메뉴 건너뛰기




Volumn 67, Issue , 2005, Pages 663-696

Surfactant protein C biosynthesis and its emerging role in conformational lung disease

Author keywords

Apoptosis; ERAD; Interstitial pneumonia; Propeptide processing; Unfolded protein response

Indexed keywords

AMINO ACID; CASPASE; HORMONE PRECURSOR; HYBRID PROTEIN; INTEGRAL MEMBRANE PROTEIN; LUNG SURFACTANT; MEMBRANE PROTEIN; PEPTIDE; PHOSPHOLIPID; PROTEASOME; PROTEIN PRECURSOR; SURFACTANT PROTEIN C; UNCLASSIFIED DRUG;

EID: 15544369388     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.67.040403.101937     Document Type: Review
Times cited : (160)

References (174)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW, Lomas DA. 1997. Conformational disease. Lancet 350:134-38
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 2
    • 0037011795 scopus 로고    scopus 로고
    • 1-antitrypsin deficiency-a model for conformational diseases
    • 1-antitrypsin deficiency-a model for conformational diseases. N. Engl. J. Med. 346:45-53
    • (2002) N. Engl. J. Med. , vol.346 , pp. 45-53
    • Carrell, R.W.1    Lomas, D.A.2
  • 7
    • 0034779954 scopus 로고    scopus 로고
    • Synthesis and post-translational processing of surfactant protein C
    • Solarin KO, Wang WJ, Beers MF. 2001. Synthesis and post-translational processing of surfactant protein C. Pediatr. Pathol. Mol. Med. 20:471-500
    • (2001) Pediatr. Pathol. Mol. Med. , vol.20 , pp. 471-500
    • Solarin, K.O.1    Wang, W.J.2    Beers, M.F.3
  • 8
    • 0035931973 scopus 로고    scopus 로고
    • A mutation in the surfactant protein C gene associated with familial interstitial lung disease
    • Nogee LM, Dunbar AE, Wert SE, Askin F, Hamvas A, Whitsett JA. 2001. A mutation in the surfactant protein C gene associated with familial interstitial lung disease. N. Engl. J. Med. 344:573-79
    • (2001) N. Engl. J. Med. , vol.344 , pp. 573-579
    • Nogee, L.M.1    Dunbar, A.E.2    Wert, S.E.3    Askin, F.4    Hamvas, A.5    Whitsett, J.A.6
  • 9
    • 0036126333 scopus 로고    scopus 로고
    • Mutations in the surfactant protein C gene associated with interstitial lung disease
    • Nogee LM, Dunbar AE III, Wert S, Askin F, Hamvas A, Whitsett JA. 2002. Mutations in the surfactant protein C gene associated with interstitial lung disease. Chest 121:20S-21S
    • (2002) Chest , vol.121
    • Nogee, L.M.1    Dunbar III, A.E.2    Wert, S.3    Askin, F.4    Hamvas, A.5    Whitsett, J.A.6
  • 10
    • 0036570052 scopus 로고    scopus 로고
    • Heterozygosity for a surfactant protein C gene mutation associated with usual interstitial pneumonitis and cellular nonspecific interstitial pneumonitis in one kindred
    • Thomas AQ, Lane K, Phillips J III, Prince M, Markin C, et al. 2002. Heterozygosity for a surfactant protein C gene mutation associated with usual interstitial pneumonitis and cellular nonspecific interstitial pneumonitis in one kindred. Am. J. Respir. Crit. Care Med. 165:1322-28
    • (2002) Am. J. Respir. Crit. Care Med. , vol.165 , pp. 1322-1328
    • Thomas, A.Q.1    Lane, K.2    Phillips III, J.3    Prince, M.4    Markin, C.5
  • 11
    • 2142671425 scopus 로고    scopus 로고
    • Progressive lung disease and surfactant dysfunction with a deletion of surfactant protein C gene
    • Hamvas A, Nogee LM, White FV, Schuler P, Hackett BP, et al. 2004. Progressive lung disease and surfactant dysfunction with a deletion of surfactant protein C gene. Am. J. Respir. Cell Mol. Biol. 30:771-76
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.30 , pp. 771-776
    • Hamvas, A.1    Nogee, L.M.2    White, F.V.3    Schuler, P.4    Hackett, B.P.5
  • 12
    • 0028219389 scopus 로고
    • Human surfactant protein-C-genetic homogeneity and expression in RDS-comparison with other species
    • Hatzis D, Deiter G, deMello DE, Floros J. 1994. Human surfactant protein-C-genetic homogeneity and expression in RDS-comparison with other species. Exp. Lung Res. 20:57-72
    • (1994) Exp. Lung Res. , vol.20 , pp. 57-72
    • Hatzis, D.1    Deiter, G.2    DeMello, D.E.3    Floros, J.4
  • 14
    • 0028605818 scopus 로고
    • Mapping of the pulmonary surfactant SP5 (SFTP2) locus to 8p21 and characterization of a microsatellite repeat marker that shows frequent loss of heterozygosity in human carcinomas
    • Wood S, Yaremko ML, Schertzer M, Kelemen PR, Minna J, Westbrook CA. 1994. Mapping of the pulmonary surfactant SP5 (SFTP2) locus to 8p21 and characterization of a microsatellite repeat marker that shows frequent loss of heterozygosity in human carcinomas. Genomics 24:597-600
    • (1994) Genomics , vol.24 , pp. 597-600
    • Wood, S.1    Yaremko, M.L.2    Schertzer, M.3    Kelemen, P.R.4    Minna, J.5    Westbrook, C.A.6
  • 15
    • 0023902154 scopus 로고
    • cDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL (pVal)
    • Glasser SW, Korfhagen TR, Weaver TE, Clark JC, Pilot-Matias T, et al. 1988. cDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL (pVal). J. Biol. Chem. 263:9-12
    • (1988) J. Biol. Chem. , vol.263 , pp. 9-12
    • Glasser, S.W.1    Korfhagen, T.R.2    Weaver, T.E.3    Clark, J.C.4    Pilot-Matias, T.5
  • 16
    • 0345696724 scopus 로고
    • Low molecular weight human pulmonary surfactant protein (SP5): Isolation, characterization, and cDNA and amino acid sequences
    • Warr RG, Hawgood S, Buckley DI, Crisp TM, Schilling J, et al. 1987. Low molecular weight human pulmonary surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences. Proc. Natl. Acad. Sci. USA 84:7915-19
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7915-7919
    • Warr, R.G.1    Hawgood, S.2    Buckley, D.I.3    Crisp, T.M.4    Schilling, J.5
  • 17
    • 0026609266 scopus 로고
    • Surfactant protein C precursor is palmitoylated and associates with subcellular membranes
    • Vorbroker DK, Dey C, Weaver TE, Whitsett JA. 1992. Surfactant protein C precursor is palmitoylated and associates with subcellular membranes. Biochim. Biophys. Acta 1105:161-69
    • (1992) Biochim. Biophys. Acta , vol.1105 , pp. 161-169
    • Vorbroker, D.K.1    Dey, C.2    Weaver, T.E.3    Whitsett, J.A.4
  • 18
  • 19
    • 0034835903 scopus 로고    scopus 로고
    • Maintenance of differentiated function of the surfactant system in human fetal lung type II epithelial cells cultured on plastic
    • Gonzales LW, Angampalli S, Guttentag SH, Beers MF, Feinstein SI, et al. 2001. Maintenance of differentiated function of the surfactant system in human fetal lung type II epithelial cells cultured on plastic. Pediatr. Pathol. Mol. Med. 20:387-412
    • (2001) Pediatr. Pathol. Mol. Med. , vol.20 , pp. 387-412
    • Gonzales, L.W.1    Angampalli, S.2    Guttentag, S.H.3    Beers, M.F.4    Feinstein, S.I.5
  • 20
    • 0024550157 scopus 로고
    • Nucleotide and deduced amino acid sequence of the hydrophobic surfactant protein SP-C from rat: Expression in alveolar type II cells and homology with SP-C from other species
    • Fisher JH, Shannon JM, Hofmann T, Mason RJ. 1989. Nucleotide and deduced amino acid sequence of the hydrophobic surfactant protein SP-C from rat: expression in alveolar type II cells and homology with SP-C from other species. Biochim. Biophys. Acta 995:225-30
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 225-230
    • Fisher, J.H.1    Shannon, J.M.2    Hofmann, T.3    Mason, R.J.4
  • 21
    • 0027080431 scopus 로고
    • Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs
    • Boggaram V, Margana RK. 1992. Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs. Am. J. Physiol. Lung Cell Mol. Physiol. 263:L634-44
    • (1992) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.263
    • Boggaram, V.1    Margana, R.K.2
  • 22
    • 0023949137 scopus 로고
    • Hydrophobic 3.7 kDa surfactant polypeptide: Structural characterization of the human and bovine forms
    • Johansson J, Jornvall H, Eklund A, Christensen N, Robertson B, Curstedt T. 1988. Hydrophobic 3.7 kDa surfactant polypeptide: structural characterization of the human and bovine forms. FEBS Lett. 232:61-64
    • (1988) FEBS Lett. , vol.232 , pp. 61-64
    • Johansson, J.1    Jornvall, H.2    Eklund, A.3    Christensen, N.4    Robertson, B.5    Curstedt, T.6
  • 23
    • 0023893969 scopus 로고
    • Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide
    • Johansson J, Curstedt T, Robertson B, Jornvall H. 1988. Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide. Biochemistry (Mosc) 27:3544-47
    • (1988) Biochemistry (Mosc) , vol.27 , pp. 3544-3547
    • Johansson, J.1    Curstedt, T.2    Robertson, B.3    Jornvall, H.4
  • 24
    • 0023656392 scopus 로고
    • Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant; characterization and biophysical activity
    • Curstedt T, Jornvall H, Robertson B, Bergman T, Berggren P. 1987. Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant; characterization and biophysical activity. Eur. J. Biochem. 168:255-62
    • (1987) Eur. J. Biochem. , vol.168 , pp. 255-262
    • Curstedt, T.1    Jornvall, H.2    Robertson, B.3    Bergman, T.4    Berggren, P.5
  • 25
    • 0023631940 scopus 로고
    • Characterization and partial amino acid sequence of a low molecular weight surfactant protein
    • Phelps DS, Smith LM, Taeusch HW. 1987. Characterization and partial amino acid sequence of a low molecular weight surfactant protein. Am. Rev. Resp. Dis. 135:1112-17
    • (1987) Am. Rev. Resp. Dis. , vol.135 , pp. 1112-1117
    • Phelps, D.S.1    Smith, L.M.2    Taeusch, H.W.3
  • 26
    • 0025239383 scopus 로고
    • Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups
    • Curstedt T, Johansson J, Persson P, Eklund A, Robertson B, et al. 1990. Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups. Proc. Natl. Acad. Sci. USA 87:2985-89
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2985-2989
    • Curstedt, T.1    Johansson, J.2    Persson, P.3    Eklund, A.4    Robertson, B.5
  • 28
    • 0033150427 scopus 로고    scopus 로고
    • Effects of early treatment with rSP-C surfactant on oxygenation and histology in rats with acute lung injury
    • Hafner D, Germann PG, Hauschke D, Kilian U. 1999. Effects of early treatment with rSP-C surfactant on oxygenation and histology in rats with acute lung injury. Pulm. Pharmacol. Ther 12:193-201
    • (1999) Pulm. Pharmacol. Ther. , vol.12 , pp. 193-201
    • Hafner, D.1    Germann, P.G.2    Hauschke, D.3    Kilian, U.4
  • 29
    • 0031857891 scopus 로고    scopus 로고
    • Comparison of rSP-C surfactant with natural and synthetic surfactants after late treatment in a rat model of the acute respiratory distress syndrome
    • Hafner D, Germann PG, Hauschke D. 1998. Comparison of rSP-C surfactant with natural and synthetic surfactants after late treatment in a rat model of the acute respiratory distress syndrome. Br. J. Pharmacol. 124:1083-90
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 1083-1090
    • Hafner, D.1    Germann, P.G.2    Hauschke, D.3
  • 30
    • 0037794407 scopus 로고    scopus 로고
    • Treatment of acute respiratory distress syndrome with recombinant surfactant protein C surfactant
    • Spragg RG, Lewis JF, Wurst W, Hafner D, Baughman RP, et al. 2003. Treatment of acute respiratory distress syndrome with recombinant surfactant protein C surfactant. Am. J. Respir. Crit. Care Med. 167:1562-66
    • (2003) Am. J. Respir. Crit. Care Med. , vol.167 , pp. 1562-1566
    • Spragg, R.G.1    Lewis, J.F.2    Wurst, W.3    Hafner, D.4    Baughman, R.P.5
  • 32
  • 33
    • 0032791063 scopus 로고    scopus 로고
    • Pulmonary surfactant in health and human lung diseases: State of the art
    • Griese M. 1999. Pulmonary surfactant in health and human lung diseases: state of the art. Eur. Respir. J. 13:1455-76
    • (1999) Eur. Respir. J. , vol.13 , pp. 1455-1476
    • Griese, M.1
  • 34
    • 3242721053 scopus 로고    scopus 로고
    • Functional composition and component biophysicis of endogenous lung surfactant
    • New York: Marcell-Dekker
    • Notter RH. 2000. Functional composition and component biophysicis of endogenous lung surfactant. In Lung Surfactants: Basic Science and Clinical Applications, pp. 171-206. New York: Marcell-Dekker
    • (2000) Lung Surfactants: Basic Science and Clinical Applications , pp. 171-206
    • Notter, R.H.1
  • 36
    • 0027090063 scopus 로고
    • Structure and functions of a dimeric form of surfactant protein SP-C: A Fourier transform infrared and surfactometry study
    • Baatz JE, Smyth KL, Whitsett JA, Baxter C, Absolom DR. 1992. Structure and functions of a dimeric form of surfactant protein SP-C: a Fourier transform infrared and surfactometry study. Chem. Phys. Lipids 63:91-104
    • (1992) Chem. Phys. Lipids , vol.63 , pp. 91-104
    • Baatz, J.E.1    Smyth, K.L.2    Whitsett, J.A.3    Baxter, C.4    Absolom, D.R.5
  • 37
    • 0031940348 scopus 로고    scopus 로고
    • Removal of a dimeric form of surfactant protein C from mouse lungs: Its acceleration by reduction
    • Li ZY, Suzuki Y, Kurozumi M, Shen HQ, Duan CX. 1998. Removal of a dimeric form of surfactant protein C from mouse lungs: its acceleration by reduction. J. Appl. Physiol. 84:471-78
    • (1998) J. Appl. Physiol. , vol.84 , pp. 471-478
    • Li, Z.Y.1    Suzuki, Y.2    Kurozumi, M.3    Shen, H.Q.4    Duan, C.X.5
  • 39
    • 0028358907 scopus 로고
    • The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-Helix
    • Johansson J, Szyperski T, Curstedt T, Wuthrich K. 1994. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-Helix. Biochemistry (Mosc) 33:6015-23
    • (1994) Biochemistry (Mosc) , vol.33 , pp. 6015-6023
    • Johansson, J.1    Szyperski, T.2    Curstedt, T.3    Wuthrich, K.4
  • 40
    • 0027331636 scopus 로고
    • 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-in-glycero-3-phosphocholine headgroup: A model for transbilayer peptides in surfactant and biological membranes
    • 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-in-glycero-3-phosphocholine headgroup: A model for transbilayer peptides in surfactant and biological membranes. Biochemistry (Mosc) 32:11338-44
    • (1993) Biochemistry (Mosc) , vol.32 , pp. 11338-11344
    • Morrow, M.R.1    Taneva, S.2    Simatos, G.A.3    Allwood, L.A.4    Keough, K.M.W.5
  • 41
    • 0031647114 scopus 로고    scopus 로고
    • Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates
    • Szyperski T, Vandenbussche G, Curstedt T, Ruysschaert JM, Wuthrich K, Johansson J. 1998. Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates. Protein Sci. 7:2533-40
    • (1998) Protein Sci. , vol.7 , pp. 2533-2540
    • Szyperski, T.1    Vandenbussche, G.2    Curstedt, T.3    Ruysschaert, J.M.4    Wuthrich, K.5    Johansson, J.6
  • 42
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly JW. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6:11-17
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 44
    • 0035919776 scopus 로고    scopus 로고
    • The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate
    • Gustafsson M, Griffiths WJ, Furusjo E, Johansson J. 2001. The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate. J. Mol. Biol. 310:937-50
    • (2001) J. Mol. Biol. , vol.310 , pp. 937-950
    • Gustafsson, M.1    Griffiths, W.J.2    Furusjo, E.3    Johansson, J.4
  • 45
    • 0141530970 scopus 로고    scopus 로고
    • Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: An infrared structural investigation
    • Dluhy RA, Shanmukh S, Leapard JB, Kruger P, Baatz JE. 2003. Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: an infrared structural investigation. Biophys. J. 85:2417-29
    • (2003) Biophys. J. , vol.85 , pp. 2417-2429
    • Dluhy, R.A.1    Shanmukh, S.2    Leapard, J.B.3    Kruger, P.4    Baatz, J.E.5
  • 47
    • 0023922706 scopus 로고
    • Localization of surfactant protein synthesis in human lung by in situ hybridization
    • Phelps DS, Floros J. 1988. Localization of surfactant protein synthesis in human lung by in situ hybridization. Am. Rev. Resp. Dis. 137:939-42
    • (1988) Am. Rev. Resp. Dis. , vol.137 , pp. 939-942
    • Phelps, D.S.1    Floros, J.2
  • 48
    • 0026816112 scopus 로고
    • Localization of surfactant-associated protein C (SP-C) mRNA in fetal rabbit lung tissue by in situ hybridization
    • Wohlford-Lenane CL, Durham PL, Snyder JM. 1992. Localization of surfactant-associated protein C (SP-C) mRNA in fetal rabbit lung tissue by in situ hybridization. Am. J Respir. Cell Mol. Biol. 6:225-34
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 225-234
    • Wohlford-Lenane, C.L.1    Durham, P.L.2    Snyder, J.M.3
  • 49
    • 0025989304 scopus 로고
    • Localization of pulmonary surfactant proteins using immunohistochemistry and tissue in situ hybridization
    • Phelps DS, Floros J. 1991. Localization of pulmonary surfactant proteins using immunohistochemistry and tissue in situ hybridization. Exp. Lung Res. 17:985-95
    • (1991) Exp. Lung Res. , vol.17 , pp. 985-995
    • Phelps, D.S.1    Floros, J.2
  • 50
    • 0018608269 scopus 로고
    • Hydrophobic proteins of lamellated osmiophillic bodies isolated from pig lung
    • Phizackerly PJ, Town RMH, Newman GE. 1979. Hydrophobic proteins of lamellated osmiophillic bodies isolated from pig lung. Biochem. J. 183:731-36
    • (1979) Biochem. J. , vol.183 , pp. 731-736
    • Phizackerly, P.J.1    Town, R.M.H.2    Newman, G.E.3
  • 51
    • 0020560675 scopus 로고
    • Cells of the lung: Biology and clinical implications
    • Gail DB, Lenfant CJM. 1983. Cells of the lung: biology and clinical implications. Am. Rev. Resp. Dis. 127:366-87
    • (1983) Am. Rev. Resp. Dis. , vol.127 , pp. 366-387
    • Gail, D.B.1    Lenfant, C.J.M.2
  • 53
    • 17544375900 scopus 로고    scopus 로고
    • Inhibition of cellular processing of surfactant protein C by drugs affecting intracellular pH gradients
    • Beers MF. 1996. Inhibition of cellular processing of surfactant protein C by drugs affecting intracellular pH gradients. J. Biol. Chem. 271:14361-70
    • (1996) J. Biol. Chem. , vol.271 , pp. 14361-14370
    • Beers, M.F.1
  • 56
    • 0034055937 scopus 로고    scopus 로고
    • Deficiency of lamellar bodies in alveolar type II cells associated with fatal respiratory disease in a full-term infant
    • Cutz E, Wert SE, Nogee LM, Moore AM. 2000. Deficiency of lamellar bodies in alveolar type II cells associated with fatal respiratory disease in a full-term infant. Am. J. Respir. Crit. Care Med. 161:608-14
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161 , pp. 608-614
    • Cutz, E.1    Wert, S.E.2    Nogee, L.M.3    Moore, A.M.4
  • 57
    • 0033946086 scopus 로고    scopus 로고
    • Absence of lamellar bodies with accumulation of dense bodies characterizes a novel form of congenital surfactant defect
    • Tryka AF, Wert SE, Mazursky JE, Arrington RW, Nogee LM. 2000. Absence of lamellar bodies with accumulation of dense bodies characterizes a novel form of congenital surfactant defect. Pediatr. Dev. Pathol. 3:335-45
    • (2000) Pediatr. Dev. Pathol. , vol.3 , pp. 335-345
    • Tryka, A.F.1    Wert, S.E.2    Mazursky, J.E.3    Arrington, R.W.4    Nogee, L.M.5
  • 58
    • 0034953105 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M, Hamon Y, Chimini G. 2001. The human ATP-binding cassette (ABC) transporter superfamily. J. Lipid Res. 42:1007-17
    • (2001) J. Lipid Res. , vol.42 , pp. 1007-1017
    • Dean, M.1    Hamon, Y.2    Chimini, G.3
  • 59
    • 0037151018 scopus 로고    scopus 로고
    • Identification of LBM180, a lamellar body limiting membrane protein of alveolar type II cells, as the ABC transporter protein ABCA3
    • Mulugeta S, Gray JM, Notarfrancesco KL, Gonzales LW, Koval M, et al. 2002. Identification of LBM180, a lamellar body limiting membrane protein of alveolar type II cells, as the ABC transporter protein ABCA3. J. Biol. Chem. 277:22147-55
    • (2002) J. Biol. Chem. , vol.277 , pp. 22147-22155
    • Mulugeta, S.1    Gray, J.M.2    Notarfrancesco, K.L.3    Gonzales, L.W.4    Koval, M.5
  • 63
    • 0026178541 scopus 로고
    • The relationship between lamellar bodies and lysosomes in type-II pneumocytes
    • Gibson KF, Widnell CC. 1991. The relationship between lamellar bodies and lysosomes in type-II pneumocytes. Am. J. Respir. Cell Mol. Biol. 4:504-13
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 504-513
    • Gibson, K.F.1    Widnell, C.C.2
  • 64
    • 0028171319 scopus 로고
    • Lamellar bodies of rat alveolar type II cells have late endosomal marker proteins on their limiting membranes
    • Wasano K, Hirakawa Y. 1994. Lamellar bodies of rat alveolar type II cells have late endosomal marker proteins on their limiting membranes. Biochemistry 102:329-35
    • (1994) Biochemistry , vol.102 , pp. 329-335
    • Wasano, K.1    Hirakawa, Y.2
  • 66
    • 0036428016 scopus 로고    scopus 로고
    • Biogenesis of lamellar bodies, lysosome-related organelles involved in storage and secretion of pulmonary surfactant
    • Weaver TE, Na CL, Stahlman M. 2002. Biogenesis of lamellar bodies, lysosome-related organelles involved in storage and secretion of pulmonary surfactant. Semin. Cell Dev. Biol. 13:263-70
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 263-270
    • Weaver, T.E.1    Na, C.L.2    Stahlman, M.3
  • 69
    • 0032246698 scopus 로고    scopus 로고
    • Trafficking of newly synthesized surfactant protein A in isolated rat alveolar type II cells
    • Osanai K, Mason RJ, Voelker DR. 1998. Trafficking of newly synthesized surfactant protein A in isolated rat alveolar type II cells. Am. J. Respir. Cell Mol. Biol. 19:929-35
    • (1998) Am. J. Respir. Cell Mol. Biol. , vol.19 , pp. 929-935
    • Osanai, K.1    Mason, R.J.2    Voelker, D.R.3
  • 70
    • 0035216688 scopus 로고    scopus 로고
    • Regulation of SP-B and SP-C secretion in rat type II cells in primary culture
    • Gobran LI, Rooney SA. 2001. Regulation of SP-B and SP-C secretion in rat type II cells in primary culture. Am. J. Physiol. Lung Cell Mol. Physiol. 281:L1413-19
    • (2001) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.281
    • Gobran, L.I.1    Rooney, S.A.2
  • 73
    • 0036014822 scopus 로고    scopus 로고
    • Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes
    • Brasch F, ten Brinke A, Johnen G, Ochs M, Kapp N, et al. 2002. Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am. J. Respir. Cell Mol. Biol. 26:659-70
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 659-670
    • Brasch, F.1    Ten Brinke, A.2    Johnen, G.3    Ochs, M.4    Kapp, N.5
  • 74
    • 0035091998 scopus 로고    scopus 로고
    • Post-translational processing of surfactant protein-C proprotein-targeting motifs in the NH2-terminal flanking domain are cleaved in late compartments
    • Johnson AL, Braidotti P, Pietra GG, Russo SJ, Kabore A, et al. 2001. Post-translational processing of surfactant protein-C proprotein-targeting motifs in the NH2-terminal flanking domain are cleaved in late compartments. Am. J. Respir. Cell Mol. Biol. 24:253-63
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.24 , pp. 253-263
    • Johnson, A.L.1    Braidotti, P.2    Pietra, G.G.3    Russo, S.J.4    Kabore, A.5
  • 76
    • 0026764197 scopus 로고
    • Binding, uptake, and localization of surfactant protein B in isolated rat alveolar type II cells
    • Breslin JS, Weaver TE. 1992. Binding, uptake, and localization of surfactant protein B in isolated rat alveolar type II cells. Am. J. Physiol. Lung Cell Mol. Physiol. 262:L699-707
    • (1992) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.262
    • Breslin, J.S.1    Weaver, T.E.2
  • 77
    • 0031740518 scopus 로고    scopus 로고
    • Surfactant protein metabolism in vivo
    • Ikegami M, Jobe AH. 1998. Surfactant protein metabolism in vivo. Biochim. Biophys. Acta 1408:218-25
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 218-225
    • Ikegami, M.1    Jobe, A.H.2
  • 81
    • 0027938716 scopus 로고
    • Localization, synthesis, and processing of surfactant protein SP-C in rat lung analyzed by epitope-specific antipeptide antibodies
    • Beers MF, Kim CY, Dodia C, Fisher AB. 1994. Localization, synthesis, and processing of surfactant protein SP-C in rat lung analyzed by epitope-specific antipeptide antibodies. J. Biol. Chem. 269:20318-28
    • (1994) J. Biol. Chem. , vol.269 , pp. 20318-20328
    • Beers, M.F.1    Kim, C.Y.2    Dodia, C.3    Fisher, A.B.4
  • 82
    • 0029198388 scopus 로고
    • Synthesis and processing of hydrophobic surfactant protein C by isolated rat type II cells
    • Beers MF, Lomax C. 1995. Synthesis and processing of hydrophobic surfactant protein C by isolated rat type II cells. Am. J. Physiol. Lung Cell Mol. Physiol. 269:L744-53
    • (1995) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.269
    • Beers, M.F.1    Lomax, C.2
  • 83
    • 0032511015 scopus 로고    scopus 로고
    • Synthetic processing of surfactant protein C by alveolar epithelial cells. The COOH terminus of proSP-C is required for posttranslational targeting and proteolysis
    • Beers MF, Lomax CA, Russo SJ. 1998. Synthetic processing of surfactant protein C by alveolar epithelial cells. The COOH terminus of proSP-C is required for posttranslational targeting and proteolysis. J. Biol. Chem. 273:15287-93
    • (1998) J. Biol. Chem. , vol.273 , pp. 15287-15293
    • Beers, M.F.1    Lomax, C.A.2    Russo, S.J.3
  • 85
    • 0025772694 scopus 로고
    • The pulmonary surfactant protein C (SP-C) precursor is a type II transmembrane protein
    • Keller A, Eistetter HR, Voss T, Schafer KP. 1991. The pulmonary surfactant protein C (SP-C) precursor is a type II transmembrane protein. Biochem. J. 277:493-99
    • (1991) Biochem. J. , vol.277 , pp. 493-499
    • Keller, A.1    Eistetter, H.R.2    Voss, T.3    Schafer, K.P.4
  • 86
    • 0026876757 scopus 로고
    • The C-terminal domain of the pulmonary surfactant protein C precursor contains signals for intracellular targeting
    • Keller A, Steinhilber W, Schafer KP, Voss T. 1992. The C-terminal domain of the pulmonary surfactant protein C precursor contains signals for intracellular targeting. Am. J. Respir. Cell Mol. Biol. 6:601-8
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 601-608
    • Keller, A.1    Steinhilber, W.2    Schafer, K.P.3    Voss, T.4
  • 88
    • 0347481366 scopus 로고    scopus 로고
    • Processing of surfactant protein C requires a type II transmembrane topology directed by juxtamembrane positively charged residues
    • Mulugeta S, Beers MF. 2003. Processing of surfactant protein C requires a type II transmembrane topology directed by juxtamembrane positively charged residues. J. Biol. Chem. 278:47979-86
    • (2003) J. Biol. Chem. , vol.278 , pp. 47979-47986
    • Mulugeta, S.1    Beers, M.F.2
  • 89
    • 0035805522 scopus 로고    scopus 로고
    • Secretion of surfactant protein C, an integral membrane protein, requires the N-terminal propeptide
    • Conkright JJ, Bridges JP, Na CL, Voorhout WF, Trapnell B, et al. 2001. Secretion of surfactant protein C, an integral membrane protein, requires the N-terminal propeptide. J. Biol. Chem. 276:14658-64
    • (2001) J. Biol. Chem. , vol.276 , pp. 14658-14664
    • Conkright, J.J.1    Bridges, J.P.2    Na, C.L.3    Voorhout, W.F.4    Trapnell, B.5
  • 90
    • 0035129262 scopus 로고    scopus 로고
    • Biosynthesis of surfactant protein C: Characterization of aggresome formation by EGFP chimeras containing propeptide mutants lacking conserved cysteine residues
    • Kabore AF, Wang WJ, Russo SJ, Beers MF. 2001. Biosynthesis of surfactant protein C: characterization of aggresome formation by EGFP chimeras containing propeptide mutants lacking conserved cysteine residues. J. Cell Sci. 114:293-302
    • (2001) J. Cell Sci. , vol.114 , pp. 293-302
    • Kabore, A.F.1    Wang, W.J.2    Russo, S.J.3    Beers, M.F.4
  • 92
    • 0030825096 scopus 로고    scopus 로고
    • Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: Detection of a surfactant protein C isoform containing Nepsilon-palmitoyllysine
    • Gustafsson M, Curstedt T, Jornvall H, Johansson J. 1997. Reverse-phase HPLC of the hydrophobic pulmonary surfactant proteins: detection of a surfactant protein C isoform containing Nepsilon-palmitoyllysine. Biochem. J. 326:799-806
    • (1997) Biochem. J. , vol.326 , pp. 799-806
    • Gustafsson, M.1    Curstedt, T.2    Jornvall, H.3    Johansson, J.4
  • 95
    • 0036014822 scopus 로고    scopus 로고
    • Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes
    • Brasch F, ten Brinke A, Johnen G, Ochs M, Kapp N, et al. 2002. Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am. J. Respir. Cell Mol. Biol. 26:659-70
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 659-670
    • Brasch, F.1    Ten Brinke, A.2    Johnen, G.3    Ochs, M.4    Kapp, N.5
  • 96
    • 20244388374 scopus 로고    scopus 로고
    • Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas
    • Chuman Y, Bergman AC, Ueno T, Saito S, Sakaguchi K, et al. 1999. Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas. FEBS Lett. 462:129-34
    • (1999) FEBS Lett. , vol.462 , pp. 129-134
    • Chuman, Y.1    Bergman, A.C.2    Ueno, T.3    Saito, S.4    Sakaguchi, K.5
  • 98
    • 0032740358 scopus 로고    scopus 로고
    • Human napsin A: Expression, immunochemical detection, and tissue localization
    • Schauer-Vukasinovic V, Bur D, Kling D, Gruninger F, Giller T. 1999. Human napsin A: expression, immunochemical detection, and tissue localization. FEBS Lett. 462:135-39
    • (1999) FEBS Lett. , vol.462 , pp. 135-139
    • Schauer-Vukasinovic, V.1    Bur, D.2    Kling, D.3    Gruninger, F.4    Giller, T.5
  • 101
    • 0022979193 scopus 로고
    • Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles
    • Orci L, Ravazzola M, Amherdt M, Madsen O, Perrelet A, et al. 1986. Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. J. Cell Biol. 103:2273-81
    • (1986) J. Cell Biol. , vol.103 , pp. 2273-2281
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Perrelet, A.5
  • 102
    • 0026567259 scopus 로고
    • Dicyclohexylcardiodimide and vanadate sensitive AtPase of lung lamellar bodies
    • Chander A. 1992. Dicyclohexylcardiodimide and vanadate sensitive AtPase of lung lamellar bodies. Biochim. Biophys. Acta 1123:198-206
    • (1992) Biochim. Biophys. Acta , vol.1123 , pp. 198-206
    • Chander, A.1
  • 103
    • 0028786984 scopus 로고
    • Partial deficiency of surfactant protein B in an infant with chronic lung disease
    • Ballard PL, Nogee LM, Beers MF, Ballard RA, Planer BC, et al. 1995. Partial deficiency of surfactant protein B in an infant with chronic lung disease. Pediatrics 96:1046-52
    • (1995) Pediatrics , vol.96 , pp. 1046-1052
    • Ballard, P.L.1    Nogee, L.M.2    Beers, M.F.3    Ballard, R.A.4    Planer, B.C.5
  • 104
    • 0027466161 scopus 로고
    • Brief report: Deficiency of pulmonary surfactant protein B in congenital alveolar proteinosis
    • Nogee LM, de Mello DE, Dehner LP, Colten HR. 1993. Brief report: deficiency of pulmonary surfactant protein B in congenital alveolar proteinosis. N. Engl. J. Med. 328:406-10
    • (1993) N. Engl. J. Med. , vol.328 , pp. 406-410
    • Nogee, L.M.1    De Mello, D.E.2    Dehner, L.P.3    Colten, H.R.4
  • 105
    • 0029096591 scopus 로고
    • Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice
    • Clark JC, Wert SE, Bachurski CJ, Stahlman MT, Stripp BR, et al. 1995. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. USA 92:7794-98
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7794-7798
    • Clark, J.C.1    Wert, S.E.2    Bachurski, C.J.3    Stahlman, M.T.4    Stripp, B.R.5
  • 107
    • 0037205503 scopus 로고    scopus 로고
    • Biosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domain
    • Wang WJ, Russo SJ, Mulugeta S, Beers MF. 2002. Biosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domain. J. Biol. Chem. 277:19929-37
    • (2002) J. Biol. Chem. , vol.277 , pp. 19929-19937
    • Wang, W.J.1    Russo, S.J.2    Mulugeta, S.3    Beers, M.F.4
  • 108
    • 3442875930 scopus 로고    scopus 로고
    • Interstitial lung disease and pulmonary alveolar proteinosis in a full-term baby with a de novo heterozygous mutation of surfactant protein C gene
    • Brasch F, Griese M, Tredano M, Johnen G, Ochs M, et al. 2004. Interstitial lung disease and pulmonary alveolar proteinosis in a full-term baby with a de novo heterozygous mutation of surfactant protein C gene. Eur. Respir. J. 24:30-39
    • (2004) Eur. Respir. J. , vol.24 , pp. 30-39
    • Brasch, F.1    Griese, M.2    Tredano, M.3    Johnen, G.4    Ochs, M.5
  • 109
    • 15544363978 scopus 로고    scopus 로고
    • Non-specific interstitial pneumonitis, alveolar proteinosis, and abnormal proprotein trafficking in a patient with a novel spontaneous mutation in surfactant protein C gene
    • In press
    • Stevens PA, Pettenazzo A, Baritussio A, Mulugeta S, Brasch F, et al. 2004. Non-specific interstitial pneumonitis, alveolar proteinosis, and abnormal proprotein trafficking in a patient with a novel spontaneous mutation in surfactant protein C gene. Pediatr. Res. In press
    • (2004) Pediatr. Res.
    • Stevens, P.A.1    Pettenazzo, A.2    Baritussio, A.3    Mulugeta, S.4    Brasch, F.5
  • 110
    • 0036629254 scopus 로고    scopus 로고
    • BRICHOS: A conserved domain in proteins associated with dementia, respiratory distress and cancer
    • Sanchez-Pulido L, Devos D, Valencia A. 2002. BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancer. Trends Biochem. Sci. 27:329-32
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 329-332
    • Sanchez-Pulido, L.1    Devos, D.2    Valencia, A.3
  • 111
    • 0035925577 scopus 로고    scopus 로고
    • Sequence, genomic structure and tissue expression of human BRI3, a member of the BRI gene family
    • Vidal R, Calero M, Revesz T, Plant G, Ghiso J, Frangione B. 2001. Sequence, genomic structure and tissue expression of human BRI3, a member of the BRI gene family. Gene 266:95-102
    • (2001) Gene , vol.266 , pp. 95-102
    • Vidal, R.1    Calero, M.2    Revesz, T.3    Plant, G.4    Ghiso, J.5    Frangione, B.6
  • 112
    • 0034712749 scopus 로고    scopus 로고
    • A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred
    • Vidal R, Revesz T, Rostagno A, Kim E, Holton JL, et al. 2000. A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred. Proc. Natl. Acad. Sci. USA 97:4920-25
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4920-4925
    • Vidal, R.1    Revesz, T.2    Rostagno, A.3    Kim, E.4    Holton, J.L.5
  • 113
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal R, Frangione B, Rostagno A, Mead S, Revesz T, Plant G, Ghiso J. 1999. A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399:776-81
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5    Plant, G.6    Ghiso, J.7
  • 114
    • 0034528382 scopus 로고    scopus 로고
    • Amyloidogenesis in familial British dementia is associated with a genetic defect on chromosome 13
    • Ghiso J, Vidal R, Rostagno A, Miravale L, Holton JL, et al. 2000. Amyloidogenesis in familial British dementia is associated with a genetic defect on chromosome 13. Ann. NY Acad. Sci. 920:84-92
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 84-92
    • Ghiso, J.1    Vidal, R.2    Rostagno, A.3    Miravale, L.4    Holton, J.L.5
  • 115
    • 1242351786 scopus 로고    scopus 로고
    • Proteolytic generation and aggregation of peptides from transmembrane regions: Lung surfactant protein C and amyloid beta-peptide
    • Johansson J, Weaver TE, Tjernberg LO. 2004. Proteolytic generation and aggregation of peptides from transmembrane regions: lung surfactant protein C and amyloid beta-peptide. Cell. Mol. Life Sci. 61:326-35
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 326-335
    • Johansson, J.1    Weaver, T.E.2    Tjernberg, L.O.3
  • 116
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease
    • Selkoe DJ. 2002. Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease. J. Clin. Invest. 110:1375-81
    • (2002) J. Clin. Invest. , vol.110 , pp. 1375-1381
    • Selkoe, D.J.1
  • 118
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I, Mahlke C, Yuan JY. 2003. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421:373-79
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.Y.3
  • 119
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai YH, Koppenhafer SL, Shoesmith SJ, Perez MK, Paulson HL. 1999. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8:673-82
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 673-682
    • Chai, Y.H.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 120
    • 0032894049 scopus 로고    scopus 로고
    • Impaired intracellular trafficking is a common disease mechanism of PMP22 point mutations in peripheral neuropathies
    • Naef R, Suter U. 1999. Impaired intracellular trafficking is a common disease mechanism of PMP22 point mutations in peripheral neuropathies. Neurobiol. Dis. 6:1-14
    • (1999) Neurobiol. Dis. , vol.6 , pp. 1-14
    • Naef, R.1    Suter, U.2
  • 121
    • 0037442389 scopus 로고    scopus 로고
    • Deletion of exon 4 from human surfactant protein C results in aggresome formation and generation of a dominant negative
    • Wang WJ, Mulugeta S, Russo SJ, Beers MF. 2003. Deletion of exon 4 from human surfactant protein C results in aggresome formation and generation of a dominant negative. J. Cell. Sci. 116:683-92
    • (2003) J. Cell. Sci. , vol.116 , pp. 683-692
    • Wang, W.J.1    Mulugeta, S.2    Russo, S.J.3    Beers, M.F.4
  • 122
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR. 2000. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10:524-30
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 123
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies-symptoms of cellular indigestion?
    • Kopito RR, Sitia R. 2000. Aggresomes and Russell bodies-symptoms of cellular indigestion? EMBO Rep. 1:225-31
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 124
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. 1998. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143:1883-98
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 125
    • 0346732280 scopus 로고    scopus 로고
    • Expression of a human SP-C mutation associated with interstitial lung disease disrupts lung development in transgenic mice
    • Bridges JP, Wert SE, Nogee LM, Weaver TE. 2003. Expression of a human SP-C mutation associated with interstitial lung disease disrupts lung development in transgenic mice. J. Biol. Chem. 278:52739-46
    • (2003) J. Biol. Chem. , vol.278 , pp. 52739-52746
    • Bridges, J.P.1    Wert, S.E.2    Nogee, L.M.3    Weaver, T.E.4
  • 126
    • 0036006803 scopus 로고    scopus 로고
    • Overexpression of surfactant protein-C mature peptide causes neonatal lethality in transgenic mice
    • Conkright JJ, Na CL, Weaver TE. 2002. Overexpression of surfactant protein-C mature peptide causes neonatal lethality in transgenic mice. Am. J. Respir. Cell Mol. Biol. 26:85-90
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 85-90
    • Conkright, J.J.1    Na, C.L.2    Weaver, T.E.3
  • 128
    • 0033829367 scopus 로고    scopus 로고
    • Interstitial pneumonia in Hermansky-Pudlak syndrome: Significance of florid foamy swelling/degeneration (giant lamellar body degeneration) of type-2 pneumocytes
    • Nakatani Y, Nakamura N, Sano J, Inayama Y, Kawano N, et al. 2000. Interstitial pneumonia in Hermansky-Pudlak syndrome: significance of florid foamy swelling/degeneration (giant lamellar body degeneration) of type-2 pneumocytes. Virchows Arch. Int. J. Pathol. 437:304-13
    • (2000) Virchows Arch. Int. J. Pathol. , vol.437 , pp. 304-313
    • Nakatani, Y.1    Nakamura, N.2    Sano, J.3    Inayama, Y.4    Kawano, N.5
  • 130
    • 0034177476 scopus 로고    scopus 로고
    • A new variant of Hermansky-Pudlak syndrome due to mutations in a gene responsible for vesicle formation
    • Shotelersuk V, Dell'Angelica EC, Hartnell L, Bonifacino JS, Gahl WA. 2000. A new variant of Hermansky-Pudlak syndrome due to mutations in a gene responsible for vesicle formation. Am. J. Med. 108:423-27
    • (2000) Am. J. Med. , vol.108 , pp. 423-427
    • Shotelersuk, V.1    Dell'Angelica, E.C.2    Hartnell, L.3    Bonifacino, J.S.4    Gahl, W.A.5
  • 131
    • 0034566189 scopus 로고    scopus 로고
    • Abnormal vesicular trafficking in mouse models of Hermansky-Pudlak syndrome
    • Swank RT, Novak EK, McGarry MP, Zhang YK, Li W, et al. 2000. Abnormal vesicular trafficking in mouse models of Hermansky-Pudlak syndrome. Pigment Cell Res. 13:59-67
    • (2000) Pigment Cell Res. , vol.13 , pp. 59-67
    • Swank, R.T.1    Novak, E.K.2    McGarry, M.P.3    Zhang, Y.K.4    Li, W.5
  • 133
    • 0036606871 scopus 로고    scopus 로고
    • Transmission of proteotoxicity across cellular compartments
    • Yoneda T, Urano F, Ron D. 2002. Transmission of proteotoxicity across cellular compartments. Genes Dev. 16:1307-13
    • (2002) Genes Dev. , vol.16 , pp. 1307-1313
    • Yoneda, T.1    Urano, F.2    Ron, D.3
  • 136
    • 0037189590 scopus 로고    scopus 로고
    • Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide
    • Augusto LA, Li J, Synguelakis M, Johansson J, Chaby R. 2002. Structural basis for interactions between lung surfactant protein C and bacterial lipopolysaccharide. J Biol. Chem. 277:23484-92
    • (2002) J. Biol. Chem. , vol.277 , pp. 23484-23492
    • Augusto, L.A.1    Li, J.2    Synguelakis, M.3    Johansson, J.4    Chaby, R.5
  • 139
    • 0034711207 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells
    • Chen F, Yang DS, Petanceska S, Yang A, Tandon A, et al. 2000. Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells. J. Biol. Chem. 275:36794-802
    • (2000) J. Biol. Chem. , vol.275 , pp. 36794-36802
    • Chen, F.1    Yang, D.S.2    Petanceska, S.3    Yang, A.4    Tandon, A.5
  • 140
    • 0032477873 scopus 로고    scopus 로고
    • The environmental dependency of protein folding best explains prion and amyloid diseases
    • Kelly JW. 1998. The environmental dependency of protein folding best explains prion and amyloid diseases. Proc. Natl. Acad. Sci. USA 95:930-32
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 930-932
    • Kelly, J.W.1
  • 141
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman RJ. 2002. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. 110:1389-98
    • (2002) J. Clin. Invest. , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 142
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R, Braakman I. 2003. Quality control in the endoplasmic reticulum protein factory. Nature 426:891-94
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 143
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton RY. 2002. ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 14:476-82
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 144
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Paul CK, Wodicka LF, Lockhart DJ, Weissman JS, Walter P. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-58
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Paul, C.K.2    Wodicka, L.F.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 145
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C, Walter P. 2001. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13:349-55
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 146
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, et al. 2002. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16:1345-55
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5
  • 147
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • Oyadomari S, Araki E, Mori M. 2002. Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis 7:335-45
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 148
    • 0035845568 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis in pancreatic beta cells is mediated by the endoplasmic reticulum stress pathway
    • Oyadomari S, Takeda K, Takiguchi M, Gotoh T, Matsumoto M, et al. 2001. Nitric oxide-induced apoptosis in pancreatic beta cells is mediated by the endoplasmic reticulum stress pathway. Proc. Natl. Acad. Sci. USA 98:10845-50
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10845-10850
    • Oyadomari, S.1    Takeda, K.2    Takiguchi, M.3    Gotoh, T.4    Matsumoto, M.5
  • 149
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S, Koizumi A, Takeda K, Gotoh T, Akira S, et al. 2002. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J. Clin. Invest. 109:525-32
    • (2002) J. Clin. Invest. , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5
  • 150
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I, Xu CJ, Juo P, Kakizaka A, Blenis J, Yuan JY. 1999. Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22:623-33
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.Y.6
  • 151
    • 0036005866 scopus 로고    scopus 로고
    • DeltaF508-CFTR causes constitutive NF-kappaB activation through an ER-overload response in cystic fibrosis lungs
    • Knorre A, Wagner M, Schaefer HE, Colledge WH, Pahl HL. 2002. DeltaF508-CFTR causes constitutive NF-kappaB activation through an ER-overload response in cystic fibrosis lungs. Biol. Chem. 383:271-82
    • (2002) Biol. Chem. , vol.383 , pp. 271-282
    • Knorre, A.1    Wagner, M.2    Schaefer, H.E.3    Colledge, W.H.4    Pahl, H.L.5
  • 152
    • 15544391202 scopus 로고    scopus 로고
    • Mutations within the BRICHOS domain of SP-C proprotein induce aggregation, caspase 3 expression, and cell toxicity
    • Abstr.
    • Beers MF, Russo SJ, Ngyuen V, Mulugeta S. 2004. Mutations within the BRICHOS domain of SP-C proprotein induce aggregation, caspase 3 expression, and cell toxicity. Am. J. Respir. Crit. Care Med. 169: A740 (Abstr.)
    • (2004) Am. J. Respir. Crit. Care Med. , vol.169
    • Beers, M.F.1    Russo, S.J.2    Ngyuen, V.3    Mulugeta, S.4
  • 154
    • 0034330457 scopus 로고    scopus 로고
    • Traffic jam: A compendium of human diseases that affect intracellular transport processes
    • Aridor M, Hannan LA. 2000. Traffic jam: a compendium of human diseases that affect intracellular transport processes. Traffic 1:836-51
    • (2000) Traffic , vol.1 , pp. 836-851
    • Aridor, M.1    Hannan, L.A.2
  • 155
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman MS, Kannegaard ES, Kopito RR. 2002. A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277:11709-14
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 156
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata R, Bebok Z, Sorscher EJ, Sztul ES. 1999. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 146:1239-54
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 157
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly JW. 1997. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 5:595-600
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 159
    • 0035137042 scopus 로고    scopus 로고
    • Regional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementia
    • Holton JL, Ghiso J, Lashley T, Rostagno A, Guerin CJ, et al. 2001. Regional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementia. Am. J. Pathol. 158:515-26
    • (2001) Am. J. Pathol. , vol.158 , pp. 515-526
    • Holton, J.L.1    Ghiso, J.2    Lashley, T.3    Rostagno, A.4    Guerin, C.J.5
  • 160
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR. 2001. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292:1552-55
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 161
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly JW. 2000. Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7:824-26
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 162
    • 0036238472 scopus 로고    scopus 로고
    • Towards an understanding of amyloidogenesis
    • Kelly JW. 2002. Towards an understanding of amyloidogenesis. Nat. Struct. Biol. 9:323-25
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 323-325
    • Kelly, J.W.1
  • 163
    • 0029001576 scopus 로고
    • A novel signal-transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
    • Pahl HL, Baeurele PA. 1995. A novel signal-transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B. EMBO J. 14:2580-88
    • (1995) EMBO J. , vol.14 , pp. 2580-2588
    • Pahl, H.L.1    Baeurele, P.A.2
  • 164
    • 0032779694 scopus 로고    scopus 로고
    • Signal transduction from the endoplasmic reticulum to the cell nucleus
    • Pahl HL. 1999. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol. Rev. 79:683-701
    • (1999) Physiol. Rev. , vol.79 , pp. 683-701
    • Pahl, H.L.1
  • 165
    • 0031080946 scopus 로고    scopus 로고
    • Endoplasmic-reticulum-induced signal transduction and gene expression
    • Pahl HL, Baeuerle PA. 1997. Endoplasmic-reticulum-induced signal transduction and gene expression. Trends Cell Biol. 7:50-55
    • (1997) Trends Cell Biol. , vol.7 , pp. 50-55
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 166
    • 0031081340 scopus 로고    scopus 로고
    • The ER-overload response: Activation of NF-κB
    • Pahl HL, Baeuerle PA. 1997. The ER-overload response: activation of NF-κB. Trends Biochem. Sci. 22:63-67
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 63-67
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 167
    • 0034805392 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate downregulates HSC70 expression by facilitating mRNA degradation
    • Rubenstein RC, Lyons BM. 2001. Sodium 4-phenylbutyrate downregulates HSC70 expression by facilitating mRNA degradation. Am. J. Physiol. Lung Cell Mol. Physiol. 281:L43-51
    • (2001) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.281
    • Rubenstein, R.C.1    Lyons, B.M.2
  • 168
    • 0034099743 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate downregulates Hsc70: Implications for intracellular trafficking of DeltaF508-CFTR
    • RubensteinRC, Zeitlin PL. 2000. Sodium 4-phenylbutyrate downregulates Hsc70: implications for intracellular trafficking of DeltaF508-CFTR. Am. J. Physiol. Cell Physiol. 278:C259-67
    • (2000) Am. J. Physiol. Cell Physiol. , vol.278
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 169
    • 0030809817 scopus 로고    scopus 로고
    • In vitro pharmacologie restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR
    • Rubenstein RC, Egan ME, Zeitlin PL. 1997. In vitro pharmacologie restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR. J. Clin. Invest. 100:2457-65
    • (1997) J. Clin. Invest. , vol.100 , pp. 2457-2465
    • Rubenstein, R.C.1    Egan, M.E.2    Zeitlin, P.L.3
  • 170
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows JA, Willis LK, Perlmutter DH. 2000. Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc. Natl. Acad. Sci. USA 97:1796-801
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 171
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: Partial restoration of nasal epithelial CFTR function
    • Rubenstein RC, Zeitlin PL. 1998. A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: partial restoration of nasal epithelial CFTR function. Am. J. Respir. Crit. Care Med. 157:484-90
    • (1998) Am. J. Respir. Crit. Care Med. , vol.157 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 172
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • Brown CR, Hong-Brown LQ, Biwersi J, Verkman AS, Welch WJ. 1996. Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1:117-25
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 173
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato S, Ward CL, Krouse ME, Wine JJ, Kopito RR. 1996. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271:635-38
    • (1996) J. Biol. Chem. , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.