고    scopus 로고
    • The transthyretin gene is expressed in Schwann cells of peripheral nerves
    • Murakami T, Ohsawa Y, Zhenghua L, Yamamura K, Sunada Y. The transthyretin gene is expressed in Schwann cells of peripheral nerves. Brain Res 2010; 1348: 222-225.
    • (2010) Brain Res , vol.1348 , pp. 222-225
    • Murakami, T.1    Ohsawa, Y.2    Zhenghua, L.3    Yamamura, K.4    Sunada, Y.5
  • 49
    • 80052350163 scopus 로고    scopus 로고
    • Neuronal production of transthyretin in human and murine alzheimer's disease: is it protective?
    • Li X, Masliah E, Reixach N, Buxbaum JN. Neuronal production of transthyretin in human and murine alzheimer's disease: is it protective? J Neurosci 2011; 31: 12483-12490.
    • (2011) J Neurosci , vol.31 , pp. 12483-12490
    • Li, X.1    Masliah, E.2    Reixach, N.3    Buxbaum, J.N.4
  • 50
    • 3042855348 scopus 로고
    • Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat
    • Soprano DR, Soprano KJ, Goodman DS. Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat. Proc Natl Acad Sci USA 1986; 83: 7330-7334.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7330-7334
    • Soprano, D.R.1    Soprano, K.J.2    Goodman, D.S.3
  • 51
    • 0022202960 scopus 로고
    • Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat
    • Soprano DR, Herbert J, Soprano KJ, Schon EA, Goodman DS. Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat. J Biol Chem 1985; 260: 11793-11798.
    • (1985) J Biol Chem , vol.260 , pp. 11793-11798
    • Soprano, D.R.1    Herbert, J.2    Soprano, K.J.3    Schon, E.A.4    Goodman, D.S.5
  • 53
    • 0022447169 scopus 로고
    • Synthesis of transthyretin (pre-albumin) mRNA in choroid plexus epithelial cells, localized by in situ hybridization in rat brain
    • Stauder AJ, Dickson PW, Aldred AR, Schreiber G, Mendelsohn FA, Hudson P. Synthesis of transthyretin (pre-albumin) mRNA in choroid plexus epithelial cells, localized by in situ hybridization in rat brain. J Histochem Cytochem 1986; 34: 949-952.
    • (1986) J Histochem Cytochem , vol.34 , pp. 949-952
    • Stauder, A.J.1    Dickson, P.W.2    Aldred, A.R.3    Schreiber, G.4    Mendelsohn, F.A.5    Hudson, P.6
  • 55
    • 0026577768 scopus 로고
    • Role of transthyretin in the transport of thyroxine from the blood to the choroid plexus, the cerebrospinal fluid, and the brain
    • Chanoine JP, Alex S, Fang SL, Stone S, Leonard JL, Korhle J, Braverman LE. Role of transthyretin in the transport of thyroxine from the blood to the choroid plexus, the cerebrospinal fluid, and the brain. Endocrinology 1992; 130: 933-938.
    • (1992) Endocrinology , vol.130 , pp. 933-938
    • Chanoine, J.P.1    Alex, S.2    Fang, S.L.3    Stone, S.4    Leonard, J.L.5    Korhle, J.6    Braverman, L.E.7
  • 57
    • 0023811701 scopus 로고
    • The expression of transthyretin mRNA in the developing rat brain
    • Thomas T, Power B, Hudson P, Schreiber G, Dziadek M. The expression of transthyretin mRNA in the developing rat brain. Dev Biol 1988; 128: 415-427.
    • (1988) Dev Biol , vol.128 , pp. 415-427
    • Thomas, T.1    Power, B.2    Hudson, P.3    Schreiber, G.4    Dziadek, M.5
  • 59
    • 0025125103 scopus 로고
    • Expression of the genes for transthyretin, cystatin C and beta A4 amyloid precursor protein in sheep choroid plexus during development
    • Tu GF, Cole T, Southwell BR, Schreiber G. Expression of the genes for transthyretin, cystatin C and beta A4 amyloid precursor protein in sheep choroid plexus during development. Brain Res Dev Brain Res 1990; 55: 203-208.
    • (1990) Brain Res Dev Brain Res , vol.55 , pp. 203-208
    • Tu, G.F.1    Cole, T.2    Southwell, B.R.3    Schreiber, G.4
  • 60
    • 22144465949 scopus 로고    scopus 로고
    • Expression of transthyretin in the choroid plexus: relationship to brain homeostasis of thyroid hormones
    • Zheng W, Chodobski A., ed. Boca Raton, FL: Taylor and Francis
    • Richardson SJ. Expression of transthyretin in the choroid plexus: relationship to brain homeostasis of thyroid hormones. In: Zheng W, Chodobski A., ed. The Blood-Cerebrospinal Fluid Barrier. Boca Raton, FL: Taylor and Francis, 2005: 279-307.
    • (2005) The Blood-Cerebrospinal Fluid Barrier , pp. 279-307
    • Richardson, S.J.1
  • 61
    • 0025735197 scopus 로고
    • Transthyretin (prealbumin) gene-expression in choroid-plexus is strongly conserved during evolution of vertebrates
    • Harms PJ, Tu GF, Richardson SJ, Aldred AR, Jaworowski A, Schreiber G. Transthyretin (prealbumin) gene-expression in choroid-plexus is strongly conserved during evolution of vertebrates. Comp Biochem Physiol B 1991; 99: 239-249.
    • (1991) Comp Biochem Physiol B , vol.99 , pp. 239-249
    • Harms, P.J.1    Tu, G.F.2    Richardson, S.J.3    Aldred, A.R.4    Jaworowski, A.5    Schreiber, G.6
  • 62
    • 0026475385 scopus 로고
    • Protein synthesis at the blood-brain barrier. The major protein secreted by amphibian choroid plexus is a lipocalin
    • Achen MG, Harms PJ, Thomas T, Richardson SJ, Wettenhall RE, Schreiber G. Protein synthesis at the blood-brain barrier. The major protein secreted by amphibian choroid plexus is a lipocalin. J Biol Chem 1992; 267: 23170-23174.
    • (1992) J Biol Chem , vol.267 , pp. 23170-23174
    • Achen, M.G.1    Harms, P.J.2    Thomas, T.3    Richardson, S.J.4    Wettenhall, R.E.5    Schreiber, G.6
  • 63
    • 0025008962 scopus 로고
    • Distinct positive and negative elements control the limited hepatocyte and choroid plexus expression of transthyretin in transgenic mice
    • Yan C, Costa RH, Darnell JE Jr, Chen JD, Van Dyke TA. Distinct positive and negative elements control the limited hepatocyte and choroid plexus expression of transthyretin in transgenic mice. EMBO J 1990; 9: 869-878.
    • (1990) EMBO J , vol.9 , pp. 869-878
    • Yan, C.1    Costa, R.H.2    Darnell, J.E.3    Chen, J.D.4    Van Dyke, T.A.5
  • 64
    • 0025054242 scopus 로고
    • Similarities in transthyretin gene expression and differences in transcription factors: liver and yolk sac compared to choroid plexus
    • Costa RH, Van Dyke TA, Yan C, Kuo F, Darnell JE Jr. Similarities in transthyretin gene expression and differences in transcription factors: liver and yolk sac compared to choroid plexus. Proc Natl Acad Sci USA 1990; 87: 6589-6593.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6589-6593
    • Costa, R.H.1    Van Dyke, T.A.2    Yan, C.3    Kuo, F.4    Darnell, J.E.5
  • 65
    • 0028804622 scopus 로고
    • Decreased expression of hepatocyte nuclear factor 3 alpha during the acute-phase response influences transthyretin gene transcription
    • Qian X, Samadani U, Porcella A, Costa RH. Decreased expression of hepatocyte nuclear factor 3 alpha during the acute-phase response influences transthyretin gene transcription. Mol Cell Biol 1995; 15: 1364-1376.
    • (1995) Mol Cell Biol , vol.15 , pp. 1364-1376
    • Qian, X.1    Samadani, U.2    Porcella, A.3    Costa, R.H.4
  • 66
    • 0030330471 scopus 로고    scopus 로고
    • Identification of a transthyretin enhancer site that selectively binds the hepatocyte nuclear factor-3 beta isoform
    • Samadani U, Qian X, Costa RH. Identification of a transthyretin enhancer site that selectively binds the hepatocyte nuclear factor-3 beta isoform. Gene Expr 1996; 6: 23-33.
    • (1996) Gene Expr , vol.6 , pp. 23-33
    • Samadani, U.1    Qian, X.2    Costa, R.H.3
  • 67
    • 0022970287 scopus 로고
    • Rat choroid plexus specializes in the synthesis and the secretion of transthyretin (prealbumin). Regulation of transthyretin synthesis in choroid plexus is independent from that in liver
    • Dickson PW, Aldred AR, Marley PD, Bannister D, Schreiber G. Rat choroid plexus specializes in the synthesis and the secretion of transthyretin (prealbumin). Regulation of transthyretin synthesis in choroid plexus is independent from that in liver. J Biol Chem 1986; 261: 3475-3478.
    • (1986) J Biol Chem , vol.261 , pp. 3475-3478
    • Dickson, P.W.1    Aldred, A.R.2    Marley, P.D.3    Bannister, D.4    Schreiber, G.5
  • 71
    • 0030993449 scopus 로고    scopus 로고
    • Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice
    • Palha J, Hays M, Morreale de EG, Episkopou V, Gottesman M, Saraiva M. Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice. Am J Physiol 1997; 272: E485-E489.
    • (1997) Am J Physiol , vol.272 , pp. E485-E489
    • Palha, J.1    Hays, M.2    Morreale de, E.G.3    Episkopou, V.4    Gottesman, M.5    Saraiva, M.6
  • 72
    • 0034458354 scopus 로고    scopus 로고
    • Transthyretin regulates thyroid hormone levels in the choroid plexus, but not in the brain parenchyma: study in a transthyretin-null mouse model
    • Palha JA, Fernandes R, de Escobar GM, Episkopou V, Gottesman M, Saraiva MJ. Transthyretin regulates thyroid hormone levels in the choroid plexus, but not in the brain parenchyma: study in a transthyretin-null mouse model. Endocrinology 2000; 141: 3267-3272.
    • (2000) Endocrinology , vol.141 , pp. 3267-3272
    • Palha, J.A.1    Fernandes, R.2    de Escobar, G.M.3    Episkopou, V.4    Gottesman, M.5    Saraiva, M.J.6
  • 73
    • 28044432318 scopus 로고    scopus 로고
    • Transthyretin is not necessary for thyroid hormone metabolism in conditions of increased hormone demand
    • Sousa J, de Escobar GM, Oliveira P, Saraiva M, Palha J. Transthyretin is not necessary for thyroid hormone metabolism in conditions of increased hormone demand. J Endocrinol 2005; 187: 257-266.
    • (2005) J Endocrinol , vol.187 , pp. 257-266
    • Sousa, J.1    de Escobar, G.M.2    Oliveira, P.3    Saraiva, M.4    Palha, J.5
  • 76
    • 0023176623 scopus 로고
    • Effects of maternal iodine deficiency on thyroid hormone economy of lactating dams and pups: maintenance of normal cerebral 3,5,3′-triiodo-l-thyronine concentrations in pups during major phases of brain development
    • Escobar del Rey F, Mallol J, Pastor R, Morreale de Escobar G. Effects of maternal iodine deficiency on thyroid hormone economy of lactating dams and pups: maintenance of normal cerebral 3, 5, 3′-triiodo-l-thyronine concentrations in pups during major phases of brain development. Endocrinology 1987; 121: 803-811.
    • (1987) Endocrinology , vol.121 , pp. 803-811
    • Escobar del Rey, F.1    Mallol, J.2    Pastor, R.3    Morreale de Escobar, G.4
  • 78
    • 0004349813 scopus 로고
    • Concentration of taurine, beta-alanine, and triiodothyronine by ascites carcinoma cells
    • Christensen HN, Hess B, Riggs TR. Concentration of taurine, beta-alanine, and triiodothyronine by ascites carcinoma cells. Cancer Res 1954; 14: 124-127.
    • (1954) Cancer Res , vol.14 , pp. 124-127
    • Christensen, H.N.1    Hess, B.2    Riggs, T.R.3
  • 79
    • 78650916392 scopus 로고    scopus 로고
    • Minireview: thyroid hormone transporters: the knowns and the unknowns
    • Visser WE, Friesema EC, Visser TJ. Minireview: thyroid hormone transporters: the knowns and the unknowns. Mol Endocrinol 2011; 25: 1-14.
    • (2011) Mol Endocrinol , vol.25 , pp. 1-14
    • Visser, W.E.1    Friesema, E.C.2    Visser, T.J.3
  • 81
    • 84857433358 scopus 로고    scopus 로고
    • Impact of Oatp1c1 deficiency on thyroid hormone metabolism and action in the mouse brain
    • Mayerl S, Visser TJ, Darras VM, Horn S, Heuer H. Impact of Oatp1c1 deficiency on thyroid hormone metabolism and action in the mouse brain. Endocrinology 2012; 153: 1528-1537.
    • (2012) Endocrinology , vol.153 , pp. 1528-1537
    • Mayerl, S.1    Visser, T.J.2    Darras, V.M.3    Horn, S.4    Heuer, H.5
  • 82
    • 79954458012 scopus 로고    scopus 로고
    • Tissue-specific effects of mutations in the thyroid hormone transporter MCT8
    • Kersseboom S, Visser TJ. Tissue-specific effects of mutations in the thyroid hormone transporter MCT8. Arq Bras Endocrinol Metabol 2011; 55: 1-5.
    • (2011) Arq Bras Endocrinol Metabol , vol.55 , pp. 1-5
    • Kersseboom, S.1    Visser, T.J.2
  • 83
    • 0021174089 scopus 로고
    • Vitamin A and retinoids in health and disease
    • Goodman DS. Vitamin A and retinoids in health and disease. N Engl J Med 1984; 310: 1023-1031.
    • (1984) N Engl J Med , vol.310 , pp. 1023-1031
    • Goodman, D.S.1
  • 84
    • 0026468669 scopus 로고
    • Interactions of retinol with binding proteins: studies with retinol-binding protein and with transthyretin
    • Noy N, Slosberg E, Scarlata S. Interactions of retinol with binding proteins: studies with retinol-binding protein and with transthyretin. Biochemistry 1992; 31: 11118-11124.
    • (1992) Biochemistry , vol.31 , pp. 11118-11124
    • Noy, N.1    Slosberg, E.2    Scarlata, S.3
  • 85
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
    • Monaco HL, Rizzi M, Coda A. Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science 1995; 268: 1039-1041.
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 86
    • 0015884467 scopus 로고
    • The interaction of human plasma retinol-binding protein and prealbumin
    • van Jaarsveld PP, Edelhoch H, Goodman DS, Robbins J. The interaction of human plasma retinol-binding protein and prealbumin. J Biol Chem 1973; 248: 4698-4705.
    • (1973) J Biol Chem , vol.248 , pp. 4698-4705
    • van Jaarsveld, P.P.1    Edelhoch, H.2    Goodman, D.S.3    Robbins, J.4
  • 87
    • 0014336534 scopus 로고
    • Retinol-binding protein: the transport protein for vitamin A in human plasma
    • Kanai M, Raz A, Goodman DS. Retinol-binding protein: the transport protein for vitamin A in human plasma. J Clin Invest 1968; 47: 2025-2044.
    • (1968) J Clin Invest , vol.47 , pp. 2025-2044
    • Kanai, M.1    Raz, A.2    Goodman, D.S.3
  • 88
    • 0015216953 scopus 로고
    • Studies on the interaction between prealbumin, retinol-binding protein, and vitamin A
    • Peterson P. Studies on the interaction between prealbumin, retinol-binding protein, and vitamin A. J Biol Chem 1971; 246: 44-49.
    • (1971) J Biol Chem , vol.246 , pp. 44-49
    • Peterson, P.1
  • 89
    • 0024445843 scopus 로고
    • Retinol-binding protein: the serum transport protein for vitamin A
    • Blaner WS. Retinol-binding protein: the serum transport protein for vitamin A. Endocr Rev 1989; 10: 308-316.
    • (1989) Endocr Rev , vol.10 , pp. 308-316
    • Blaner, W.S.1
  • 91
    • 0028959254 scopus 로고
    • Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous recombination
    • Wei S, Episkopou V, Piantedosi R, Maeda S, Shimada K, Gottesman ME, Blaner WS. Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous recombination. J Biol Chem 1995; 270: 866-870.
    • (1995) J Biol Chem , vol.270 , pp. 866-870
    • Wei, S.1    Episkopou, V.2    Piantedosi, R.3    Maeda, S.4    Shimada, K.5    Gottesman, M.E.6    Blaner, W.S.7
  • 92
    • 0025937134 scopus 로고
    • Retinol-binding protein and transthyretin expressed in HeLa cells form a complex in the endoplasmic reticulum in both the absence and the presence of retinol
    • Melhus H, Nilsson T, Peterson PA, Rask L. Retinol-binding protein and transthyretin expressed in HeLa cells form a complex in the endoplasmic reticulum in both the absence and the presence of retinol. Exp Cell Res 1991; 197: 119-124.
    • (1991) Exp Cell Res , vol.197 , pp. 119-124
    • Melhus, H.1    Nilsson, T.2    Peterson, P.A.3    Rask, L.4
  • 94
    • 0026584568 scopus 로고
    • The piscine plasma retinol-binding protein. Purification, partial amino acid sequence and interaction with mammalian transthyretin of rainbow trout (Oncorhynchus mykiss) retinol-binding protein
    • Berni R, Stoppini M, Zapponi MC. The piscine plasma retinol-binding protein. Purification, partial amino acid sequence and interaction with mammalian transthyretin of rainbow trout (Oncorhynchus mykiss) retinol-binding protein. Eur J Biochem 1992; 204: 99-106.
    • (1992) Eur J Biochem , vol.204 , pp. 99-106
    • Berni, R.1    Stoppini, M.2    Zapponi, M.C.3
  • 96
    • 0023913120 scopus 로고
    • The steroid and thyroid-hormone receptor superfamily
    • Evans RM. The steroid and thyroid-hormone receptor superfamily. Science 1988; 240: 889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 97
    • 22144436966 scopus 로고    scopus 로고
    • Evolution of the thyroid hormone distributor protein transthyretin in microbes, C. elegans, and vertebrates
    • Richardson SJ, Hennebry SC, Smith BJ, Wright HM. Evolution of the thyroid hormone distributor protein transthyretin in microbes, C. elegans, and vertebrates. Ann NY Acad Sci 2005; 1040: 448-451.
    • (2005) Ann NY Acad Sci , vol.1040 , pp. 448-451
    • Richardson, S.J.1    Hennebry, S.C.2    Smith, B.J.3    Wright, H.M.4
  • 98
    • 0033639180 scopus 로고    scopus 로고
    • Evolution of structure, ontogeny of gene expression and function of Xenopus transthyretin
    • Prapunpoj P, Yamauchi K, Nishiyama N, Richardson SJ, Schreiber G. Evolution of structure, ontogeny of gene expression and function of Xenopus transthyretin. Am. J. Physiol. 2000; 279: R2026-R2041.
    • (2000) Am. J. Physiol. , vol.279 , pp. R2026-R2041
    • Prapunpoj, P.1    Yamauchi, K.2    Nishiyama, N.3    Richardson, S.J.4    Schreiber, G.5
  • 99
    • 33748475698 scopus 로고    scopus 로고
    • Structural and functional evolution of transthyretin and transthyretin-like proteins
    • Hennebry SC, Wright HM, Likic VA, Richardson SJ. Structural and functional evolution of transthyretin and transthyretin-like proteins. Proteins 2006; 64: 1024-1045.
    • (2006) Proteins , vol.64 , pp. 1024-1045
    • Hennebry, S.C.1    Wright, H.M.2    Likic, V.A.3    Richardson, S.J.4
  • 100
    • 33745231703 scopus 로고    scopus 로고
    • The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase
    • Hennebry SC, Law RH, Richardson SJ, Buckle AM, Whisstock JC. The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase. J Mol Biol 2006; 359: 1389-1399.
    • (2006) J Mol Biol , vol.359 , pp. 1389-1399
    • Hennebry, S.C.1    Law, R.H.2    Richardson, S.J.3    Buckle, A.M.4    Whisstock, J.C.5
  • 103
    • 30744463914 scopus 로고    scopus 로고
    • Transthyretin knockouts are a new mouse model for increased neuropeptide Y
    • Nunes AF, Saraiva MJ, Sousa MM. Transthyretin knockouts are a new mouse model for increased neuropeptide Y. FASEB J 2006; 20: 166-168.
    • (2006) FASEB J , vol.20 , pp. 166-168
    • Nunes, A.F.1    Saraiva, M.J.2    Sousa, M.M.3
  • 107
    • 34848818080 scopus 로고    scopus 로고
    • Transthyretin enhances nerve regeneration
    • Fleming CE, Saraiva MJ, Sousa MM. Transthyretin enhances nerve regeneration. J Neurochem 2007; 103: 831-839.
    • (2007) J Neurochem , vol.103 , pp. 831-839
    • Fleming, C.E.1    Saraiva, M.J.2    Sousa, M.M.3
  • 108
    • 63849199799 scopus 로고    scopus 로고
    • Transthyretin internalization by sensory neurons is megalin mediated and necessary for its neuritogenic activity
    • Fleming CE, Mar FM, Franquinho F, Saraiva MJ, Sousa MM. Transthyretin internalization by sensory neurons is megalin mediated and necessary for its neuritogenic activity. J Neurosci 2009; 29: 3220-3232.
    • (2009) J Neurosci , vol.29 , pp. 3220-3232
    • Fleming, C.E.1    Mar, F.M.2    Franquinho, F.3    Saraiva, M.J.4    Sousa, M.M.5
  • 109
    • 33645314067 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein-2/megalin is expressed in oligodendrocytes in the mouse spinal cord white matter
    • Wicher G, Larsson M, Svenningsen ÅF, Gyllencreutz E, Rask L, Aldskogius H. Low density lipoprotein receptor-related protein-2/megalin is expressed in oligodendrocytes in the mouse spinal cord white matter. J Neurosci Res 2006; 83: 864-873.
    • (2006) J Neurosci Res , vol.83 , pp. 864-873
    • Wicher, G.1    Larsson, M.2    Svenningsen, A.3    Gyllencreutz, E.4    Rask, L.5    Aldskogius, H.6
  • 111
    • 0036277955 scopus 로고    scopus 로고
    • Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry
    • McCammon MG, Scott DJ, Keetch CA, Greene LH, Purkey HE, Petrassi HM, Kelly JW, Robinson CV. Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry. Structure 2002; 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
  • 112
    • 0031787160 scopus 로고    scopus 로고
    • Effects of environmental synthetic chemicals on thyroid function
    • Brucker-Davis F. Effects of environmental synthetic chemicals on thyroid function. Thyroid 1998; 8: 827-856.
    • (1998) Thyroid , vol.8 , pp. 827-856
    • Brucker-Davis, F.1
  • 113
    • 0024311332 scopus 로고
    • Drug competition for thyroxine binding to transthyretin (prealbumin): comparison with effects on thyroxine-binding globulin
    • Munro SL, Lim CF, Hall JG, Barlow JW, Craik DJ, Topliss DJ, Stockigt JR. Drug competition for thyroxine binding to transthyretin (prealbumin): comparison with effects on thyroxine-binding globulin. J Clin Endocrinol Metab 1989; 68: 1141-1147.
    • (1989) J Clin Endocrinol Metab , vol.68 , pp. 1141-1147
    • Munro, S.L.1    Lim, C.F.2    Hall, J.G.3    Barlow, J.W.4    Craik, D.J.5    Topliss, D.J.6    Stockigt, J.R.7
  • 114
    • 0026013806 scopus 로고
    • Interactions of halogenated industrial chemicals with transthyretin and effects on thyroid hormone levels in vivo
    • Van den Berg KJ, van Raaij JA, Bragt PC, Notten WR. Interactions of halogenated industrial chemicals with transthyretin and effects on thyroid hormone levels in vivo. Arch Toxicol 1991; 65: 15-19.
    • (1991) Arch Toxicol , vol.65 , pp. 15-19
    • Van den Berg, K.J.1    van Raaij, J.A.2    Bragt, P.C.3    Notten, W.R.4
  • 117
    • 0023001362 scopus 로고
    • Inhibition of rat liver iodothyronine deiodinase. Interaction of aurones with the iodothyronine ligand-binding site
    • Auf'mkolk M, Koehrle J, Hesch RD, Cody V. Inhibition of rat liver iodothyronine deiodinase. Interaction of aurones with the iodothyronine ligand-binding site. J Biol Chem 1986; 261: 11623-11630.
    • (1986) J Biol Chem , vol.261 , pp. 11623-11630
    • Auf'mkolk, M.1    Koehrle, J.2    Hesch, R.D.3    Cody, V.4
  • 118
    • 0026723625 scopus 로고
    • Crystal structure determination at 2.3-A resolution of human transthyretin-3′,5′-dibromo-2′,4,4′,6-tetrahydroxyaurone complex
    • Ciszak E, Cody V, Luft JR. Crystal structure determination at 2.3-A resolution of human transthyretin-3′, 5′-dibromo-2′, 4, 4′, 6-tetrahydroxyaurone complex. Proc Natl Acad Sci USA 1992; 89: 6644-6648.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6644-6648
    • Ciszak, E.1    Cody, V.2    Luft, J.R.3
  • 119
    • 0024386530 scopus 로고
    • Rapid effects of the flavonoid EMD 21388 on serum thyroid hormone binding and thyrotropin regulation in the rat
    • Kohrle J, Fang SL, Yang Y, Irmscher K, Hesch RD, Pino S, Alex S, Braverman LE. Rapid effects of the flavonoid EMD 21388 on serum thyroid hormone binding and thyrotropin regulation in the rat. Endocrinology 1989; 125: 532-537.
    • (1989) Endocrinology , vol.125 , pp. 532-537
    • Kohrle, J.1    Fang, S.L.2    Yang, Y.3    Irmscher, K.4    Hesch, R.D.5    Pino, S.6    Alex, S.7    Braverman, L.E.8
  • 121
    • 0015335844 scopus 로고
    • Salicylate-induced increases in free triiodothyronine in human serum. Evidence of inhibition of triiodothyronine binding to thyroxine-binding globulin and thyroxine-binding prealbumin
    • Larsen PR. Salicylate-induced increases in free triiodothyronine in human serum. Evidence of inhibition of triiodothyronine binding to thyroxine-binding globulin and thyroxine-binding prealbumin. J Clin Invest 1972; 51: 1125-1134.
    • (1972) J Clin Invest , vol.51 , pp. 1125-1134
    • Larsen, P.R.1
  • 122
    • 0036089347 scopus 로고    scopus 로고
    • A model of the development of the brain as a construct of the thyroid system
    • Howdeshell KL. A model of the development of the brain as a construct of the thyroid system. Environ Health Perspect 2002; 110: 337-348.
    • (2002) Environ Health Perspect , vol.110 , pp. 337-348
    • Howdeshell, K.L.1
  • 123
    • 0028340123 scopus 로고
    • Vulnerability of the developing brain to thyroid abnormalities: environmental insults to the thyroid system
    • Porterfield SP. Vulnerability of the developing brain to thyroid abnormalities: environmental insults to the thyroid system. Environ Health Perspect 1994; 102(Suppl.): 2125-2130.
    • (1994) Environ Health Perspect , vol.102 , pp. 2125-2130
    • Porterfield, S.P.1
  • 124
    • 0022916441 scopus 로고
    • Structurally specific binding of halogenated biphenyls to thyroxine transport protein
    • Rickenbacher U, McKinney JD, Oatley SJ, Blake CC. Structurally specific binding of halogenated biphenyls to thyroxine transport protein. J Med Chem 1986; 29: 641-648.
    • (1986) J Med Chem , vol.29 , pp. 641-648
    • Rickenbacher, U.1    McKinney, J.D.2    Oatley, S.J.3    Blake, C.C.4
  • 125
    • 0031983407 scopus 로고    scopus 로고
    • Interactions of persistent environmental organohalogens with the thyroid hormone system: mechanisms and possible consequences for animal and human health
    • Brouwer A, Morse DC, Lans MC, Schuur AG, Murk AJ, Klasson-Wehler E, Bergman A, Visser TJ. Interactions of persistent environmental organohalogens with the thyroid hormone system: mechanisms and possible consequences for animal and human health. Toxicol Ind Health 1998; 14: 59-84.
    • (1998) Toxicol Ind Health , vol.14 , pp. 59-84
    • Brouwer, A.1    Morse, D.C.2    Lans, M.C.3    Schuur, A.G.4    Murk, A.J.5    Klasson-Wehler, E.6    Bergman, A.7    Visser, T.J.8
  • 126
    • 0024308350 scopus 로고
    • Polychlorinated biphenyl (PCB)-contaminated fish induces vitamin-a and thyroid-hormone deficiency in the common seal (phoca-vitulina)
    • Brouwer A, Reijnders PJH, Koeman JH. Polychlorinated biphenyl (PCB)-contaminated fish induces vitamin-a and thyroid-hormone deficiency in the common seal (phoca-vitulina). Aquat Toxicol 1989; 15: 99-105.
    • (1989) Aquat Toxicol , vol.15 , pp. 99-105
    • Brouwer, A.1    Reijnders, P.J.H.2    Koeman, J.H.3
  • 127
    • 0031983620 scopus 로고    scopus 로고
    • Impact of PCBs on thyroid hormone directed brain development
    • Porterfield SP, Hendry LB. Impact of PCBs on thyroid hormone directed brain development. Toxicol Ind Health 1998; 14: 103-120.
    • (1998) Toxicol Ind Health , vol.14 , pp. 103-120
    • Porterfield, S.P.1    Hendry, L.B.2
  • 128
    • 3142730179 scopus 로고    scopus 로고
    • Neurodevelopment and endocrine disruption
    • Colborn T. Neurodevelopment and endocrine disruption. Environ Health Perspect 2004; 112: 944-949.
    • (2004) Environ Health Perspect , vol.112 , pp. 944-949
    • Colborn, T.1
  • 131
    • 0025176926 scopus 로고
    • Effects of in utero exposure to polychlorinated biphenyls and related contaminants on cognitive functioning in young children
    • Jacobson JL, Jacobson SW, Humphrey HE. Effects of in utero exposure to polychlorinated biphenyls and related contaminants on cognitive functioning in young children. J Pediatr 1990; 116: 38-45.
    • (1990) J Pediatr , vol.116 , pp. 38-45
    • Jacobson, J.L.1    Jacobson, S.W.2    Humphrey, H.E.3
  • 132
    • 0028819712 scopus 로고
    • Developmental exposure to polychlorinated biphenyls (Aroclor 1254) reduces circulating thyroid hormone concentrations and causes hearing deficits in rats
    • Goldey ES, Kehn LS, Lau C, Rehnberg GL, Crofton KM. Developmental exposure to polychlorinated biphenyls (Aroclor 1254) reduces circulating thyroid hormone concentrations and causes hearing deficits in rats. Toxicol Appl Pharmacol 1995; 135: 77-88.
    • (1995) Toxicol Appl Pharmacol , vol.135 , pp. 77-88
    • Goldey, E.S.1    Kehn, L.S.2    Lau, C.3    Rehnberg, G.L.4    Crofton, K.M.5
  • 133
    • 0028785470 scopus 로고
    • Effects of developmental hypothyroidism on auditory and motor function in the rat
    • Goldey ES, Kehn LS, Rehnberg GL, Crofton KM. Effects of developmental hypothyroidism on auditory and motor function in the rat. Toxicol Appl Pharmacol 1995; 135: 67-76.
    • (1995) Toxicol Appl Pharmacol , vol.135 , pp. 67-76
    • Goldey, E.S.1    Kehn, L.S.2    Rehnberg, G.L.3    Crofton, K.M.4
  • 134
    • 0031755002 scopus 로고    scopus 로고
    • Thyroxine replacement attenuates hypothyroxinemia, hearing loss, and motor deficits following developmental exposure to Aroclor 1254 in rats
    • Goldey ES, Crofton KM. Thyroxine replacement attenuates hypothyroxinemia, hearing loss, and motor deficits following developmental exposure to Aroclor 1254 in rats. Toxicol Sci 1998; 45: 94-105.
    • (1998) Toxicol Sci , vol.45 , pp. 94-105
    • Goldey, E.S.1    Crofton, K.M.2
  • 138
    • 84857709056 scopus 로고    scopus 로고
    • Clinical implications of TTR amyloidosis
    • Richardson SJ, Cody V, eds. Structure and Biological Functions: Springer-Verlag Berlin Heidelberg
    • Benson MD. Clinical implications of TTR amyloidosis. In: Richardson SJ, Cody V, eds. Recent Advances in Transthyretin Evolution. Structure and Biological Functions: Springer-Verlag Berlin Heidelberg, 2009:173-189.
    • (2009) Recent Advances in Transthyretin Evolution , pp. 173-189
    • Benson, M.D.1
  • 142
    • 22144438713 scopus 로고    scopus 로고
    • Senile systemic amyloidosis presenting with heart failure - a comparison with light chain-associated amyloidosis
    • Ng B, Connors LH, Davidoff R, Skinner M, Falk RH. Senile systemic amyloidosis presenting with heart failure - a comparison with light chain-associated amyloidosis. Arch Intern Med 2005; 165: 1425-1429.
    • (2005) Arch Intern Med , vol.165 , pp. 1425-1429
    • Ng, B.1    Connors, L.H.2    Davidoff, R.3    Skinner, M.4    Falk, R.H.5
  • 143
    • 77957180065 scopus 로고
    • A peculiar form of peripheral neuropathy familiar atypical generalized amyloidosis with special involvement of the peripheral nerves
    • Andrade C. A peculiar form of peripheral neuropathy familiar atypical generalized amyloidosis with special involvement of the peripheral nerves. Brain 1952; 75: 408-427.
    • (1952) Brain , vol.75 , pp. 408-427
    • Andrade, C.1
  • 144
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa PP, Figueira AS, Bravo FR. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci USA 1978; 75: 4499-4503.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 145
    • 34848818004 scopus 로고    scopus 로고
    • The molecular biology and clinical features of amyloid neuropathy
    • Benson MD, Kincaid JC. The molecular biology and clinical features of amyloid neuropathy. Muscle Nerve 2007; 36: 411-423.
    • (2007) Muscle Nerve , vol.36 , pp. 411-423
    • Benson, M.D.1    Kincaid, J.C.2
  • 146
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)
    • Saraiva MJ, Birken S, Costa PP, Goodman DS. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest 1984; 74: 104-119.
    • (1984) J Clin Invest , vol.74 , pp. 104-119
    • Saraiva, M.J.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 148
    • 0002470418 scopus 로고
    • Forty years of experience with type I amyloid neuropathy: review of 483 cases
    • eds Glenner, GG, Pinho e Costa, P & de Freitas F. ed. Excerpta Medica, Amsterdam
    • Coutinho P, Martins da Silva A, Lopes Lima J. Forty years of experience with type I amyloid neuropathy: review of 483 cases. In: Amyloid and Amyloidosis. eds Glenner, GG, Pinho e Costa, P & de Freitas F. ed. Excerpta Medica, Amsterdam 1980: 88-98.
    • (1980) Amyloid and Amyloidosis , pp. 88-98
    • Coutinho, P.1    Martins da Silva, A.2    Lopes Lima, J.3
  • 149
    • 0014381436 scopus 로고
    • Dissociated sensation in amyloidosis: compound action potentials; quantitative histologic and teased fibers; and electron microscopic studies of sural nerve biopsies
    • Dyck PJ, Lambert EH. Dissociated sensation in amyloidosis: compound action potentials; quantitative histologic and teased fibers; and electron microscopic studies of sural nerve biopsies. Trans Am Neurol Assoc 1968; 93: 112-115.
    • (1968) Trans Am Neurol Assoc , vol.93 , pp. 112-115
    • Dyck, P.J.1    Lambert, E.H.2
  • 150
    • 0013565530 scopus 로고
    • Pathology of the autonomic nervous system in Andrade type of familial amyloidotic polyneuropathy
    • Amyloid and Amyloidosis eds Glenner, GG, Pinho e Costa, P & de Freitas F. Excerpta Medica, Amsterdam
    • Guimarães A, Monteiro L, Coutinho P. Pathology of the autonomic nervous system in Andrade type of familial amyloidotic polyneuropathy. In: Amyloid and Amyloidosis eds Glenner, GG, Pinho e Costa, P & de Freitas F. Excerpta Medica, Amsterdam 1980: 139-146.
    • (1980) , pp. 139-146
    • Guimarães, A.1    Monteiro, L.2    Coutinho, P.3
  • 151
    • 8544219879 scopus 로고
    • Anatomie pathologique de la paramyloidose du type portugais
    • Da Silva Horta J, Trinc AOR. Anatomie pathologique de la paramyloidose du type portugais. Acta Neuropathol 1963; Suppl. II: 54-65.
    • (1963) Acta Neuropathol , pp. 54-65
    • Da Silva Horta, J.1    Trinc, A.O.R.2
  • 153
    • 1642575162 scopus 로고    scopus 로고
    • Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling
    • Sousa MM, Saraiva MJ. Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling. Prog Neurobiol 2003; 71: 385-400.
    • (2003) Prog Neurobiol , vol.71 , pp. 385-400
    • Sousa, M.M.1    Saraiva, M.J.2
  • 154
    • 0025814662 scopus 로고
    • Familial amyloidotic polyneuropathy type 1 in Kumamoto, Japan: a clinicopathologic, histochemical, immunohistochemical, and ultrastructural study
    • Takahashi K, Yi S, Kimura Y, Araki S. Familial amyloidotic polyneuropathy type 1 in Kumamoto, Japan: a clinicopathologic, histochemical, immunohistochemical, and ultrastructural study. Hum Pathol 1991; 22: 519-527.
    • (1991) Hum Pathol , vol.22 , pp. 519-527
    • Takahashi, K.1    Yi, S.2    Kimura, Y.3    Araki, S.4
  • 155
    • 0034126224 scopus 로고    scopus 로고
    • Liver transplantation for hereditary transthyretin amyloidosis
    • Suhr OB, Herlenius G, Friman S, Ericzon BG. Liver transplantation for hereditary transthyretin amyloidosis. Liver Transpl 2000; 6: 263-276.
    • (2000) Liver Transpl , vol.6 , pp. 263-276
    • Suhr, O.B.1    Herlenius, G.2    Friman, S.3    Ericzon, B.G.4
  • 156
    • 32944465275 scopus 로고    scopus 로고
    • Liver transplantation and new therapeutic approaches for familial amyloidotic polyneuropathy (FAP)
    • Ando Y. Liver transplantation and new therapeutic approaches for familial amyloidotic polyneuropathy (FAP). Med Mol Morphol 2005; 38: 142-154.
    • (2005) Med Mol Morphol , vol.38 , pp. 142-154
    • Ando, Y.1
  • 157
    • 0028539236 scopus 로고
    • Genetic analysis and a new therapy for a hereditary disease: familial amyloid polyneuropathy
    • Furihata K. Genetic analysis and a new therapy for a hereditary disease: familial amyloid polyneuropathy. Rinsho Byori 1994; 42: 1137-1143.
    • (1994) Rinsho Byori , vol.42 , pp. 1137-1143
    • Furihata, K.1
  • 158
    • 1642566049 scopus 로고    scopus 로고
    • Ten years of international experience with liver transplantation for familial amyloidotic polyneuropathy: results from the Familial Amyloidotic Polyneuropathy World Transplant Registry
    • Herlenius G, Wilczek HE, Larsson M, Ericzon BG. Ten years of international experience with liver transplantation for familial amyloidotic polyneuropathy: results from the Familial Amyloidotic Polyneuropathy World Transplant Registry. Transplantation 2004; 77: 64-71.
    • (2004) Transplantation , vol.77 , pp. 64-71
    • Herlenius, G.1    Wilczek, H.E.2    Larsson, M.3    Ericzon, B.G.4
  • 161
    • 79951681211 scopus 로고    scopus 로고
    • Variation in amount of wild-type transthyretin in different fibril and tissue types in ATTR amyloidosis
    • Ihse E, Suhr OB, Hellman U, Westermark P. Variation in amount of wild-type transthyretin in different fibril and tissue types in ATTR amyloidosis. J Mol Med 2011; 89: 171-180.
    • (2011) J Mol Med , vol.89 , pp. 171-180
    • Ihse, E.1    Suhr, O.B.2    Hellman, U.3    Westermark, P.4
  • 163
    • 35648964702 scopus 로고    scopus 로고
    • Progression of cardiac amyloid deposition in hereditary transthyretin amyloidosis patients after liver transplantation
    • Liepnieks JJ, Benson MD. Progression of cardiac amyloid deposition in hereditary transthyretin amyloidosis patients after liver transplantation. Amyloid 2007; 14: 277-282.
    • (2007) Amyloid , vol.14 , pp. 277-282
    • Liepnieks, J.J.1    Benson, M.D.2
  • 165
    • 2942599707 scopus 로고    scopus 로고
    • Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants
    • Miller SR, Sekijima Y, Kelly JW. Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants. Lab Invest 2004; 84: 545-552.
    • (2004) Lab Invest , vol.84 , pp. 545-552
    • Miller, S.R.1    Sekijima, Y.2    Kelly, J.W.3
  • 167
    • 33847641359 scopus 로고    scopus 로고
    • Transthyretin-derived amyloid deposition on the gastric mucosa in domino recipients of familial amyloid polyneuropathy liver
    • Takei Y, Gono T, Yazaki M, Ikeda S, Ikegami T, Hashikura Y, Miyagawa S, Hoshii Y. Transthyretin-derived amyloid deposition on the gastric mucosa in domino recipients of familial amyloid polyneuropathy liver. Liver Transpl 2007; 13: 215-218.
    • (2007) Liver Transpl , vol.13 , pp. 215-218
    • Takei, Y.1    Gono, T.2    Yazaki, M.3    Ikeda, S.4    Ikegami, T.5    Hashikura, Y.6    Miyagawa, S.7    Hoshii, Y.8
  • 169
    • 44949167482 scopus 로고    scopus 로고
    • Domino liver transplantation: risks and benefits
    • Ericzon BG, Larsson M, Wilczek HE. Domino liver transplantation: risks and benefits. Transplant Proc 2008; 40: 1130-1131.
    • (2008) Transplant Proc , vol.40 , pp. 1130-1131
    • Ericzon, B.G.1    Larsson, M.2    Wilczek, H.E.3
  • 170
    • 21144444931 scopus 로고    scopus 로고
    • Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation
    • Stangou AJ, Heaton ND, Hawkins PN. Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation. N Engl J Med 2005; 352: 2356.
    • (2005) N Engl J Med , vol.352 , pp. 2356
    • Stangou, A.J.1    Heaton, N.D.2    Hawkins, P.N.3
  • 172
    • 77955156168 scopus 로고    scopus 로고
    • Progression of transthyretin amyloid neuropathy after liver transplantation
    • Liepnieks JJ, Zhang LQ, Benson MD. Progression of transthyretin amyloid neuropathy after liver transplantation. Neurology 2010; 75: 324-327.
    • (2010) Neurology , vol.75 , pp. 324-327
    • Liepnieks, J.J.1    Zhang, L.Q.2    Benson, M.D.3
  • 173
    • 84896725893 scopus 로고    scopus 로고
    • Novel drugs targeting transthyretin amyloidosis
    • Hanna M. Novel drugs targeting transthyretin amyloidosis. Curr Heart Fail Rep 2014; 11: 50-57.
    • (2014) Curr Heart Fail Rep , vol.11 , pp. 50-57
    • Hanna, M.1
  • 174
    • 84883095065 scopus 로고    scopus 로고
    • A new era in the treatment of amyloidosis?
    • Lachmann HJ. A new era in the treatment of amyloidosis? N Engl J Med 2013; 369: 866-868.
    • (2013) N Engl J Med , vol.369 , pp. 866-868
    • Lachmann, H.J.1
  • 175
    • 79955453676 scopus 로고    scopus 로고
    • Making sense of therapeutics using antisense technology
    • Malik R, Roy I. Making sense of therapeutics using antisense technology. Expert Opin Drug Discov 2011; 6: 507-526.
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 507-526
    • Malik, R.1    Roy, I.2
  • 177
    • 0346333094 scopus 로고    scopus 로고
    • Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis
    • Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW. Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J Med Chem 2004; 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
  • 178
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • Johnson SM, Connelly S, Fearns C, Powers ET, Kelly JW. The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. J Mol Biol 2012; 421: 185-203.
    • (2012) J Mol Biol , vol.421 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 179
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model
    • Cardoso I, Saraiva MJ. Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model. FASEB J 2006; 20: 234-239.
    • (2006) FASEB J , vol.20 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 181
    • 0023686402 scopus 로고
    • Neural cell adhesion molecule (NCAM) and prealbumin in cerebrospinal fluid from depressed patients
    • Jorgensen OS. Neural cell adhesion molecule (NCAM) and prealbumin in cerebrospinal fluid from depressed patients. Acta Psychiatr Scand Suppl 1988; 345: 29-37.
    • (1988) Acta Psychiatr Scand Suppl , vol.345 , pp. 29-37
    • Jorgensen, O.S.1
  • 182
    • 33747881922 scopus 로고    scopus 로고
    • Low cerebrospinal fluid transthyretin levels in depression: correlations with suicidal ideation and low serotonin function
    • Sullivan GM, Mann JJ, Oquendo MA, Lo ES, Cooper TB, Gorman JM. Low cerebrospinal fluid transthyretin levels in depression: correlations with suicidal ideation and low serotonin function. Biol Psychiatry 2006; 60: 500-506.
    • (2006) Biol Psychiatry , vol.60 , pp. 500-506
    • Sullivan, G.M.1    Mann, J.J.2    Oquendo, M.A.3    Lo, E.S.4    Cooper, T.B.5    Gorman, J.M.6
  • 183
    • 0028924365 scopus 로고
    • Borderline hypothyroidism and depression
    • Haggerty JJ Jr, Prange AJ Jr. Borderline hypothyroidism and depression. Annu Rev Med 1995; 46: 37-46.
    • (1995) Annu Rev Med , vol.46 , pp. 37-46
    • Haggerty, J.J.1    Prange, A.J.2
  • 184
    • 84870234518 scopus 로고    scopus 로고
    • The link between thyroid function and depression
    • Hage MP, Azar ST. The link between thyroid function and depression. J Thyroid Res 2012; 2012: 1.
    • (2012) J Thyroid Res , vol.2012 , pp. 1
    • Hage, M.P.1    Azar, S.T.2
  • 185
    • 0017651126 scopus 로고
    • Behavioral despair in mice: a primary screening test for antidepressants
    • Porsolt RD, Bertin A, Jalfre M. Behavioral despair in mice: a primary screening test for antidepressants. Arch Int Pharmacodyn Ther 1977; 229: 327-336.
    • (1977) Arch Int Pharmacodyn Ther , vol.229 , pp. 327-336
    • Porsolt, R.D.1    Bertin, A.2    Jalfre, M.3
  • 186
    • 0024310089 scopus 로고
    • Centrally administered neuropeptide Y (NPY) produces anxiolytic-like effects in animal anxiety models
    • Heilig M, Soderpalm B, Engel JA, Widerlov E. Centrally administered neuropeptide Y (NPY) produces anxiolytic-like effects in animal anxiety models. Psychopharmacology 1989; 98: 524-529.
    • (1989) Psychopharmacology , vol.98 , pp. 524-529
    • Heilig, M.1    Soderpalm, B.2    Engel, J.A.3    Widerlov, E.4
  • 187
    • 4444346012 scopus 로고    scopus 로고
    • Differential roles for neuropeptide Y Y1 and Y5 receptors in anxiety and sedation
    • Sorensen G, Lindberg C, Wortwein G, Bolwig TG, Woldbye DP. Differential roles for neuropeptide Y Y1 and Y5 receptors in anxiety and sedation. J Neurosci Res 2004; 77: 723-729.
    • (2004) J Neurosci Res , vol.77 , pp. 723-729
    • Sorensen, G.1    Lindberg, C.2    Wortwein, G.3    Bolwig, T.G.4    Woldbye, D.P.5
  • 188
    • 0036196933 scopus 로고    scopus 로고
    • The neuropeptide Y (NPY) Y1 receptor subtype mediates NPY-induced antidepressant-like activity in the mouse forced swimming test
    • Redrobe JP, Dumont Y, Fournier A, Quirion R. The neuropeptide Y (NPY) Y1 receptor subtype mediates NPY-induced antidepressant-like activity in the mouse forced swimming test. Neuropsychopharmacology 2002; 26: 615-624.
    • (2002) Neuropsychopharmacology , vol.26 , pp. 615-624
    • Redrobe, J.P.1    Dumont, Y.2    Fournier, A.3    Quirion, R.4
  • 189
    • 34247548709 scopus 로고    scopus 로고
    • Infusion of neuropeptide Y into CA3 region of hippocampus produces antidepressant-like effect via Y1 receptor
    • Ishida H, Shirayama Y, Iwata M, Katayama S, Yamamoto A, Kawahara R, Nakagome K. Infusion of neuropeptide Y into CA3 region of hippocampus produces antidepressant-like effect via Y1 receptor. Hippocampus 2007; 17: 271-280.
    • (2007) Hippocampus , vol.17 , pp. 271-280
    • Ishida, H.1    Shirayama, Y.2    Iwata, M.3    Katayama, S.4    Yamamoto, A.5    Kawahara, R.6    Nakagome, K.7
  • 190
    • 0033732324 scopus 로고    scopus 로고
    • Behavioral insensitivity to restraint stress, absent fear suppression of behavior and impaired spatial learning in transgenic rats with hippocampal neuropeptide Y overexpression
    • Thorsell A, Michalkiewicz M, Dumont Y, Quirion R, Caberlotto L, Rimondini R, Mathe AA, Heilig M. Behavioral insensitivity to restraint stress, absent fear suppression of behavior and impaired spatial learning in transgenic rats with hippocampal neuropeptide Y overexpression. Proc Natl Acad Sci USA 2000; 97: 12852-12857.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12852-12857
    • Thorsell, A.1    Michalkiewicz, M.2    Dumont, Y.3    Quirion, R.4    Caberlotto, L.5    Rimondini, R.6    Mathe, A.A.7    Heilig, M.8
  • 192
    • 54049141743 scopus 로고    scopus 로고
    • Behavioural profile of a new mouse model for NPY deficiency
    • Karl T, Duffy L, Herzog H. Behavioural profile of a new mouse model for NPY deficiency. Eur J Neurosci 2008; 28: 173-180.
    • (2008) Eur J Neurosci , vol.28 , pp. 173-180
    • Karl, T.1    Duffy, L.2    Herzog, H.3
  • 193
    • 51449094431 scopus 로고    scopus 로고
    • Transthyretin: a key gene involved in the maintenance of memory capacities during aging
    • Brouillette J, Quirion R. Transthyretin: a key gene involved in the maintenance of memory capacities during aging. Neurobiol Aging 2008; 29: 1721-1732.
    • (2008) Neurobiol Aging , vol.29 , pp. 1721-1732
    • Brouillette, J.1    Quirion, R.2
  • 195
    • 84877742326 scopus 로고    scopus 로고
    • Transthyretin regulates hippocampal 14-3-3zeta protein levels
    • Vieira M, Saraiva MJ. Transthyretin regulates hippocampal 14-3-3zeta protein levels. FEBS Lett 2013; 587: 1482-1488.
    • (2013) FEBS Lett , vol.587 , pp. 1482-1488
    • Vieira, M.1    Saraiva, M.J.2
  • 196
    • 0035503073 scopus 로고    scopus 로고
    • Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene Leonardo
    • Philip N, Acevedo SF, Skoulakis EM. Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene Leonardo. J Neurosci 2001; 21: 8417-8425.
    • (2001) J Neurosci , vol.21 , pp. 8417-8425
    • Philip, N.1    Acevedo, S.F.2    Skoulakis, E.M.3
  • 198
    • 84904043403 scopus 로고    scopus 로고
    • Silencing of murine transthyretin and retinol binding protein genes has distinct and shared behavioral and neuropathologic effects
    • Buxbaum JN, Roberts AJ, Adame A, Masliah E. Silencing of murine transthyretin and retinol binding protein genes has distinct and shared behavioral and neuropathologic effects. Neuroscience 2014; 275: 352-364.
    • (2014) Neuroscience , vol.275 , pp. 352-364
    • Buxbaum, J.N.1    Roberts, A.J.2    Adame, A.3    Masliah, E.4
  • 199
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002; 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 200
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
    • Tanzi RE, Bertram L. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 2005; 120(4): 545-555.
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 201
    • 0028136865 scopus 로고
    • Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension
    • Jin LW, Ninomiya H, Roch JM, Schubert D, Masliah E, Otero DA, Saitoh T. Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension. J Neurosci 1994; 14: 5461-5470.
    • (1994) J Neurosci , vol.14 , pp. 5461-5470
    • Jin, L.W.1    Ninomiya, H.2    Roch, J.M.3    Schubert, D.4    Masliah, E.5    Otero, D.A.6    Saitoh, T.7
  • 203
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice
    • Meziane H, Dodart JC, Mathis C, Little S, Clemens J, Paul SM, Ungerer A. Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice. Proc Natl Acad Sci USA 1998; 95: 12683-12688.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12683-12688
    • Meziane, H.1    Dodart, J.C.2    Mathis, C.3    Little, S.4    Clemens, J.5    Paul, S.M.6    Ungerer, A.7
  • 204
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein
    • Mattson MP, Cheng B, Culwell AR, Esch FS, Lieberburg I, Rydel RE. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein. Neuron 1993; 10: 243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 205
    • 4444255624 scopus 로고    scopus 로고
    • Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis
    • Stein TD, Anders NJ, DeCarli C, Chan SL, Mattson MP, Johnson JA. Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis. J Neurosci 2004; 24: 7707-7717.
    • (2004) J Neurosci , vol.24 , pp. 7707-7717
    • Stein, T.D.1    Anders, N.J.2    DeCarli, C.3    Chan, S.L.4    Mattson, M.P.5    Johnson, J.A.6
  • 206
    • 0345307739 scopus 로고    scopus 로고
    • Genetic programming by the proteolytic fragments of the amyloid precursor protein: somewhere between confusion and clarity
    • Stein TD, Johnson JA. Genetic programming by the proteolytic fragments of the amyloid precursor protein: somewhere between confusion and clarity. Rev Neurosci 2003; 14: 317-341.
    • (2003) Rev Neurosci , vol.14 , pp. 317-341
    • Stein, T.D.1    Johnson, J.A.2
  • 207
    • 33947305482 scopus 로고    scopus 로고
    • Characterization of Abeta11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Abeta species in the pathogenesis of Alzheimer's disease
    • Liu K, Solano I, Mann D, Lemere C, Mercken M, Trojanowski JQ, Lee VM. Characterization of Abeta11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Abeta species in the pathogenesis of Alzheimer's disease. Acta Neuropathol 2006; 112: 163-174.
    • (2006) Acta Neuropathol , vol.112 , pp. 163-174
    • Liu, K.1    Solano, I.2    Mann, D.3    Lemere, C.4    Mercken, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 208
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe MS, Xia W, Moore CL, Leatherwood DD, Ostaszewski B, Rahmati T, Donkor IO, Selkoe DJ. Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 1999; 38: 4720-4727.
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3    Leatherwood, D.D.4    Ostaszewski, B.5    Rahmati, T.6    Donkor, I.O.7    Selkoe, D.J.8
  • 209
    • 0035937153 scopus 로고    scopus 로고
    • The role of presenilins in gamma-secretase activity
    • Wolfe MS, Haass C. The role of presenilins in gamma-secretase activity. J Biol Chem 2001; 276: 5413-5416.
    • (2001) J Biol Chem , vol.276 , pp. 5413-5416
    • Wolfe, M.S.1    Haass, C.2
  • 210
    • 0022973995 scopus 로고
    • Serum amysoid A protein, albumin and prealbumin in Alzheimer's disease and in demented patients with Down's syndrome
    • Elovaara I, Maury C, Palo J. Serum amysoid A protein, albumin and prealbumin in Alzheimer's disease and in demented patients with Down's syndrome. Acta Neurol Scand 1986; 74: 245-250.
    • (1986) Acta Neurol Scand , vol.74 , pp. 245-250
    • Elovaara, I.1    Maury, C.2    Palo, J.3
  • 211
    • 0024260006 scopus 로고
    • Reduced prealbumin (transthyretin) in CSF of severely demented patients with Alzheimer's disease
    • Riisøen H. Reduced prealbumin (transthyretin) in CSF of severely demented patients with Alzheimer's disease. Acta Neurol Scand 1988; 78: 455-459.
    • (1988) Acta Neurol Scand , vol.78 , pp. 455-459
    • Riisøen, H.1
  • 215
    • 81555232259 scopus 로고    scopus 로고
    • Transthyretin and the brain re-visited: is neuronal synthesis of transthyretin protective in Alzheimer's disease?
    • Li XY, Buxbaum JN. Transthyretin and the brain re-visited: is neuronal synthesis of transthyretin protective in Alzheimer's disease? Mol Neurodegener 2011; 6: 79.
    • (2011) Mol Neurodegener , vol.6 , pp. 79
    • Li, X.Y.1    Buxbaum, J.N.2
  • 216
    • 0028297520 scopus 로고
    • Epidemiology of nonaffective acute remitting psychosis vs schizophrenia - sex and sociocultural setting
    • Susser E, Wanderling J. Epidemiology of nonaffective acute remitting psychosis vs schizophrenia - sex and sociocultural setting. Arch Gen Psychiatry 1994; 51: 294-301.
    • (1994) Arch Gen Psychiatry , vol.51 , pp. 294-301
    • Susser, E.1    Wanderling, J.2
  • 217
    • 33846642542 scopus 로고    scopus 로고
    • The genetics of schizophrenia
    • Sullivan PF. The genetics of schizophrenia. PLoS Med 2005; 2: e212.
    • (2005) PLoS Med , vol.2 , pp. e212
    • Sullivan, P.F.1
  • 219
    • 0035921150 scopus 로고    scopus 로고
    • Dynamics of brain-derived proteins in cerebrospinal fluid
    • Reiber H. Dynamics of brain-derived proteins in cerebrospinal fluid. Clin Chim Acta 2001; 310: 173-186.
    • (2001) Clin Chim Acta , vol.310 , pp. 173-186
    • Reiber, H.1
  • 221
    • 33751016334 scopus 로고    scopus 로고
    • Dysregulation of retinoid transporters expression in body fluids of schizophrenia patients
    • Wan C, Yang Y, Li H, La Y, Zhu H, Jiang L, Chen Y, Feng G, He L. Dysregulation of retinoid transporters expression in body fluids of schizophrenia patients. J Proteome Res 2006; 5: 3213-3216.
    • (2006) J Proteome Res , vol.5 , pp. 3213-3216
    • Wan, C.1    Yang, Y.2    Li, H.3    La, Y.4    Zhu, H.5    Jiang, L.6    Chen, Y.7    Feng, G.8    He, L.9
  • 222
    • 33750695928 scopus 로고    scopus 로고
    • Comparative proteome analysis revealed up-regulation of transthyretin in rat brain under chronic clozapine treatment
    • Chen ML, Chen CH. Comparative proteome analysis revealed up-regulation of transthyretin in rat brain under chronic clozapine treatment. J Psychiatr Res 2007; 41: 63-68.
    • (2007) J Psychiatr Res , vol.41 , pp. 63-68
    • Chen, M.L.1    Chen, C.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.