메뉴 건너뛰기




Volumn 26, Issue 6, 2012, Pages 2283-2293

Why are some amyloidoses systemic? Does hepatic "chaperoning at a distance" prevent cardiac deposition in a transgenic model of human senile systemic (transthyretin) amyloidosis?

Author keywords

Microarrays; Protein misfolding diseases

Indexed keywords

ANTIOXIDANT; CHAPERONE; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 40; PREALBUMIN; PROTEASOME; PROTEINASE; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 84861772766     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-189571     Document Type: Article
Times cited : (60)

References (37)
  • 1
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010 Recommendations from the nomenclature committee of the International Society of Amyloidosis
    • Sipe, J. D., Benson, M. D., Buxbaum, J. N., Ikeda, S., Merlini, G., Saraiva, M. J., and Westermark, P. (2010) Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid 17, 101-104
    • (2010) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008) Adapting proteostasis for disease intervention. Science 319, 916-919 (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 5
    • 36049032748 scopus 로고    scopus 로고
    • An Adaptable Standard for Protein Export from the Endoplasmic Reticulum
    • DOI 10.1016/j.cell.2007.10.025, PII S0092867407013438
    • Wiseman, R. L., Powers, E. T., Buxbaum, J. N., Kelly, J. W., and Balch, W. E. (2007) An adaptable standard for protein export from the endoplasmic reticulum. Cell 131, 809-821 (Pubitemid 350087203)
    • (2007) Cell , vol.131 , Issue.4 , pp. 809-821
    • Wiseman, R.L.1    Powers, E.T.2    Buxbaum, J.N.3    Kelly, J.W.4    Balch, W.E.5
  • 6
    • 70349323359 scopus 로고    scopus 로고
    • Transthyretin and the transthyretin amyloidoses
    • Uversky, V. N., and Fink, A., eds. . Springer, Santa Cruz, CA, USA
    • Buxbaum, J. N. (2007) Transthyretin and the transthyretin amyloidoses. In Protein Misfolding, Aggregation, and Conformational Diseases (Uversky, V. N., and Fink, A., eds.) pp. 259-283, Springer, Santa Cruz, CA, USA
    • (2007) Protein Misfolding, Aggregation, and Conformational Diseases , pp. 259-283
    • Buxbaum, J.N.1
  • 7
    • 0033780005 scopus 로고    scopus 로고
    • Pathology of familial amyloidotic polyneuropathy with TTR met 30 in Kumamoto, Japan
    • Araki, S., and Yi, S. (2000) Pathology of familial amyloidotic polyneuropathy with TTR met 30 in Kumamoto, Japan. Neuropathology 20(Suppl.), S47-S51
    • (2000) Neuropathology , vol.20 , Issue.SUPPL.
    • Araki, S.1    Yi, S.2
  • 8
    • 0016705572 scopus 로고
    • Postmortem findings in primary familial amyloidosis with polyneuropathy
    • Hofer, P. A., and Anderson, R. (1975) Postmortem findings in primary familial amyloidosis with polyneuropathy. Acta Pathol. Microbiol. Scand. A 83, 309-322
    • (1975) Acta Pathol. Microbiol. Scand. A , vol.83 , pp. 309-322
    • Hofer, P.A.1    Anderson, R.2
  • 12
    • 23944458138 scopus 로고    scopus 로고
    • A general framework for weighted gene co-expression network analysis
    • Article 17
    • Zhang, B., and Horvath, S. (2005) A general framework for weighted gene co-expression network analysis. Stat. Appl. Genet. Mol. Biol. 4, Article 17
    • (2005) Stat. Appl. Genet. Mol. Biol. , vol.4
    • Zhang, B.1    Horvath, S.2
  • 13
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang, K., and Kaufman, R. J. (2006) Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb. Exp. Pharmacol. 69-91
    • (2006) Handb. Exp. Pharmacol. , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 14
    • 31344438651 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the making of a professional secretory cell
    • DOI 10.1080/10409230500315352
    • Van Anken, E., and Braakman, I. (2005) Endoplasmic reticulum stress and the making of a professional secretory cell. Crit. Rev. Biochem. Molec. Biol. 40, 269-283 (Pubitemid 43142394)
    • (2005) Critical Reviews in Biochemistry and Molecular Biology , vol.40 , Issue.5 , pp. 269-283
    • Van Anken, E.1    Braakman, I.2
  • 15
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., and Balch, W. E. (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78, 959-991
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4    Balch, W.E.5
  • 16
    • 0025963347 scopus 로고
    • Systemic amyloidosis in transgenic mice carrying the human mutant transthyretin (Met30) gene: Pathologic similarity to human familial amyloidotic polyneuropathy, type I
    • Yi, S., Takahashi, K., Naito, M., Tashiro, F., Wakasugi, S., Maeda, S., Shimada, K., Yamamura, K., and Araki, S. (1991) Systemic amyloidosis in transgenic mice carrying the human mutant transthyretin (Met30) gene: Pathologic similarity to human familial amyloidotic polyneuropathy, type I. Am. J. Pathol. 138, 403-412
    • (1991) Am. J. Pathol. , vol.138 , pp. 403-412
    • Yi, S.1    Takahashi, K.2    Naito, M.3    Tashiro, F.4    Wakasugi, S.5    Maeda, S.6    Shimada, K.7    Yamamura, K.8    Araki, S.9
  • 17
    • 71349088766 scopus 로고    scopus 로고
    • The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems
    • Santos, S. D., Fernandes, R., and Saraiva, M. J. (2010) The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems. Neurobiol. Aging 31, 280-289
    • (2010) Neurobiol. Aging , vol.31 , pp. 280-289
    • Santos, S.D.1    Fernandes, R.2    Saraiva, M.J.3
  • 18
    • 38349085003 scopus 로고    scopus 로고
    • Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins
    • Reixach, N., Foss, T. R., Santelli, E., Pascual, J., Kelly, J. W., and Buxbaum, J. N. (2008) Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins. J. Biol. Chem. 283, 2098-2107
    • (2008) J. Biol. Chem. , vol.283 , pp. 2098-2107
    • Reixach, N.1    Foss, T.R.2    Santelli, E.3    Pascual, J.4    Kelly, J.W.5    Buxbaum, J.N.6
  • 19
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • Hollien, J., Lin, J. H., Li, H., Stevens, N., Walter, P., and Weissman, J. S. (2009) Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J. Cell Biol. 186, 323-331
    • (2009) J. Cell Biol. , vol.186 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 20
    • 34249076067 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell
    • DOI 10.1038/sj.emboj.7601685, PII 7601685
    • Sato, T., Susuki, S., Suico, M. A., Miyata, M., Ando, Y., Mizuguchi, M., Takeuchi, M., Dobashi, M., Shuto, T., and Kai, H. (2007) Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell. EMBO J. 26, 2501-2512 (Pubitemid 46788312)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2501-2512
    • Sato, T.1    Susuki, S.2    Suico, M.A.3    Miyata, M.4    Ando, Y.5    Mizuguchi, M.6    Takeuchi, M.7    Dobashi, M.8    Shuto, T.9    Kai, H.10
  • 21
    • 34548647535 scopus 로고    scopus 로고
    • TRB3 protects cells against the growth inhibitory and cytotoxic effect of ATF4
    • DOI 10.1016/j.yexcr.2007.07.017, PII S0014482707003515
    • Ord, D., Meerits, K., and Ord, T. (2007) TRB3 protects cells against the growth inhibitory and cytotoxic effect of ATF4. Exp. Cell Res. 313, 3556-3567 (Pubitemid 47404553)
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , pp. 3556-3567
    • Ord, D.1    Meerits, K.2    Ord, T.3
  • 23
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka, N. (2005) TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J. 24, 1243-1255
    • (2005) EMBO J. , vol.24 , pp. 1243-1255
    • Ohoka, N.1
  • 24
    • 33845692825 scopus 로고    scopus 로고
    • Tribbles: A family of kinase-like proteins with potent signalling regulatory function
    • Hegedus, Z. (2007) Tribbles: a family of kinase-like proteins with potent signalling regulatory function. Cell. Signal. 19, 238-250
    • (2007) Cell. Signal. , vol.19 , pp. 238-250
    • Hegedus, Z.1
  • 25
    • 78149434112 scopus 로고    scopus 로고
    • The Nrf2 system as a potential target for the development of indirect antioxidants
    • Jung, K. A., and Kwak, M. K. (2010) The Nrf2 system as a potential target for the development of indirect antioxidants. Molecules 15, 7266-7291
    • (2010) Molecules , vol.15 , pp. 7266-7291
    • Jung, K.A.1    Kwak, M.K.2
  • 26
    • 33746814859 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress associated with extracellular aggregates: Evidence from transthyretin deposition in familial amyloid polyneuropathy
    • DOI 10.1074/jbc.M602302200
    • Teixeira, P. F., Cerca, F., Santos, S. D., and Saraiva, M. J. (2006) Endoplasmic reticulum stress associated with extracellular aggregates. Evidence from transthyretin deposition in familial amyloid polyneuropathy. J. Biol. Chem. 281, 21998-22003 (Pubitemid 44181903)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 21998-22003
    • Teixeira, P.F.1    Cerca, F.2    Santos, S.D.3    Saraiva, M.J.4
  • 27
    • 32644432826 scopus 로고    scopus 로고
    • pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
    • DOI 10.1083/jcb.200508145
    • Yoshida, H., Oku, M., Suzuki, M., and Mori, K. (2006) pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J. Cell Biol. 172, 565-575 (Pubitemid 43243877)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4
  • 28
    • 63649157914 scopus 로고    scopus 로고
    • pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation
    • Yoshida, H., Uemura, A., and Mori, K. (2009) pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation. Cell Struct. Funct. 34, 1-10
    • (2009) Cell Struct. Funct. , vol.34 , pp. 1-10
    • Yoshida, H.1    Uemura, A.2    Mori, K.3
  • 29
    • 79953210362 scopus 로고    scopus 로고
    • Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis
    • Fernandez-Marcos, P. J., and Auwerx, J. (2011) Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis. Am. J. Clin. Nutr. 93, 884S-890S
    • (2011) Am. J. Clin. Nutr. , vol.93
    • Fernandez-Marcos, P.J.1    Auwerx, J.2
  • 30
    • 44649151707 scopus 로고    scopus 로고
    • The PPAR trio: Regulators of myocardial energy metabolism in health and disease
    • Madrazo, J. A., and Kelly, D. P. (2008) The PPAR trio: regulators of myocardial energy metabolism in health and disease. J. Mol. Cell. Cardiol. 44, 968-975
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 968-975
    • Madrazo, J.A.1    Kelly, D.P.2
  • 31
    • 77950900273 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible genes by PGC-1 alpha
    • Shoag, J., and Arany, Z. (2010) Regulation of hypoxia-inducible genes by PGC-1 alpha. Arterioscler. Thromb. Vasc. Biol. 30, 662-666
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 662-666
    • Shoag, J.1    Arany, Z.2
  • 32
  • 33
    • 11244280869 scopus 로고    scopus 로고
    • Up-regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase-associated lipocalin, and matrix metalloproteinase-9 in familial amyloid polyneuropathy
    • DOI 10.1096/fj.04-2022fje
    • Sousa, M. M., do Amaral, J. B., Guimaraes, A., and Saraiva, M. J. (2005) Up-regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase-associated lipocalin, and matrix metalloproteinase-9 in familial amyloid polyneuropathy. FASEB J. 19, 124-126 (Pubitemid 40069939)
    • (2005) FASEB Journal , vol.19 , Issue.1 , pp. 124-126
    • Sousa, M.M.1    Do, A.J.B.2    Guimaraes, A.3    Saraiva, M.J.4
  • 34
    • 21144444931 scopus 로고    scopus 로고
    • Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation
    • DOI 10.1056/NEJM200506023522219
    • Stangou, A. J., Heaton, N. D., and Hawkins, P. N. (2005) Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation. N. Engl. J. Med. 352, 2356 (Pubitemid 40740565)
    • (2005) New England Journal of Medicine , vol.352 , Issue.22 , pp. 2356
    • Stangou, A.J.1    Heaton, N.D.2    Hawkins, P.N.3
  • 35
    • 33847641359 scopus 로고    scopus 로고
    • Transthyretin-derived amyloid deposition on the gastric mucosa in domino recipients of familial amyloid polyneuropathy liver
    • DOI 10.1002/lt.20954
    • Takei, Y., Gono, T., Yazaki, M., Ikeda, S., Ikegami, T., Hashikura, Y., Miyagawa, S., and Hoshii, Y. (2007) Transthyretin-derived amyloid deposition on the gastric mucosa in domino recipients of familial amyloid polyneuropathy liver. Liver Transpl. 13, 215-218 (Pubitemid 46351646)
    • (2007) Liver Transplantation , vol.13 , Issue.2 , pp. 215-218
    • Takei, Y.-I.1    Gono, T.2    Yazaki, M.3    Ikeda, S.-I.4    Ikegami, T.5    Hashikura, Y.6    Miyagawa, S.-I.7    Hoshii, Y.8
  • 36
    • 35148837588 scopus 로고    scopus 로고
    • Long-term consequences of domino liver transplantation using familial amyloidotic polyneuropathy grafts
    • DOI 10.1111/j.1432-2277.2007.00516.x
    • Yamamoto, S., Wilczek, H. E., Iwata, T., Larsson, M., Gjertsen, H., Soderdahl, G., Solders, G., and Ericzon, B. G. (2007) Long-term consequences of domino liver transplantation using familial amyloidotic polyneuropathy grafts. Transpl. Int. 20, 926-933 (Pubitemid 47537564)
    • (2007) Transplant International , vol.20 , Issue.11 , pp. 926-933
    • Yamamoto, S.1    Wilczek, H.E.2    Iwata, T.3    Larsson, M.4    Gjertsen, H.5    Soderdahl, G.6    Solders, G.7    Ericzon, B.-G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.