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Volumn 118, Issue 25, 2011, Pages 6610-6617

Doxycycline reduces fibril formation in a transgenic mouse model of AL amyloidosis

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN FIBRIL; DOXYCYCLINE; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 84055223035     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2011-04-351643     Document Type: Article
Times cited : (122)

References (50)
  • 1
    • 79955842001 scopus 로고    scopus 로고
    • Amyloidosis: Pathogenesis and new therapeutic options
    • Merlini G, Seldin DC, Gertz MA. Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol. 2011;29(14)1924-1933.
    • (2011) J Clin Oncol , vol.29 , Issue.14 , pp. 1924-1933
    • Merlini, G.1    Seldin, D.C.2    Gertz, M.A.3
  • 2
    • 0027080695 scopus 로고
    • Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition
    • Kisilevsky R. Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition. J Intern Med. 1992;232(6):515-516. (Pubitemid 23024322)
    • (1992) Journal of Internal Medicine , vol.232 , Issue.6 , pp. 515-516
    • Kisilevsky, R.1
  • 3
    • 84055175539 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: Two possible avenues for therapy
    • Pepys MB, Tennent GA, Booth DR, et al. Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy. Ciba Found Symp. 1996;19973-19981.
    • (1996) Ciba Found Symp , pp. 19973-19981
    • Pepys, M.B.1    Tennent, G.A.2    Booth, D.R.3
  • 4
    • 2342525940 scopus 로고    scopus 로고
    • Human Amyloidogenic Light Chains Directly Impair Cardiomyocyte Function Through an Increase in Cellular Oxidant Stress
    • DOI 10.1161/01.RES.0000126569.75419.74
    • Brenner DA, Jain M, Pimentel DR, et al. Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress. Circ Res. 2004;94(8):1008-1010. (Pubitemid 38579694)
    • (2004) Circulation Research , vol.94 , Issue.8 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3    Wang, B.4    Connors, L.H.5    Skinner, M.6    Apstein, C.S.7    Liao, R.8
  • 5
    • 0035797855 scopus 로고    scopus 로고
    • Infusion of light chains from patients with cardiac amyloidosis causes diastolic dysfunction in isolated mouse hearts
    • Liao R, Jain M, Teller P, et al. Infusion of light chains from patients with cardiac amyloidosis causes diastolic dysfunction in isolated mouse hearts. Circulation. 2001;104(14):1594-1597. (Pubitemid 32947519)
    • (2001) Circulation , vol.104 , Issue.14 , pp. 1594-1597
    • Liao, R.1    Jain, M.2    Teller, P.3    Connors, L.H.4    Ngoy, S.5    Skinner, M.6    Falk, R.H.7    Apstein, C.S.8
  • 8
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300(5618):486-489. (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 10
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • Walsh DM, Selkoe DJ. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett. 2004;11(3):213-228. (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 11
    • 0026534711 scopus 로고
    • Induction in mice of human light-chain-associated amyloidosis
    • Solomon A, Weiss DT, Pepys MB. Induction in mice of human light-chain-associated amyloidosis. Am J Pathol. 1992;140(3):629-637.
    • (1992) Am J Pathol , vol.140 , Issue.3 , pp. 629-637
    • Solomon, A.1    Weiss, D.T.2    Pepys, M.B.3
  • 12
    • 83255185724 scopus 로고    scopus 로고
    • Preclinical development of siRNA therapeutics for AL amyloidosis
    • [published online ahead of print May 12, 2011]. doi:10.1038/gt.2011.69
    • Hovey BM, Ward JE, Soo Hoo PT, O'Hara CJ, Connors LH, Seldin DC. Preclinical development of siRNA therapeutics for AL amyloidosis [published online ahead of print May 12, 2011]. Gene Therapy. doi:10.1038/gt.2011.69.
    • Gene Therapy
    • Hovey, B.M.1    Ward, J.E.2    Soo Hoo, P.T.3    O'Hara, C.J.4    Connors, L.H.5    Seldin, D.C.6
  • 13
    • 0028955645 scopus 로고
    • Amino acid sequence based PCR primers for amplification of rearranged human heavy and light chain immunoglobulin variable region genes
    • Welschof M, Terness P, Kolbinger F, et al. Amino acid sequence based PCR primers for amplification of rearranged human heavy and light chain immunoglobulin variable region genes. J Immunol Methods. 1995;179(2):203-214.
    • (1995) J Immunol Methods , vol.179 , Issue.2 , pp. 203-214
    • Welschof, M.1    Terness, P.2    Kolbinger, F.3
  • 14
    • 33749620423 scopus 로고    scopus 로고
    • Merger of laser capture microdissection and mass spectrometry: A window into the amyloid plaque proteome
    • Gozal YM, Cheng D, Duong DM, Lah JJ, Levey AI, Peng J. Merger of laser capture microdissection and mass spectrometry: a window into the amyloid plaque proteome. Methods Enzymol. 2006;41277-41293.
    • (2006) Methods Enzymol , pp. 41277-41293
    • Gozal, Y.M.1    Cheng, D.2    Duong, D.M.3    Lah, J.J.4    Levey, A.I.5    Peng, J.6
  • 15
    • 78149425311 scopus 로고    scopus 로고
    • The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain
    • Klimtchuk ES, Gursky O, Patel RS, et al. The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain. Biochem. 2010;49(45):9848-9857.
    • (2010) Biochem , vol.49 , Issue.45 , pp. 9848-9857
    • Klimtchuk, E.S.1    Gursky, O.2    Patel, R.S.3
  • 17
    • 0020308923 scopus 로고
    • The association of amyloid P-component (AP) with the amyloid fibril: An updated method for amyloid fibril protein isolation
    • Skinner M, Shirahama T, Cohen AS, Deal CL. The association of amyloid P-component (AP) with the amyloid fibril: an updated method for amyloid fibril protein isolation. Prep Biochem. 1982;12(5):461-476. (Pubitemid 13134726)
    • (1982) Preparative Biochemistry , vol.12 , Issue.5 , pp. 461-476
    • Skinner, M.1    Shirahama, T.2    Cohen, A.S.3    Deal, C.L.4
  • 18
    • 78549247499 scopus 로고    scopus 로고
    • Role of glycosaminoglycan sulfation in the formation of immunoglobulin light chain amyloid oligomers and fibrils
    • Ren R, Hong Z, Gong H, et al. Role of glycosaminoglycan sulfation in the formation of immunoglobulin light chain amyloid oligomers and fibrils. J Biol Chem. 2010;285(48):37672-37682.
    • (2010) J Biol Chem , vol.285 , Issue.48 , pp. 37672-37682
    • Ren, R.1    Hong, Z.2    Gong, H.3
  • 19
    • 0037109094 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of GLUT1 prevents the development of heart failure attributable to pressure overload in mice
    • DOI 10.1161/01.CIR.0000034049.61181.F3
    • Liao R, Jain M, Cui L, et al. Cardiac-specific overexpression of GLUT1 prevents the development of heart failure attributable to pressure overload in mice. Circulation. 2002;106(16):2125-2131. (Pubitemid 35192820)
    • (2002) Circulation , vol.106 , Issue.16 , pp. 2125-2131
    • Liao, R.1    Jain, M.2    Cui, L.3    D'Agostino, J.4    Aiello, F.5    Luptak, I.6    Ngoy, S.7    Mortensen, R.M.8    Tian, R.9
  • 22
    • 2342561865 scopus 로고    scopus 로고
    • Motor neurons rely on motor proteins
    • DOI 10.1016/j.tcb.2004.03.009, PII S0962892404000832
    • Holzbaur EL. Motor neurons rely on motor proteins. Trends Cell Biol. 2004;14(5):233-240. (Pubitemid 38591327)
    • (2004) Trends in Cell Biology , vol.14 , Issue.5 , pp. 233-240
    • Holzbaur, E.L.F.1
  • 24
    • 77749251993 scopus 로고    scopus 로고
    • Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38alpha MAPK pathway
    • Shi J, Guan J, Jiang B, et al. Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38alpha MAPK pathway. Proc Natl Acad Sci U S A. 2010;107(9):4188-4193.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.9 , pp. 4188-4193
    • Shi, J.1    Guan, J.2    Jiang, B.3
  • 25
    • 84055175537 scopus 로고    scopus 로고
    • Contribution of light chain variable region genes to organ tropism and survival in AL amyloidosis
    • Prokaeva T, Spencer B, Doros G, Connors LH, Skinner M, Seldin DC. Contribution of light chain variable region genes to organ tropism and survival in AL amyloidosis. Amyloid. 2010;17(S1):62.
    • (2010) Amyloid , vol.17 , Issue.S1 , pp. 62
    • Prokaeva, T.1    Spencer, B.2    Doros, G.3    Connors, L.H.4    Skinner, M.5    Seldin, D.C.6
  • 26
    • 79960007241 scopus 로고    scopus 로고
    • Mouse models of AL amyloidosis
    • Skinner M, Berk JL, Connors LH, Seldin DC, eds. Boca Raton, FL: Taylor & Francis;
    • Ward JE, Brenner D, SooHoo P, et al. Mouse models of AL amyloidosis. In: Skinner M, Berk JL, Connors LH, Seldin DC, eds. XIth International Symposium of Amyloidosis. Boca Raton, FL: Taylor & Francis; 2008:321-323.
    • (2008) XIth International Symposium of Amyloidosis , pp. 321-323
    • Ward, J.E.1    Brenner, D.2    SooHoo, P.3
  • 28
    • 84855202169 scopus 로고    scopus 로고
    • Amyloidosis: An EUS view
    • [published online ahead of print April 4, 2011]. doi:10.1016/j.gie.2011. 01.039
    • Shuttleworth E, Keld R, Willert R, Benbow EW. Amyloidosis: an EUS view [published online ahead of print April 4, 2011]. Gastrointest Endosc. doi:10.1016/j.gie.2011.01.039.
    • Gastrointest Endosc
    • Shuttleworth, E.1    Keld, R.2    Willert, R.3    Benbow, E.W.4
  • 30
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • Vrana JA, Gamez JD, Madden BJ, Theis JD, Bergen HR 3rd, Dogan A. Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood. 2009;114(24):4957-4959.
    • (2009) Blood , vol.114 , Issue.24 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3    Theis, J.D.4    Bergen III, H.R.5    Dogan, A.6
  • 31
    • 38349085003 scopus 로고    scopus 로고
    • Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic: A lesson in the generation of transgenic models of disease involving oligomeric proteins
    • Reixach N, Foss TR, Santelli E, Pascual J, Kelly JW, Buxbaum JN. Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic: a lesson in the generation of transgenic models of disease involving oligomeric proteins. J Biol Chem. 2008;283(4):2098-2107.
    • (2008) J Biol Chem , vol.283 , Issue.4 , pp. 2098-2107
    • Reixach, N.1    Foss, T.R.2    Santelli, E.3    Pascual, J.4    Kelly, J.W.5    Buxbaum, J.N.6
  • 32
    • 84055169195 scopus 로고    scopus 로고
    • Mouse models of amyloidoses generated by transgenesis
    • Maeda S. Mouse models of amyloidoses generated by transgenesis. Amyloid. 1996;3214-3215.
    • (1996) Amyloid , pp. 3214-3215
    • Maeda, S.1
  • 33
    • 1842432531 scopus 로고    scopus 로고
    • Transgenic mice in amyloid research: An interpretive review
    • Teng M, Buxbaum JN. Transgenic mice in amyloid research: an interpretive review. Amyloid. 1996;3187-3208.
    • (1996) Amyloid , pp. 3187-3208
    • Teng, M.1    Buxbaum, J.N.2
  • 34
    • 0027200418 scopus 로고
    • Molecular characterization of transgene-induced immunodeficiency in B- less mice using a novel quantitative limiting dilution polymerase chain reaction method
    • Levinson DA, Campos-Torres J, Leder P. Molecular characterization of transgene-induced immunodeficiency in B-less mice using a novel quantitative limiting dilution polymerase chain reaction method. J Exp Med. 1993;178(1):317-329. (Pubitemid 23173267)
    • (1993) Journal of Experimental Medicine , vol.178 , Issue.1 , pp. 317-329
    • Levinson, D.A.1    Campos-Torres, J.2    Leder, P.3
  • 37
    • 0033659115 scopus 로고    scopus 로고
    • Predominant transgene expression in exocrine pancreas directed by the CMV promoter
    • Zhan Y, Brady JL, Johnston AM, Lew AM. Predominant transgene expression in exocrine pancreas directed by the CMV promoter. DNA Cell Biol. 2000;19(11):639-645.
    • (2000) DNA Cell Biol , vol.19 , Issue.11 , pp. 639-645
    • Zhan, Y.1    Brady, J.L.2    Johnston, A.M.3    Lew, A.M.4
  • 38
    • 34848818004 scopus 로고    scopus 로고
    • The molecular biology and clinical features of amyloid neuropathy
    • DOI 10.1002/mus.20821
    • Benson MD, Kincaid JC. The molecular biology and clinical features of amyloid neuropathy. Muscle Nerve. 2007;36(4):411-423. (Pubitemid 47512065)
    • (2007) Muscle and Nerve , vol.36 , Issue.4 , pp. 411-423
    • Benson, M.D.1    Kincaid, J.C.2
  • 39
    • 33750910096 scopus 로고    scopus 로고
    • Neuropathy Associated with Malignancy: 108: Amyloidosis and Neuropathy
    • Dyck PJ, Thomas PK, eds. (4th ed). Philadelphia, PA: W.B. Saunders
    • Kyle RA, Kelly JJ, Dyck PJ. Neuropathy Associated with Malignancy: 108: Amyloidosis and Neuropathy. In: Dyck PJ, Thomas PK, eds. Peripheral Neuropathy (4th ed). Philadelphia, PA: W.B. Saunders; 2005:2427-2451.
    • (2005) Peripheral Neuropathy , pp. 2427-2451
    • Kyle, R.A.1    Kelly, J.J.2    Dyck, P.J.3
  • 40
    • 36248971777 scopus 로고    scopus 로고
    • Mechanisms of amyloid plaque pathogenesis
    • DOI 10.1007/s00401-007-0284-8
    • Fiala JC. Mechanisms of amyloid plaque pathogenesis. Acta Neuropathol. 2007;114(6):551-571. (Pubitemid 50003186)
    • (2007) Acta Neuropathologica , vol.114 , Issue.6 , pp. 551-571
    • Fiala, J.C.1
  • 41
    • 33746355958 scopus 로고    scopus 로고
    • Axonal transport and Alzheimer's disease
    • Stokin GB, Goldstein LS. Axonal transport and Alzheimer's disease. Annu Rev Biochem. 2006;75607-75627.
    • (2006) Annu Rev Biochem , pp. 75607-75627
    • Stokin, G.B.1    Goldstein, L.S.2
  • 43
    • 0024580097 scopus 로고
    • Peripheral neuropathy as an early marker of AL amyloidosis
    • DOI 10.1001/archinte.149.2.358
    • Duston MA, Skinner M, Anderson J, Cohen AS. Peripheral neuropathy as an early marker of AL amyloidosis. Arch Intern Med. 1989;149(2):358-360. (Pubitemid 19058520)
    • (1989) Archives of Internal Medicine , vol.149 , Issue.2 , pp. 358-360
    • Duston, M.A.1    Skinner, M.2    Anderson, J.3    Cohen, A.S.4
  • 44
    • 77954988796 scopus 로고    scopus 로고
    • Synergy of combined Doxycycline/TUDCA treatment in lowering Transthyretin deposition and associated biomarkers: Studies in FAP mouse models
    • Cardoso I, Martins D, Ribeiro T, Merlini G, Saraiva MJ. Synergy of combined Doxycycline/TUDCA treatment in lowering Transthyretin deposition and associated biomarkers: studies in FAP mouse models. J Transl Med. 2010;8:74.
    • (2010) J Transl Med , vol.8 , pp. 74
    • Cardoso, I.1    Martins, D.2    Ribeiro, T.3    Merlini, G.4    Saraiva, M.J.5
  • 45
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: Evidence from studies in a FAP transgenic mice model
    • DOI 10.1096/fj.05-4509com
    • Cardoso I, Saraiva MJ. Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model. FASEB J. 2006;20(2):234-239. (Pubitemid 44933170)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 46
    • 0038375018 scopus 로고    scopus 로고
    • 4′-iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters
    • DOI 10.1096/fj.02-0764com
    • Cardoso I, Merlini G, Saraiva MJ. 4′-iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters. Faseb J. 2003;17(8):803-809. (Pubitemid 36538654)
    • (2003) FASEB Journal , vol.17 , Issue.8 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 47
    • 0035808264 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tetracyclines: Studies in vitro
    • DOI 10.1016/S0014-5793(00)02380-2, PII S0014579300023802
    • Forloni G, Colombo L, Girola L, Tagliavini F, Salmona M. Anti-amyloidogenic activity of tetracyclines: studies in vitro. FEBS Lett. 2001;487(3):404-407. (Pubitemid 32121764)
    • (2001) FEBS Letters , vol.487 , Issue.3 , pp. 404-407
    • Forloni, G.1    Colombo, L.2    Girola, L.3    Tagliavini, F.4    Salmona, M.5
  • 48
    • 33748057491 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of the tetracyclines including glycylcyclines
    • DOI 10.1093/jac/dkl224
    • Agwuh KN, MacGowan A. Pharmacokinetics and pharmacodynamics of the tetracyclines including glycylcyclines. J Antimicrob Chemother. 2006;58(2):256-265. (Pubitemid 44294934)
    • (2006) Journal of Antimicrobial Chemotherapy , vol.58 , Issue.2 , pp. 256-265
    • Agwuh, K.N.1    MacGowan, A.2
  • 49
    • 77950371336 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: Relationship to structural, functional myocardial changes and to light chain amyloid deposition
    • Biolo A, Ramamurthy S, Connors LH, et al. Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: relationship to structural, functional myocardial changes and to light chain amyloid deposition. Circ Heart Fail. 2008;1(4):249-257.
    • (2008) Circ Heart Fail , vol.1 , Issue.4 , pp. 249-257
    • Biolo, A.1    Ramamurthy, S.2    Connors, L.H.3
  • 50
    • 31644449261 scopus 로고    scopus 로고
    • Matrix metalloproteinases and mesangial remodeling in light chain-related glomerular damage
    • DOI 10.1111/j.1523-1755.2005.00571.x, PII 4494762
    • Keeling J, Herrera GA. Matrix metalloproteinases and mesangial remodeling in light chain-related glomerular damage. Kidney Int. 2005;68(4):1590-1603. (Pubitemid 43169904)
    • (2005) Kidney International , vol.68 , Issue.4 , pp. 1590-1603
    • Keeling, J.1    Herrera, G.A.2


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