메뉴 건너뛰기




Volumn 7, Issue 6, 2010, Pages 346-355

Protein misfolding and obstructive lung disease

Author keywords

A1 antichymotrypsin; A1 antitrypsin; Endoplasmic reticulum stress

Indexed keywords

CHRONIC OBSTRUCTIVE LUNG DISEASE; HUMAN; METABOLISM; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCY; REVIEW;

EID: 79952638021     PISSN: 15463222     EISSN: 19435665     Source Type: Journal    
DOI: 10.1513/pats.201002-019AW     Document Type: Conference Paper
Times cited : (23)

References (57)
  • 1
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra JD, Kaufman RJ. The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol 2007;18:716-731.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 2
    • 85047683832 scopus 로고    scopus 로고
    • Liver injury in a1-antitrypsin deficiency: An aggregated protein induces mitochondrial injury
    • Perlmutter DH. Liver injury in a1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury. J Clin Invest 2002;110:1579-1583.
    • (2002) J Clin Invest , vol.110 , pp. 1579-1583
    • Perlmutter, D.H.1
  • 3
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant a1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman JH, Perlmutter DH. Retention of mutant a1-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 2000;279:G961-G974.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279 , pp. G961-G974
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 7
    • 0024247866 scopus 로고
    • The functional role of acute phase plasma proteinase inhibitors
    • Travis J, Shieh BH, Potempa J. The functional role of acute phase plasma proteinase inhibitors. Tokai J Exp Clin Med 1988;13:313-320.
    • (1988) Tokai J Exp Clin Med , vol.13 , pp. 313-320
    • Travis, J.1    Shieh, B.H.2    Potempa, J.3
  • 9
    • 85047684827 scopus 로고    scopus 로고
    • Alpha1-antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy
    • Lomas DA, Mahadeva R. Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 2002;110:1585-1590.
    • (2002) J Clin Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 10
    • 0024550746 scopus 로고
    • Molecular basis for defective secretion of the Z variant of human a1-proteinase inhibitor: Secretion of variants having altered potential for salt bridge formation between amino acids 290 and 342
    • McCracken AA, Kruse KB, Brown JL. Molecular basis for defective secretion of the Z variant of human a1-proteinase inhibitor: secretion of variants having altered potential for salt bridge formation between amino acids 290 and 342. Mol Cell Biol 1989;9:1406-1414.
    • (1989) Mol Cell Biol , vol.9 , pp. 1406-1414
    • McCracken, A.A.1    Kruse, K.B.2    Brown, J.L.3
  • 11
    • 0026755363 scopus 로고
    • The mechanism of Z a1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z a1-antitrypsin accumulation in the liver. Nature 1992;357:605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 12
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in a1-antitrypsin causes loss of anti-neutrophil elastase activity
    • Taggart C, Cervantes-Laurean D, Kim G, McElvaney NG, Wehr N, Moss J, Levine RL. Oxidation of either methionine 351 or methionine 358 in a1-antitrypsin causes loss of anti-neutrophil elastase activity. J Biol Chem 2000;275:27258-27265.
    • (2000) J Biol Chem , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3    McElvaney, N.G.4    Wehr, N.5    Moss, J.6    Levine, R.L.7
  • 13
    • 0027945627 scopus 로고
    • Conformational changes in serpins and the mechanism of a1-antitrypsin deficiency
    • Carrell RW, Whisstock J, Lomas DA. Conformational changes in serpins and the mechanism of a1-antitrypsin deficiency. Am J Respir Crit Care Med 1994;150:S171-S175.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. S171-S175
    • Carrell, R.W.1    Whisstock, J.2    Lomas, D.A.3
  • 14
    • 0027328108 scopus 로고
    • A leucine-to-proline substitution causes a defective a1-antichymotrypsin allele associated with familial obstructive lung disease
    • Poller W, Faber JP, Weidinger S, Tief K, Scholz S, Fischer M, Olek K, Kirchgesser M, Heidtmann HH. A leucine-to-proline substitution causes a defective a1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics 1993;17:740-743.
    • (1993) Genomics , vol.17 , pp. 740-743
    • Poller, W.1    Faber, J.P.2    Weidinger, S.3    Tief, K.4    Scholz, S.5    Fischer, M.6    Olek, K.7    Kirchgesser, M.8    Heidtmann, H.H.9
  • 15
    • 0034602778 scopus 로고    scopus 로고
    • Inactive conformation of the serpin a1-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease
    • Gooptu B, Hazes B, Chang WS, Dafforn TR, Carrell RW, Read RJ, Lomas DA. Inactive conformation of the serpin a1-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease. Proc Natl Acad Sci USA 2000;97:67-72.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    Chang, W.S.3    Dafforn, T.R.4    Carrell, R.W.5    Read, R.J.6    Lomas, D.A.7
  • 16
    • 2142768895 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z a1-antitrypsin deficiency
    • Lawless MW, Greene CM, Mulgrew A, Taggart CC, O'Neill SJ, McElvaney NG. Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z a1-antitrypsin deficiency. J Immunol 2004;172:5722-5726.
    • (2004) J Immunol , vol.172 , pp. 5722-5726
    • Lawless, M.W.1    Greene, C.M.2    Mulgrew, A.3    Taggart, C.C.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 17
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 2006;7:880-885.
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 19
    • 1942520367 scopus 로고    scopus 로고
    • Nrf2 signaling in coordinated activation of antioxidant gene expression
    • Jaiswal AK. Nrf2 signaling in coordinated activation of antioxidant gene expression. Free Radic Biol Med 2004;36:1199-1207.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 20
    • 72549115279 scopus 로고    scopus 로고
    • Heightened endoplasmic reticulum stress in the lungs of patients with chronic obstructive pulmonary disease: The role of Nrf2-regulated proteasomal activity
    • Malhotra D, Thimmulappa R, Vij N, Navas-Acien A, Sussan T, Merali S, Zhang L, Kelsen SG, Myers A, Wise R, et al. Heightened endoplasmic reticulum stress in the lungs of patients with chronic obstructive pulmonary disease: the role of Nrf2-regulated proteasomal activity. Am J Respir Crit Care Med 2009;180:1196-1207.
    • (2009) Am J Respir Crit Care Med , vol.180 , pp. 1196-1207
    • Malhotra, D.1    Thimmulappa, R.2    Vij, N.3    Navas-Acien, A.4    Sussan, T.5    Merali, S.6    Zhang, L.7    Kelsen, S.G.8    Myers, A.9    Wise, R.10
  • 21
    • 77952770299 scopus 로고    scopus 로고
    • Evidence for unfolded protein response activation in monocytes from individuals with a1-antitrypsin deficiency
    • Carroll T, Greene CM, O'Connor CA, Nolan A, O'Neill SJ, McElvaney NG. Evidence for unfolded protein response activation in monocytes from individuals with a1-antitrypsin deficiency. J Immunol 2010;184: 4538-4546.
    • (2010) J Immunol , vol.184 , pp. 4538-4546
    • Carroll, T.1    Greene, C.M.2    O'Connor, C.A.3    Nolan, A.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 23
    • 12244288323 scopus 로고    scopus 로고
    • BAD and Bcl-2 regulation are early events linking neuronal endoplasmic reticulum stress to mitochondria-mediated apoptosis
    • Elyaman W, Terro F, Suen KC, Yardin C, Chang RC, Hugon J. BAD and Bcl-2 regulation are early events linking neuronal endoplasmic reticulum stress to mitochondria-mediated apoptosis. Brain Res Mol Brain Res 2002;109:233-238.
    • (2002) Brain Res Mol Brain Res , vol.109 , pp. 233-238
    • Elyaman, W.1    Terro, F.2    Suen, K.C.3    Yardin, C.4    Chang, R.C.5    Hugon, J.6
  • 24
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, Yui D, Gomi F, Katayama T, Tohyama M. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276:13935-13940.
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 30
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 1995;83:1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 31
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y, Vattem KM, Sood R, An J, Liang J, Stramm L, Wek RC. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol Cell Biol 1998;18:7499-7509.
    • (1998) Mol Cell Biol , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 33
    • 0032065494 scopus 로고    scopus 로고
    • Lung polymers in Za1-antitrypsin deficiency-related emphysema
    • Elliott PR, Bilton D, Lomas DA. Lung polymers in Za1-antitrypsin deficiency-related emphysema. Am J Respir Cell Mol Biol 1998;18: 670-674.
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 670-674
    • Elliott, P.R.1    Bilton, D.2    Lomas, D.A.3
  • 36
    • 65349083154 scopus 로고    scopus 로고
    • Gene targeted therapeutics for liver disease in alpha-1 antitrypsin deficiency
    • McLean C, Greene CM, McElvaney NG. Gene targeted therapeutics for liver disease in alpha-1 antitrypsin deficiency. Biologics 2009;3: 63-75.
    • (2009) Biologics , vol.3 , pp. 63-75
    • McLean, C.1    Greene, C.M.2    McElvaney, N.G.3
  • 37
    • 0035803583 scopus 로고    scopus 로고
    • Functional anatomy of siRNAs for mediating efficient RNai in Drosophila melanogaster embryo lysate
    • Elbashir SM, Martinez J, Patkaniowska A, Lendeckel W, Tuschl T. Functional anatomy of siRNAs for mediating efficient RNai in Drosophila melanogaster embryo lysate. EMBO J 2001;20:6877-6888.
    • (2001) EMBO J , vol.20 , pp. 6877-6888
    • Elbashir, S.M.1    Martinez, J.2    Patkaniowska, A.3    Lendeckel, W.4    Tuschl, T.5
  • 41
    • 0026341239 scopus 로고
    • Sequence-selective recognition of DNA by strand displacement with a thyminesubstituted polyamide
    • Nielsen PE, Egholm M, Berg RH, Buchardt O. Sequence-selective recognition of DNA by strand displacement with a thyminesubstituted polyamide. Science 1991;254:1497-1500.
    • (1991) Science , vol.254 , pp. 1497-1500
    • Nielsen, P.E.1    Egholm, M.2    Berg, R.H.3    Buchardt, O.4
  • 42
    • 0020417286 scopus 로고
    • Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of tetrahymena
    • Kruger K, Grabowski PJ, Zaug AJ, Sands J, Gottschling DE, Cech TR. Self-splicing RNA: autoexcision and autocyclization of the ribosomal RNA intervening sequence of tetrahymena. Cell 1982;31:147-157.
    • (1982) Cell , vol.31 , pp. 147-157
    • Kruger, K.1    Grabowski, P.J.2    Zaug, A.J.3    Sands, J.4    Gottschling, D.E.5    Cech, T.R.6
  • 43
    • 0032992064 scopus 로고    scopus 로고
    • Ribozymemediated specific gene replacement of the a1-antitrypsin gene in human hepatoma cells
    • Ozaki I, Zern MA, Liu S, Wei DL, Pomerantz RJ, Duan L. Ribozymemediated specific gene replacement of the a1-antitrypsin gene in human hepatoma cells. J Hepatol 1999;31:53-60.
    • (1999) J Hepatol , vol.31 , pp. 53-60
    • Ozaki, I.1    Zern, M.A.2    Liu, S.3    Wei, D.L.4    Pomerantz, R.J.5    Duan, L.6
  • 44
    • 0034969249 scopus 로고    scopus 로고
    • Prevention of polymerization of M and Z a1-antitrypsin (a1-AT) with trimethylamine n-oxide: Implications for the treatment of a1-at deficiency
    • Devlin GL, Parfrey H, Tew DJ, Lomas DA, Bottomley SP. Prevention of polymerization of M and Z a1-antitrypsin (a1-AT) with trimethylamine n-oxide: implications for the treatment of a1-at deficiency. Am J Respir Cell Mol Biol 2001;24:727-732.
    • (2001) Am J Respir Cell Mol Biol , vol.24 , pp. 727-732
    • Devlin, G.L.1    Parfrey, H.2    Tew, D.J.3    Lomas, D.A.4    Bottomley, S.P.5
  • 45
  • 46
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant a1-antitrypsin (a1-at) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in a1-at deficiency
    • Burrows JA, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant a1-antitrypsin (a1-at) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in a1-at deficiency. Proc Natl Acad Sci USA 2000;97:1796-1801.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 47
    • 0034695450 scopus 로고    scopus 로고
    • Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z
    • Marcus NY, Perlmutter DH. Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z. J Biol Chem 2000;275:1987-1992.
    • (2000) J Biol Chem , vol.275 , pp. 1987-1992
    • Marcus, N.Y.1    Perlmutter, D.H.2
  • 48
    • 0036510604 scopus 로고    scopus 로고
    • 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization: Implications for the prevention of Z a1-antitrypsinrelated cirrhosis
    • Mahadeva R, Dafforn TR, Carrell RW, Lomas DA. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization: implications for the prevention of Z a1-antitrypsinrelated cirrhosis. J Biol Chem 2002;277:6771-6774.
    • (2002) J Biol Chem , vol.277 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 51
    • 33750725161 scopus 로고    scopus 로고
    • Identification of a 4-mer peptide inhibitor that effectively blocks the polymerization of pathogenic Z a1-antitrypsin
    • Chang YP, Mahadeva R, Chang WS, Shukla A, Dafforn TR, Chu YH. Identification of a 4-mer peptide inhibitor that effectively blocks the polymerization of pathogenic Z a1-antitrypsin. Am J Respir Cell Mol Biol 2006;35:540-548.
    • (2006) Am J Respir Cell Mol Biol , vol.35 , pp. 540-548
    • Chang, Y.P.1    Mahadeva, R.2    Chang, W.S.3    Shukla, A.4    Dafforn, T.R.5    Chu, Y.H.6
  • 53
    • 67650514352 scopus 로고    scopus 로고
    • Selenoprotein S/SEPS1 modifies endoplasmic reticulum stress in Z variant a1-antitrypsin deficiency
    • Kelly E, Greene CM, Carroll TP, McElvaney NG, O'Neill SJ. Selenoprotein S/SEPS1 modifies endoplasmic reticulum stress in Z variant a1-antitrypsin deficiency. J Biol Chem 2009;284:16891-16897.
    • (2009) J Biol Chem , vol.284 , pp. 16891-16897
    • Kelly, E.1    Greene, C.M.2    Carroll, T.P.3    McElvaney, N.G.4    O'Neill, S.J.5
  • 56
    • 28244462778 scopus 로고    scopus 로고
    • Selenium in cancer prevention: A review of the evidence and mechanism of action
    • Rayman MP. Selenium in cancer prevention: a review of the evidence and mechanism of action. Proc Nutr Soc 2005;64:527-542.
    • (2005) Proc Nutr Soc , vol.64 , pp. 527-542
    • Rayman, M.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.