메뉴 건너뛰기




Volumn 1832, Issue 8, 2013, Pages 1183-1193

Hepatic production of transthyretin L12P leads to intracellular lysosomal aggregates in a new somatic transgenic mouse model

Author keywords

Cellular models; Intracellular aggregation; Leptomeningeal amyloidosis; Lysosomes; N glycosylation; Transthyretin

Indexed keywords

PREALBUMIN;

EID: 84877340049     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2013.04.001     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 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
  • 4
    • 0030075631 scopus 로고    scopus 로고
    • Leptomeningeal amyloid and variant transthyretins
    • Benson M.D. Leptomeningeal amyloid and variant transthyretins. Am. J. Pathol. 1996, 148:351-354.
    • (1996) Am. J. Pathol. , vol.148 , pp. 351-354
    • Benson, M.D.1
  • 5
    • 0037344272 scopus 로고    scopus 로고
    • Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology
    • Sekijima Y., Hammarström P., Matsumura M., Shimizu Y., Iwata M., Tokuda T., Ikeda S.-I., Kelly J.W. Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology. Lab. Invest. 2003, 83:409-417.
    • (2003) Lab. Invest. , vol.83 , pp. 409-417
    • Sekijima, Y.1    Hammarström, P.2    Matsumura, M.3    Shimizu, Y.4    Iwata, M.5    Tokuda, T.6    Ikeda, S.-I.7    Kelly, J.W.8
  • 6
  • 7
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A., Vaz D.C., Cardoso I., Saraiva M.J., Brito R.M. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J. Biol. Chem. 2001, 276:27207-27213.
    • (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
  • 10
    • 36348960658 scopus 로고    scopus 로고
    • Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design
    • Cardoso I., Almeida M.R., Ferreira N., Arsequell G., Valencia G., Saraiva M.J. Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design. Biochem. J. 2007, 408:131-138.
    • (2007) Biochem. J. , vol.408 , pp. 131-138
    • Cardoso, I.1    Almeida, M.R.2    Ferreira, N.3    Arsequell, G.4    Valencia, G.5    Saraiva, M.J.6
  • 13
    • 33845970263 scopus 로고    scopus 로고
    • Complete correction of enzymatic deficiency and neurochemistry in the GM1-gangliosidosis mouse brain by neonatal adeno-associated virus-mediated gene delivery
    • Broekman M.L., Baek R.C., Comer L.A., Fernandez J.L., Seyfried T.N., Sena-Esteves M. Complete correction of enzymatic deficiency and neurochemistry in the GM1-gangliosidosis mouse brain by neonatal adeno-associated virus-mediated gene delivery. Mol. Ther. 2007, 15:30-37.
    • (2007) Mol. Ther. , vol.15 , pp. 30-37
    • Broekman, M.L.1    Baek, R.C.2    Comer, L.A.3    Fernandez, J.L.4    Seyfried, T.N.5    Sena-Esteves, M.6
  • 14
    • 33645528206 scopus 로고    scopus 로고
    • Self-complementary adeno-associated virus vectors containing a novel liver-specific human factor IX expression cassette enable highly efficient transduction of murine and nonhuman primate liver
    • Nathwani A.C., Gray J.T., Ng C.Y., Zhou J., Spence Y., Waddington S.N., Tuddenham E.G., Kemball-Cook G., McIntosh J., Boon-Spijker M., Mertens K., Davidoff A.M. Self-complementary adeno-associated virus vectors containing a novel liver-specific human factor IX expression cassette enable highly efficient transduction of murine and nonhuman primate liver. Blood 2006, 107:2653-2661.
    • (2006) Blood , vol.107 , pp. 2653-2661
    • Nathwani, A.C.1    Gray, J.T.2    Ng, C.Y.3    Zhou, J.4    Spence, Y.5    Waddington, S.N.6    Tuddenham, E.G.7    Kemball-Cook, G.8    McIntosh, J.9    Boon-Spijker, M.10    Mertens, K.11    Davidoff, A.M.12
  • 15
    • 0346777307 scopus 로고    scopus 로고
    • Adeno-associated virus terminal repeat (TR) mutant generates self-complementary vectors to overcome the rate-limiting step to transduction in vivo
    • McCarty D.M., Fu H., Monahan P.E., Toulson C.E., Naik P., Samulski R.J. Adeno-associated virus terminal repeat (TR) mutant generates self-complementary vectors to overcome the rate-limiting step to transduction in vivo. Gene Ther. 2003, 10:2112-2118.
    • (2003) Gene Ther. , vol.10 , pp. 2112-2118
    • McCarty, D.M.1    Fu, H.2    Monahan, P.E.3    Toulson, C.E.4    Naik, P.5    Samulski, R.J.6
  • 16
    • 32844456598 scopus 로고    scopus 로고
    • Adeno-associated virus vectors serotyped with AAV8 capsid are more efficient than AAV-1 or -2 serotypes for widespread gene delivery to the neonatal mouse brain
    • Broekman M.L., Comer L.A., Hyman B.T., Sena-Esteves M. Adeno-associated virus vectors serotyped with AAV8 capsid are more efficient than AAV-1 or -2 serotypes for widespread gene delivery to the neonatal mouse brain. Neuroscience 2006, 138:501-510.
    • (2006) Neuroscience , vol.138 , pp. 501-510
    • Broekman, M.L.1    Comer, L.A.2    Hyman, B.T.3    Sena-Esteves, M.4
  • 19
    • 0021996005 scopus 로고
    • Rat transthyretin (prealbumin). Molecular cloning, nucleotide sequence, and gene expression in liver and brain
    • Dickson P.W., Howlett G.J., 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
  • 20
    • 0035109551 scopus 로고    scopus 로고
    • Conditionally immortalized cell lines as a new in vitro model for the study of barrier functions
    • Terasaki T., Hosoya K. Conditionally immortalized cell lines as a new in vitro model for the study of barrier functions. Biol. Pharm. Bull. 2001, 24:111-118.
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 111-118
    • Terasaki, T.1    Hosoya, K.2
  • 21
    • 18144366620 scopus 로고    scopus 로고
    • HEK293 cell line: a vehicle for the expression of recombinant proteins
    • Thomas P., Smart T.G. HEK293 cell line: a vehicle for the expression of recombinant proteins. J. Pharmacol. Toxicol. Methods 2005, 51:187-200.
    • (2005) J. Pharmacol. Toxicol. Methods , vol.51 , pp. 187-200
    • Thomas, P.1    Smart, T.G.2
  • 22
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., Tsien R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 1998, 281:269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 23
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., Adams S.R., Jones J., Tsien R.Y. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol. 2000, 327:565-578.
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 24
    • 0038661338 scopus 로고    scopus 로고
    • D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?
    • Hammarström P., Sekijima Y., White J.T., Wiseman R.L., Lim A., Costello C.E., Altland K., Garzuly F., Budka H., Kelly J.W. D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?. Biochemistry 2003, 42:6656-6663.
    • (2003) Biochemistry , vol.42 , pp. 6656-6663
    • Hammarström, P.1    Sekijima, Y.2    White, J.T.3    Wiseman, R.L.4    Lim, A.5    Costello, C.E.6    Altland, K.7    Garzuly, F.8    Budka, H.9    Kelly, J.W.10
  • 26
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • Parekh R.B., Tse A.G., Dwek R.A., Williams A.F., Rademacher T.W. Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. EMBO J. 1987, 6:1233-1244.
    • (1987) EMBO J. , vol.6 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 28
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001, 29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 30
    • 80051681133 scopus 로고    scopus 로고
    • Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity
    • Wang S., Thibault G., Ng D.T. Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity. J. Biol. Chem. 2011, 286:29376-29387.
    • (2011) J. Biol. Chem. , vol.286 , pp. 29376-29387
    • Wang, S.1    Thibault, G.2    Ng, D.T.3
  • 31
    • 0024978029 scopus 로고
    • Role of acidic intracellular compartments in the biosynthesis of dictyostelium lysosomal enzymes. The weak bases ammonium chloride and chloroquine differentially affect proteolytic processing and sorting
    • Cardelli J.A., Richardson J., Miears D. Role of acidic intracellular compartments in the biosynthesis of dictyostelium lysosomal enzymes. The weak bases ammonium chloride and chloroquine differentially affect proteolytic processing and sorting. J. Biol. Chem. 1989, 264:3454-3463.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3454-3463
    • Cardelli, J.A.1    Richardson, J.2    Miears, D.3
  • 32
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T., Sitia R. Protein quality control in the early secretory pathway. EMBO J. 2008, 27:315-327.
    • (2008) EMBO J. , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 33
    • 70449640181 scopus 로고    scopus 로고
    • Quality control against misfolded proteins in the cytosol: a network for cell survival
    • Kubota H. Quality control against misfolded proteins in the cytosol: a network for cell survival. J. Biochem. 2009, 146:609-616.
    • (2009) J. Biochem. , vol.146 , pp. 609-616
    • Kubota, H.1
  • 34
    • 67649745807 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation of transthyretin variants is negatively regulated by BiP in mammalian cells
    • Susuki S., Sato T., Miyata M., Momohara M., Suico M.A., Shuto T., Ando Y., Kai H. The endoplasmic reticulum-associated degradation of transthyretin variants is negatively regulated by BiP in mammalian cells. J. Biol. Chem. 2009, 284:8312-8321.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8312-8321
    • Susuki, S.1    Sato, T.2    Miyata, M.3    Momohara, M.4    Suico, M.A.5    Shuto, T.6    Ando, Y.7    Kai, H.8
  • 37
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 2004, 4:454-465.
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wisniewski, J.R.4
  • 38
    • 38849103042 scopus 로고    scopus 로고
    • Detection of a gamma-carboxy-glutamate as novel post-translational modification of human transthyretin
    • Ruggeberg S., Horn P., Li X., Vajkoczy P., Franz T. Detection of a gamma-carboxy-glutamate as novel post-translational modification of human transthyretin. Protein Pept. Lett. 2008, 15:43-46.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 43-46
    • Ruggeberg, S.1    Horn, P.2    Li, X.3    Vajkoczy, P.4    Franz, T.5
  • 40
    • 84875784710 scopus 로고    scopus 로고
    • Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD
    • Teixeira A.C., Saraiva M.J. Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD. J. Cell. Mol. Med. 2013, 17:429-443.
    • (2013) J. Cell. Mol. Med. , vol.17 , pp. 429-443
    • Teixeira, A.C.1    Saraiva, M.J.2
  • 42
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: a close look at thermodynamic stabilization
    • Shental-Bechor D., Levy Y. Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:8256-8261.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 43
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada C., Kelleher D.J., Gilmore R. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 2009, 136:272-283.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 45
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A.M., Stefanis L., Fredenburg R., Lansbury P.T., Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 46
    • 0038015531 scopus 로고    scopus 로고
    • Modeling CNS neurodegeneration by overexpression of disease-causing proteins using viral vectors
    • Kirik D., Bjorklund A. Modeling CNS neurodegeneration by overexpression of disease-causing proteins using viral vectors. Trends Neurosci. 2003, 26:386-392.
    • (2003) Trends Neurosci. , vol.26 , pp. 386-392
    • Kirik, D.1    Bjorklund, A.2
  • 47
    • 0022338373 scopus 로고
    • Biochemical marker in familial amyloidotic polyneuropathy, Portuguese type. Family studies on the transthyretin (prealbumin)-methionine-30 variant
    • Saraiva M.J., Costa P.P., Goodman D.S. Biochemical marker in familial amyloidotic polyneuropathy, Portuguese type. Family studies on the transthyretin (prealbumin)-methionine-30 variant. J. Clin. Invest. 1985, 76:2171-2177.
    • (1985) J. Clin. Invest. , vol.76 , pp. 2171-2177
    • Saraiva, M.J.1    Costa, P.P.2    Goodman, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.