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Volumn 65, Issue 2, 2016, Pages 413-424

Update on alpha-1 antitrypsin deficiency: New therapies

Author keywords

Cirrhosis; Emphysema; Polymerisation; Serpins; Therapeutic strategies

Indexed keywords

ALPHA 1 ANTITRYPSIN; RETINOIC ACID;

EID: 84973885468     PISSN: 01688278     EISSN: 16000641     Source Type: Journal    
DOI: 10.1016/j.jhep.2016.03.010     Document Type: Review
Times cited : (60)

References (98)
  • 1
    • 85047684827 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin polymerisation and the serpinopathies: pathobiology and prospects for therapy
    • [1] Lomas, D.A., Mahadeva, R., Alpha-1-antitrypsin polymerisation and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 110 (2002), 1585–1590.
    • (2002) J Clin Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 3
    • 0017099344 scopus 로고
    • 1-antitrypsin deficiency detected by screening of 200,000 infants
    • 1-antitrypsin deficiency detected by screening of 200,000 infants. N Engl J Med 294 (1976), 1316–1321.
    • (1976) N Engl J Med , vol.294 , pp. 1316-1321
    • Sveger, T.1
  • 5
    • 84875162950 scopus 로고    scopus 로고
    • Prevalence and risk factors for liver involvement in individuals with PiZZ-related lung disease
    • [5] Dawwas, M.F., Davies, S.E., Griffiths, W.J., Lomas, D.A., Alexander, G.J., Prevalence and risk factors for liver involvement in individuals with PiZZ-related lung disease. Am J Respir Crit Care Med 187 (2013), 502–508.
    • (2013) Am J Respir Crit Care Med , vol.187 , pp. 502-508
    • Dawwas, M.F.1    Davies, S.E.2    Griffiths, W.J.3    Lomas, D.A.4    Alexander, G.J.5
  • 6
    • 0013828812 scopus 로고
    • Studies in α1-antitrypsin deficiency
    • [6] Eriksson, S., Studies in α1-antitrypsin deficiency. Acta Med Scand 432 (1965), 1–85.
    • (1965) Acta Med Scand , vol.432 , pp. 1-85
    • Eriksson, S.1
  • 10
    • 84879633515 scopus 로고    scopus 로고
    • Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway
    • e00046
    • [10] Haq, I., Irving, J.A., Faull, S.V., Dickens, J.A., Ordóñez, A., Belorgey, D., et al. Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway. Biosci Rep, 33, 2013, e00046.
    • (2013) Biosci Rep , vol.33
    • Haq, I.1    Irving, J.A.2    Faull, S.V.3    Dickens, J.A.4    Ordóñez, A.5    Belorgey, D.6
  • 11
    • 84899424699 scopus 로고    scopus 로고
    • Altered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization
    • [11] Irving, J.A., Haq, I., Dickens, J.A., Faull, S.V., Lomas, D.A., Altered native stability is the dominant basis for susceptibility of α1-antitrypsin mutants to polymerization. Biochem J 460 (2014), 103–115.
    • (2014) Biochem J , vol.460 , pp. 103-115
    • Irving, J.A.1    Haq, I.2    Dickens, J.A.3    Faull, S.V.4    Lomas, D.A.5
  • 13
    • 62649174885 scopus 로고    scopus 로고
    • Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha-1-antitrypsin: implications for disease and drug design
    • [13] Gooptu, B., Miranda, E., Nobeli, I., Mallya, M., Purkiss, A., Leigh Brown, S.C., et al. Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha-1-antitrypsin: implications for disease and drug design. J Mol Biol 387 (2009), 857–868.
    • (2009) J Mol Biol , vol.387 , pp. 857-868
    • Gooptu, B.1    Miranda, E.2    Nobeli, I.3    Mallya, M.4    Purkiss, A.5    Leigh Brown, S.C.6
  • 14
    • 84857926856 scopus 로고    scopus 로고
    • Structural dynamics associated with intermediate formation in an archetypal conformational disease
    • [14] Nyon, M.P., Segu, L., Cabrita, L.D., Lévy, G.R., Kirkpatrick, J., Roussel, B.D., et al. Structural dynamics associated with intermediate formation in an archetypal conformational disease. Structure 20 (2012), 504–512.
    • (2012) Structure , vol.20 , pp. 504-512
    • Nyon, M.P.1    Segu, L.2    Cabrita, L.D.3    Lévy, G.R.4    Kirkpatrick, J.5    Roussel, B.D.6
  • 16
    • 84943250968 scopus 로고    scopus 로고
    • An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of α1-antitrypsin upon ligand binding
    • [16] Nyon, M.P., Prentice, T., Day, J., Kirkpatrick, J., Sivalingam, G.N., Levy, G., et al. An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of α1-antitrypsin upon ligand binding. Protein Sci 24 (2015), 1301–1312.
    • (2015) Protein Sci , vol.24 , pp. 1301-1312
    • Nyon, M.P.1    Prentice, T.2    Day, J.3    Kirkpatrick, J.4    Sivalingam, G.N.5    Levy, G.6
  • 22
    • 84905169292 scopus 로고    scopus 로고
    • Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency
    • [22] Nyon, M.P., Gooptu, B., Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency. Future Med Chem 6 (2014), 1047–1065.
    • (2014) Future Med Chem , vol.6 , pp. 1047-1065
    • Nyon, M.P.1    Gooptu, B.2
  • 24
    • 81755163563 scopus 로고    scopus 로고
    • Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809
    • [24] Van Goor, F., Hadida, S., Grootenhuis, P.D., Burton, B., Stack, J.H., Straley, K.S., et al. Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809. Proc Natl Acad Sci U S A 108 (2011), 18843–18848.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18843-18848
    • Van Goor, F.1    Hadida, S.2    Grootenhuis, P.D.3    Burton, B.4    Stack, J.H.5    Straley, K.S.6
  • 25
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • [25] Yamasaki, M., Li, W., Johnson, D.J., Huntington, J.A., Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455 (2008), 1255–1258.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 26
    • 79551646854 scopus 로고    scopus 로고
    • Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization
    • [26] Krishnan, B., Gierasch, L.M., Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat Struct Mol Biol 18 (2011), 222–226.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 222-226
    • Krishnan, B.1    Gierasch, L.M.2
  • 27
    • 84858629624 scopus 로고    scopus 로고
    • Folding mechanism of the metastable serpin α1-antitrypsin
    • [27] Tsutsui, Y., Dela Cruz, R., Wintrode, P.L., Folding mechanism of the metastable serpin α1-antitrypsin. Proc Natl Acad Sci U S A 109 (2012), 4467–4472.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4467-4472
    • Tsutsui, Y.1    Dela Cruz, R.2    Wintrode, P.L.3
  • 28
    • 80053561166 scopus 로고    scopus 로고
    • Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer
    • [28] Yamasaki, M., Sendall, T.J., Pearce, M.C., Whisstock, J.C., Huntington, J.A., Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO Rep 12 (2011), 1011–1017.
    • (2011) EMBO Rep , vol.12 , pp. 1011-1017
    • Yamasaki, M.1    Sendall, T.J.2    Pearce, M.C.3    Whisstock, J.C.4    Huntington, J.A.5
  • 29
    • 84908231015 scopus 로고    scopus 로고
    • The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization
    • [29] Behrens, M.A., Sendall, T.J., Pedersen, J.S., Kjeldgaard, M., Huntington, J.A., Jensen, J.K., The shapes of Z-α1-antitrypsin polymers in solution support the C-terminal domain-swap mechanism of polymerization. Biophysical J 107 (2014), 1905–1912.
    • (2014) Biophysical J , vol.107 , pp. 1905-1912
    • Behrens, M.A.1    Sendall, T.J.2    Pedersen, J.S.3    Kjeldgaard, M.4    Huntington, J.A.5    Jensen, J.K.6
  • 30
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • [30] Kröger, H., Miranda, E., MacLeod, I., Pérez, J., Crowther, D.C., Marciniak, S.J., et al. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J Biol Chem 284 (2009), 22793–22802.
    • (2009) J Biol Chem , vol.284 , pp. 22793-22802
    • Kröger, H.1    Miranda, E.2    MacLeod, I.3    Pérez, J.4    Crowther, D.C.5    Marciniak, S.J.6
  • 31
    • 0033671965 scopus 로고    scopus 로고
    • 1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • 1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 279 (2000), G961–G974.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279 , pp. G961-G974
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 33
    • 84876803937 scopus 로고    scopus 로고
    • Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha-1-antitrypsin deficiency
    • [33] Ordóñez, A., Snapp, E.L., Tan, L., Miranda, E., Marciniak, S.J., Lomas, D.A., Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha-1-antitrypsin deficiency. Hepatology 57 (2013), 2049–2060.
    • (2013) Hepatology , vol.57 , pp. 2049-2060
    • Ordóñez, A.1    Snapp, E.L.2    Tan, L.3    Miranda, E.4    Marciniak, S.J.5    Lomas, D.A.6
  • 35
    • 67650526104 scopus 로고    scopus 로고
    • Neuroserpin polymers activate NF-kB by a calcium signalling pathway that is independent of the unfolded protein response
    • [35] Davies, M.J., Miranda, E., Roussel, B.D., Kaufman, R.J., Marciniak, S.J., Lomas, D.A., Neuroserpin polymers activate NF-kB by a calcium signalling pathway that is independent of the unfolded protein response. J Biol Chem 284 (2009), 18202–18209.
    • (2009) J Biol Chem , vol.284 , pp. 18202-18209
    • Davies, M.J.1    Miranda, E.2    Roussel, B.D.3    Kaufman, R.J.4    Marciniak, S.J.5    Lomas, D.A.6
  • 36
    • 43049141447 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin Null mutations and severity of emphysema
    • [36] Fregonese, L., Stolk, J., Frants, R.R., Veldhuisen, B., Alpha-1 antitrypsin Null mutations and severity of emphysema. Respir Med 102 (2008), 876–884.
    • (2008) Respir Med , vol.102 , pp. 876-884
    • Fregonese, L.1    Stolk, J.2    Frants, R.R.3    Veldhuisen, B.4
  • 38
    • 0031905675 scopus 로고    scopus 로고
    • Intermediate alpha 1-antitrypsin deficiency PiSZ: a risk factor for pulmonary emphysema?
    • [38] Seersholm, N., Kok-Jensen, A., Intermediate alpha 1-antitrypsin deficiency PiSZ: a risk factor for pulmonary emphysema?. Respir Med 92 (1998), 241–245.
    • (1998) Respir Med , vol.92 , pp. 241-245
    • Seersholm, N.1    Kok-Jensen, A.2
  • 41
    • 84893023527 scopus 로고    scopus 로고
    • Increased ERK signalling promotes inflammatory signalling in primary airway epithelial cells expressing Z α1-antitrypsin
    • [41] van't Wout, E.F., Dickens, J.A., van Schadewijk, A., Haq, I., Kwok, H.F., Ordóñez, A, et al. Increased ERK signalling promotes inflammatory signalling in primary airway epithelial cells expressing Z α1-antitrypsin. Hum Mol Genet 23 (2014), 929–941.
    • (2014) Hum Mol Genet , vol.23 , pp. 929-941
    • van't Wout, E.F.1    Dickens, J.A.2    van Schadewijk, A.3    Haq, I.4    Kwok, H.F.5    Ordóñez, A.6
  • 43
    • 80051635385 scopus 로고    scopus 로고
    • Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: a novel mechanism of early-onset emphysema
    • [43] Alam, S., Li, Z., Janciauskiene, S., Mahadeva, R., Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: a novel mechanism of early-onset emphysema. Am J Respir Cell Mol Biol 45 (2011), 261–269.
    • (2011) Am J Respir Cell Mol Biol , vol.45 , pp. 261-269
    • Alam, S.1    Li, Z.2    Janciauskiene, S.3    Mahadeva, R.4
  • 46
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins - themes, variations and therapeutic strategies
    • [46] Gooptu, B., Lomas, D.A., Conformational pathology of the serpins - themes, variations and therapeutic strategies. Annu Rev Biochem 78 (2009), 147–176.
    • (2009) Annu Rev Biochem , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 48
    • 0037193809 scopus 로고    scopus 로고
    • Association between conformational mutations in neuroserpin and onset and severity of dementia
    • [48] Davis, R.L., Shrimpton, A.E., Carrell, R.W., Lomas, D.A., Gerhard, L., Baumann, B., et al. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet 359 (2002), 2242–2247.
    • (2002) Lancet , vol.359 , pp. 2242-2247
    • Davis, R.L.1    Shrimpton, A.E.2    Carrell, R.W.3    Lomas, D.A.4    Gerhard, L.5    Baumann, B.6
  • 50
    • 80052033433 scopus 로고    scopus 로고
    • Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 Gene
    • [50] Hagen, M., Murrell, J.R., Delisle, M.B., Andermann, E., Andermann, F., Guiot, M.C., et al. Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 Gene. Brain Pathol 21 (2011), 575–582.
    • (2011) Brain Pathol , vol.21 , pp. 575-582
    • Hagen, M.1    Murrell, J.R.2    Delisle, M.B.3    Andermann, E.4    Andermann, F.5    Guiot, M.C.6
  • 51
    • 0037053323 scopus 로고    scopus 로고
    • Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro
    • [51] Belorgey, D., Crowther, D.C., Mahadeva, R., Lomas, D.A., Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro. J Biol Chem 277 (2002), 17367–17373.
    • (2002) J Biol Chem , vol.277 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 52
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • [52] Miranda, E., Römisch, K., Lomas, D.A., Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J Biol Chem 279 (2004), 28283–28291.
    • (2004) J Biol Chem , vol.279 , pp. 28283-28291
    • Miranda, E.1    Römisch, K.2    Lomas, D.A.3
  • 53
    • 4344586923 scopus 로고    scopus 로고
    • Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB
    • [53] Belorgey, D., Sharp, L.K., Crowther, D.C., Onda, M., Johansson, J., Lomas, D.A., Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB. Eur J Biochem 271 (2004), 3360–3367.
    • (2004) Eur J Biochem , vol.271 , pp. 3360-3367
    • Belorgey, D.1    Sharp, L.K.2    Crowther, D.C.3    Onda, M.4    Johansson, J.5    Lomas, D.A.6
  • 54
    • 44349122437 scopus 로고    scopus 로고
    • The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB
    • [54] Miranda, E., McLeod, I., Davies, M.J., Pérez, J., Römisch, K., Crowther, D.C., et al. The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB. Hum Mol Genet 17 (2008), 1527–1539.
    • (2008) Hum Mol Genet , vol.17 , pp. 1527-1539
    • Miranda, E.1    McLeod, I.2    Davies, M.J.3    Pérez, J.4    Römisch, K.5    Crowther, D.C.6
  • 55
    • 63449091253 scopus 로고    scopus 로고
    • The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability
    • [55] Takehara, S., Onda, M., Zhang, J., Nishiyama, M., Yang, X., Mikami, B., et al. The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability. J Mol Biol 388 (2009), 11–20.
    • (2009) J Mol Biol , vol.388 , pp. 11-20
    • Takehara, S.1    Onda, M.2    Zhang, J.3    Nishiyama, M.4    Yang, X.5    Mikami, B.6
  • 56
    • 76749090946 scopus 로고    scopus 로고
    • PH dependent stability of neuroserpin is mediated by Histidines 119 and 138; implications for the control of β-sheet A and polymerisation
    • [56] Belorgey, D., Hägglöf, P., Onda, M., Lomas, D.A., PH dependent stability of neuroserpin is mediated by Histidines 119 and 138; implications for the control of β-sheet A and polymerisation. Protein Sci 19 (2010), 220–228.
    • (2010) Protein Sci , vol.19 , pp. 220-228
    • Belorgey, D.1    Hägglöf, P.2    Onda, M.3    Lomas, D.A.4
  • 57
    • 84876428891 scopus 로고    scopus 로고
    • A novel interaction between aging and ER overload in a protein conformational dementia
    • [57] Schipanski, A., Lange, S., Segref, A., Gutschmidt, A., Lomas, D.A., Miranda, E., et al. A novel interaction between aging and ER overload in a protein conformational dementia. Genetics 193 (2013), 865–876.
    • (2013) Genetics , vol.193 , pp. 865-876
    • Schipanski, A.1    Lange, S.2    Segref, A.3    Gutschmidt, A.4    Lomas, D.A.5    Miranda, E.6
  • 58
    • 46949107890 scopus 로고    scopus 로고
    • Polymers and inflammation: disease mechanisms of the serpinopathies
    • [58] Gooptu, B., Lomas, D.A., Polymers and inflammation: disease mechanisms of the serpinopathies. J Exp Med 205 (2008), 1529–1534.
    • (2008) J Exp Med , vol.205 , pp. 1529-1534
    • Gooptu, B.1    Lomas, D.A.2
  • 61
    • 20744450475 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin deficiency
    • [61] Stoller, J.K., Aboussouan, L.S., Alpha-1 antitrypsin deficiency. Lancet 365 (2005), 2225–2236.
    • (2005) Lancet , vol.365 , pp. 2225-2236
    • Stoller, J.K.1    Aboussouan, L.S.2
  • 63
    • 67649407825 scopus 로고    scopus 로고
    • Exploring the role of CT densitometry: a randomised study of augmentation therapy in alpha1-antitrypsin deficiency
    • [63] Dirksen, A., Piitulainen, E., Parr, D.G., Deng, C., Wencker, M., Shaker, S.B., et al. Exploring the role of CT densitometry: a randomised study of augmentation therapy in alpha1-antitrypsin deficiency. Eur Respir J 33 (2009), 1345–1353.
    • (2009) Eur Respir J , vol.33 , pp. 1345-1353
    • Dirksen, A.1    Piitulainen, E.2    Parr, D.G.3    Deng, C.4    Wencker, M.5    Shaker, S.B.6
  • 64
    • 84856144387 scopus 로고    scopus 로고
    • Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis
    • [64] Dickens, J.A., Lomas, D.A., Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis. Drug Des Devel Ther 5 (2011), 391–405.
    • (2011) Drug Des Devel Ther , vol.5 , pp. 391-405
    • Dickens, J.A.1    Lomas, D.A.2
  • 65
    • 84944153210 scopus 로고    scopus 로고
    • Lung-function trajectories leading to chronic obstructive pulmonary disease
    • [65] Lange, P., Celli, B., Agustí, A., Boje Jensen, G., Divo, M., Faner, R., et al. Lung-function trajectories leading to chronic obstructive pulmonary disease. N Engl J Med 373 (2015), 111–122.
    • (2015) N Engl J Med , vol.373 , pp. 111-122
    • Lange, P.1    Celli, B.2    Agustí, A.3    Boje Jensen, G.4    Divo, M.5    Faner, R.6
  • 66
    • 84937969384 scopus 로고    scopus 로고
    • Intravenous augmentation treatment and lung density in severe α1-antitrypsin deficiency (RAPID): a randomised, double-blind, placebo-controlled trial
    • [66] Chapman, K.R., Burdon, J.G., Piitulainen, E., Sandhaus, R.A., Seersholm, N., Stocks, J.M., et al. Intravenous augmentation treatment and lung density in severe α1-antitrypsin deficiency (RAPID): a randomised, double-blind, placebo-controlled trial. Lancet 386 (2015), 360–368.
    • (2015) Lancet , vol.386 , pp. 360-368
    • Chapman, K.R.1    Burdon, J.G.2    Piitulainen, E.3    Sandhaus, R.A.4    Seersholm, N.5    Stocks, J.M.6
  • 68
    • 84875667881 scopus 로고    scopus 로고
    • Gene-based therapy for alpha-1 antitrypsin deficiency
    • [68] Mueller, C., Flotte, T.R., Gene-based therapy for alpha-1 antitrypsin deficiency. COPD 10 (2013), 44–49.
    • (2013) COPD , vol.10 , pp. 44-49
    • Mueller, C.1    Flotte, T.R.2
  • 69
    • 16944366965 scopus 로고    scopus 로고
    • Retinoic acid treatment abrogates elastase-induced pulmonary emphysema in rats
    • [69] Massaro, G.D., Massaro, D., Retinoic acid treatment abrogates elastase-induced pulmonary emphysema in rats. Nat Med 3 (1997), 675–677.
    • (1997) Nat Med , vol.3 , pp. 675-677
    • Massaro, G.D.1    Massaro, D.2
  • 70
    • 84864770563 scopus 로고    scopus 로고
    • Randomized controlled trial for emphysema with a selective agonist of the gamma type retinoic acid receptor
    • [70] Stolk, J., Stockley, R.A., Stoel, B.C., Cooper, B.G., Piitulainen, E., Seersholm, N., et al. Randomized controlled trial for emphysema with a selective agonist of the gamma type retinoic acid receptor. Eur Respir J 40 (2012), 306–312.
    • (2012) Eur Respir J , vol.40 , pp. 306-312
    • Stolk, J.1    Stockley, R.A.2    Stoel, B.C.3    Cooper, B.G.4    Piitulainen, E.5    Seersholm, N.6
  • 71
    • 66249110336 scopus 로고    scopus 로고
    • Lung volume reduction surgery for patients with alpha-1 antitrypsin deficiency emphysema
    • [71] Donahue, J.M., Cassivi, S.D., Lung volume reduction surgery for patients with alpha-1 antitrypsin deficiency emphysema. Thorac Surg Clin 19 (2009), 201–208.
    • (2009) Thorac Surg Clin , vol.19 , pp. 201-208
    • Donahue, J.M.1    Cassivi, S.D.2
  • 72
    • 84910070109 scopus 로고    scopus 로고
    • One- to four-year follow-up of endobronchial lung volume reduction in alpha-1-antitrypsin deficiency patients: a case series
    • [72] Hillerdal, G., Mindus, S., One- to four-year follow-up of endobronchial lung volume reduction in alpha-1-antitrypsin deficiency patients: a case series. Respiration 88 (2014), 320–328.
    • (2014) Respiration , vol.88 , pp. 320-328
    • Hillerdal, G.1    Mindus, S.2
  • 74
    • 0034652248 scopus 로고    scopus 로고
    • 1-AT) Z: a potential pharmacologcial strategy for prevention of liver injury and emphysema
    • 1-AT) Z: a potential pharmacologcial strategy for prevention of liver injury and emphysema. Proc Natl Acad Sci U S A 97 (2000), 1796–1801.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1796-1801
    • Burrows, J.A.J.1    Willis, L.K.2    Perlmutter, D.H.3
  • 75
    • 16544381001 scopus 로고    scopus 로고
    • Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antitrypsin in patients with alpha-1-antitrypsin deficiency: a preliminary study
    • [75] Teckman, J.H., Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antitrypsin in patients with alpha-1-antitrypsin deficiency: a preliminary study. J Pediatr Gastroenterol Nutr 39 (2004), 34–37.
    • (2004) J Pediatr Gastroenterol Nutr , vol.39 , pp. 34-37
    • Teckman, J.H.1
  • 76
    • 77954597127 scopus 로고    scopus 로고
    • An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis
    • [76] Hidvegi, T., Ewing, M., Hale, P., Dippold, C., Beckett, C., Kemp, C., et al. An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis. Science 329 (2010), 229–232.
    • (2010) Science , vol.329 , pp. 229-232
    • Hidvegi, T.1    Ewing, M.2    Hale, P.3    Dippold, C.4    Beckett, C.5    Kemp, C.6
  • 77
    • 77953187568 scopus 로고    scopus 로고
    • Rapamycin reduces intrahepatic alpha-1-antitrypsin mutant Z protein polymers and liver injury in a mouse model
    • [77] Kaushal, S., Annamali, M., Blomenkamp, K., Rudnick, D., Halloran, D., Brunt, E.M., et al. Rapamycin reduces intrahepatic alpha-1-antitrypsin mutant Z protein polymers and liver injury in a mouse model. Exp Biol Med (Maywood) 235 (2010), 700–709.
    • (2010) Exp Biol Med (Maywood) , vol.235 , pp. 700-709
    • Kaushal, S.1    Annamali, M.2    Blomenkamp, K.3    Rudnick, D.4    Halloran, D.5    Brunt, E.M.6
  • 78
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • [78] Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B.A., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000), 98–103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6
  • 79
    • 84880912134 scopus 로고    scopus 로고
    • Autophagy master regulator TFEB induces clearance of toxic SERPINA1/α-1-antitrypsin polymers
    • [79] Pastore, N., Ballabio, A., Brunetti-Pierri, N., Autophagy master regulator TFEB induces clearance of toxic SERPINA1/α-1-antitrypsin polymers. Autophagy 9 (2013), 1094–1096.
    • (2013) Autophagy , vol.9 , pp. 1094-1096
    • Pastore, N.1    Ballabio, A.2    Brunetti-Pierri, N.3
  • 80
    • 84868334619 scopus 로고    scopus 로고
    • Histone Deacetylase inhibitor (HDACi) Suberoylanilide Hydroxamic Acid (SAHA) mediated correction of alpha-1 antitrypsin deficiency
    • [80] Bouchecareilh, M., Hutta, D.M., Szajnera, P., Flotte, T.R., Balch, W.E., Histone Deacetylase inhibitor (HDACi) Suberoylanilide Hydroxamic Acid (SAHA) mediated correction of alpha-1 antitrypsin deficiency. J Biol Chem 287 (2012), 38265–38278.
    • (2012) J Biol Chem , vol.287 , pp. 38265-38278
    • Bouchecareilh, M.1    Hutta, D.M.2    Szajnera, P.3    Flotte, T.R.4    Balch, W.E.5
  • 82
    • 84990304685 scopus 로고    scopus 로고
    • Pre-clinical evaluation of ALN-AAT to ameliorate liver disease associated with alpha-1-antitrypsin deficiency
    • [82] Sehgal, A., Blomenkamp, K.S., Qian, K., Simon, A., Haslett, P., Barros, S., et al. Pre-clinical evaluation of ALN-AAT to ameliorate liver disease associated with alpha-1-antitrypsin deficiency. Gastroenterology, 148, 2015, S-975.
    • (2015) Gastroenterology , vol.148 , pp. S-975
    • Sehgal, A.1    Blomenkamp, K.S.2    Qian, K.3    Simon, A.4    Haslett, P.5    Barros, S.6
  • 83
    • 84892936309 scopus 로고    scopus 로고
    • Antisense oligonucleotide treatment ameliorates alpha-1 antitrypsin-related liver disease in mice
    • [83] Guo, S., Booten, S.L., Aghajan, M., Hung, G., Zhao, C., Blomenkamp, K., et al. Antisense oligonucleotide treatment ameliorates alpha-1 antitrypsin-related liver disease in mice. J Clin Invest 124 (2014), 251–261.
    • (2014) J Clin Invest , vol.124 , pp. 251-261
    • Guo, S.1    Booten, S.L.2    Aghajan, M.3    Hung, G.4    Zhao, C.5    Blomenkamp, K.6
  • 85
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9Å structure of binary-complexed antithrombin
    • [85] Skinner, R., Chang, W.-S.W., Jin, L., Pei, X., Huntington, J.A., Abrahams, J.-P., et al. Implications for function and therapy of a 2.9Å structure of binary-complexed antithrombin. J Mol Biol 283 (1998), 9–14.
    • (1998) J Mol Biol , vol.283 , pp. 9-14
    • Skinner, R.1    Chang, W.-S.W.2    Jin, L.3    Pei, X.4    Huntington, J.A.5    Abrahams, J.-P.6
  • 89
    • 0343193210 scopus 로고    scopus 로고
    • Topography of a 2.0Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • [89] Elliott, P.R., Pei, X.Y., Dafforn, T.R., Lomas, D.A., Topography of a 2.0Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Sci 9 (2000), 1274–1281.
    • (2000) Protein Sci , vol.9 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 92
    • 84915758694 scopus 로고    scopus 로고
    • Characterising the association of latency with α1-antitrypsin polymerisation using a novel monoclonal antibody
    • [92] Tan, L., Perez, J., Mela, M., Miranda, E., Burling, K.A., Rouhani, F.N., et al. Characterising the association of latency with α1-antitrypsin polymerisation using a novel monoclonal antibody. Int J Biochem Cell Biol 58 (2015), 81–91.
    • (2015) Int J Biochem Cell Biol , vol.58 , pp. 81-91
    • Tan, L.1    Perez, J.2    Mela, M.3    Miranda, E.4    Burling, K.A.5    Rouhani, F.N.6
  • 93
    • 84934920503 scopus 로고    scopus 로고
    • An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein
    • [93] Irving, J.A., Miranda, E., Haq, I., Perez, J., Kotov, V.R., Faull, S.V., et al. An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein. Biochem J 468 (2015), 99–108.
    • (2015) Biochem J , vol.468 , pp. 99-108
    • Irving, J.A.1    Miranda, E.2    Haq, I.3    Perez, J.4    Kotov, V.R.5    Faull, S.V.6
  • 94
    • 84933567270 scopus 로고    scopus 로고
    • A single-chain variable fragment intrabody prevents intracellular polymerisation of Z α1-antitrypsin
    • [94] Ordóñez, A., Pérez, J., Tan, L., Dickens, J.A., Motamedi-Shad, N., Irving, J.A., et al. A single-chain variable fragment intrabody prevents intracellular polymerisation of Z α1-antitrypsin. FASEB J 29 (2015), 2667–2678.
    • (2015) FASEB J , vol.29 , pp. 2667-2678
    • Ordóñez, A.1    Pérez, J.2    Tan, L.3    Dickens, J.A.4    Motamedi-Shad, N.5    Irving, J.A.6
  • 95
    • 77956354416 scopus 로고    scopus 로고
    • Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells
    • [95] Rashid, S.T., Corbineau, S., Hannan, N., Marciniak, S.J., Miranda, E., Alexander, G., et al. Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells. J Clin Invest 120 (2010), 3127–3136.
    • (2010) J Clin Invest , vol.120 , pp. 3127-3136
    • Rashid, S.T.1    Corbineau, S.2    Hannan, N.3    Marciniak, S.J.4    Miranda, E.5    Alexander, G.6
  • 96
    • 84929282245 scopus 로고    scopus 로고
    • Emergence of a stage-dependent human liver disease signature with directed differentiation of alpha-1 antitrypsin-deficient iPS cells
    • [96] Wilson, A.A., Yin, L., Liesa, M., Segeritz, C.P., Mills, J.A., Shen, S.S., et al. Emergence of a stage-dependent human liver disease signature with directed differentiation of alpha-1 antitrypsin-deficient iPS cells. Stem Cell Rep 4 (2015), 873–885.
    • (2015) Stem Cell Rep , vol.4 , pp. 873-885
    • Wilson, A.A.1    Yin, L.2    Liesa, M.3    Segeritz, C.P.4    Mills, J.A.5    Shen, S.S.6
  • 97
    • 80054987997 scopus 로고    scopus 로고
    • Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells
    • [97] Yusa, K., Rashid, S.T., Strick-Marchand, H., Varela, I., Liu, P.Q., Paschon, D.E., et al. Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells. Nature 478 (2011), 391–394.
    • (2011) Nature , vol.478 , pp. 391-394
    • Yusa, K.1    Rashid, S.T.2    Strick-Marchand, H.3    Varela, I.4    Liu, P.Q.5    Paschon, D.E.6
  • 98
    • 84860677190 scopus 로고    scopus 로고
    • In silico assessment of potential druggable pockets on the surface of α1-antitrypsin conformers
    • e36612
    • [98] Patschull, A.O., Gooptu, B., Ashford, P., Daviter, T., Nobeli, I., In silico assessment of potential druggable pockets on the surface of α1-antitrypsin conformers. PLoS One, 7, 2012, e36612.
    • (2012) PLoS One , vol.7
    • Patschull, A.O.1    Gooptu, B.2    Ashford, P.3    Daviter, T.4    Nobeli, I.5


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