메뉴 건너뛰기




Volumn 396, Issue 2, 2010, Pages 375-383

Kinetic instability of the serpin Z α1-antitrypsin promotes aggregation

Author keywords

Aggregation; Metastability; Misfolding; Polymerization; Serpin

Indexed keywords

ALPHA 1 ANTITRYPSIN; GUANIDINE; SERINE PROTEINASE INHIBITOR; UREA; ISOPROTEIN;

EID: 77449144020     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.11.048     Document Type: Article
Times cited : (44)

References (46)
  • 1
    • 46149105683 scopus 로고    scopus 로고
    • Hereditary alpha-1-antitrypsin deficiency and its clinical consequences
    • Fregonese L., Stolk J. Hereditary alpha-1-antitrypsin deficiency and its clinical consequences. Orphanet J. Rare Dis. 2008, 3:16.
    • (2008) Orphanet J. Rare Dis. , vol.3 , pp. 16
    • Fregonese, L.1    Stolk, J.2
  • 2
    • 0019453831 scopus 로고
    • Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema
    • Gadek J.E., Fells G.A., Zimmerman R.L., Rennard S.I., Crystal R.G. Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema. J. Clin. Invest. 1981, 68:889-898.
    • (1981) J. Clin. Invest. , vol.68 , pp. 889-898
    • Gadek, J.E.1    Fells, G.A.2    Zimmerman, R.L.3    Rennard, S.I.4    Crystal, R.G.5
  • 5
    • 0024397003 scopus 로고
    • Serum alpha 1-antitrypsin deficiency associated with the common S-type (Glu264-Val) mutation results from intracellular degradation of alpha 1-antitrypsin prior to secretion
    • Curiel D.T., Chytil A., Courtney M., Crystal R.G. Serum alpha 1-antitrypsin deficiency associated with the common S-type (Glu264-Val) mutation results from intracellular degradation of alpha 1-antitrypsin prior to secretion. J. Biol. Chem. 1989, 264:10477-10486.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10477-10486
    • Curiel, D.T.1    Chytil, A.2    Courtney, M.3    Crystal, R.G.4
  • 7
    • 0029012309 scopus 로고
    • Alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization
    • Lomas D.A., Elliott P.R., Sidhar S.K., Foreman R.C., Finch J.T., Cox D.W., et al. alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization. J. Biol. Chem. 1995, 270:16864-16870.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16864-16870
    • Lomas, D.A.1    Elliott, P.R.2    Sidhar, S.K.3    Foreman, R.C.4    Finch, J.T.5    Cox, D.W.6
  • 8
    • 0027295822 scopus 로고
    • Alpha 1-Antitrypsin Siiyama (Ser53{combining right arrow above}Phe). Further evidence for intracellular loop-sheet polymerization
    • Lomas D.A., Finch J.T., Seyama K., Nukiwa T., Carrell R.W. alpha 1-Antitrypsin Siiyama (Ser53{combining right arrow above}Phe). Further evidence for intracellular loop-sheet polymerization. J. Biol. Chem. 1993, 268:15333-15335.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15333-15335
    • Lomas, D.A.1    Finch, J.T.2    Seyama, K.3    Nukiwa, T.4    Carrell, R.W.5
  • 9
    • 0021151426 scopus 로고
    • Occurrence of alpha-1-antitrypsin deficiency in 155 patients with alcoholic liver disease
    • Roberts E.A., Cox D.W., Medline A., Wanless I.R. Occurrence of alpha-1-antitrypsin deficiency in 155 patients with alcoholic liver disease. Am. J. Clin. Pathol. 1984, 82:424-427.
    • (1984) Am. J. Clin. Pathol. , vol.82 , pp. 424-427
    • Roberts, E.A.1    Cox, D.W.2    Medline, A.3    Wanless, I.R.4
  • 10
    • 0025923680 scopus 로고
    • Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone
    • Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S. Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone. J. Biol. Chem. 1991, 266:12627-12632.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12627-12632
    • Seyama, K.1    Nukiwa, T.2    Takabe, K.3    Takahashi, H.4    Miyake, K.5    Kira, S.6
  • 11
    • 2942638034 scopus 로고    scopus 로고
    • 1-Antitrypsin deficiency: 4. Molecular pathophysiology
    • 1-Antitrypsin deficiency: 4. Molecular pathophysiology. Thorax 2004, 59:529-535.
    • (2004) Thorax , vol.59 , pp. 529-535
    • Lomas, D.A.1    Parfrey, H.2
  • 12
    • 20744450475 scopus 로고    scopus 로고
    • Antitrypsin deficiency
    • Stoller J.K., Aboussouan L.S. Antitrypsin deficiency. Lancet 2005, 365:2225-2236.
    • (2005) Lancet , vol.365 , pp. 2225-2236
    • Stoller, J.K.1    Aboussouan, L.S.2
  • 13
    • 22244489354 scopus 로고    scopus 로고
    • A review of alpha-1 antitrypsin deficiency
    • Ioachimescu O.C., Stoller J.K. A review of alpha-1 antitrypsin deficiency. COPD 2005, 2:263-275.
    • (2005) COPD , vol.2 , pp. 263-275
    • Ioachimescu, O.C.1    Stoller, J.K.2
  • 14
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H., Tokuoka R., Deisenhofer J., Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 1984, 177:531-557.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 15
    • 0036510604 scopus 로고    scopus 로고
    • 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis
    • Mahadeva R., Dafforn T.R., Carrell R.W., Lomas D.A. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related 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
  • 16
    • 0032529612 scopus 로고    scopus 로고
    • The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopy
    • James E.L., Bottomley S.P. The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopy. Arch. Biochem. Biophys. 1998, 356:296-300.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 296-300
    • James, E.L.1    Bottomley, S.P.2
  • 24
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin
    • Lomas D.A., Evans D.L., Stone S.R., Chang W.S., Carrell R.W. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. Biochemistry 1993, 32:500-508.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.S.4    Carrell, R.W.5
  • 25
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki M., Li W., Johnson D.J., Huntington J.A. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 2008, 455:1255-1258.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 26
    • 0029048542 scopus 로고
    • The Z type variation of human alpha 1-antitrypsin causes a protein folding defect
    • Yu M.H., Lee K.N., Kim J. The Z type variation of human alpha 1-antitrypsin causes a protein folding defect. Nat. Struct. Biol. 1995, 2:363-367.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 363-367
    • Yu, M.H.1    Lee, K.N.2    Kim, J.3
  • 27
    • 70349446583 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant Z alpha(1)-antitrypsin-the most common cause of alpha(1)-antitrypsin deficiency
    • Levina V., Dai W., Knaupp A.S., Kaiserman D., Pearce M.C., Cabrita L.D., et al. Expression, purification and characterization of recombinant Z alpha(1)-antitrypsin-the most common cause of alpha(1)-antitrypsin deficiency. Protein Expression Purif. 2009, 68:226-232.
    • (2009) Protein Expression Purif. , vol.68 , pp. 226-232
    • Levina, V.1    Dai, W.2    Knaupp, A.S.3    Kaiserman, D.4    Pearce, M.C.5    Cabrita, L.D.6
  • 28
    • 3042617720 scopus 로고    scopus 로고
    • How do proteins avoid becoming too stable? Biophysical studies into metastable proteins
    • Cabrita L.D., Bottomley S.P. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur. Biophys. J. 2004, 33:83-88.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 83-88
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 29
    • 34848911346 scopus 로고    scopus 로고
    • Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap
    • Cabrita L.D., Irving J.A., Pearce M.C., Whisstock J.C., Bottomley S.P. Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. J. Biol. Chem. 2007, 282:26802-26809.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26802-26809
    • Cabrita, L.D.1    Irving, J.A.2    Pearce, M.C.3    Whisstock, J.C.4    Bottomley, S.P.5
  • 30
    • 0026504260 scopus 로고
    • Effects of glycosylation on the folding and stability of human, recombinant and cleaved alpha 1-antitrypsin
    • Powell L.M., Pain R.H. Effects of glycosylation on the folding and stability of human, recombinant and cleaved alpha 1-antitrypsin. J. Mol. Biol. 1992, 224:241-252.
    • (1992) J. Mol. Biol. , vol.224 , pp. 241-252
    • Powell, L.M.1    Pain, R.H.2
  • 31
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition
    • Cabrita L.D., Dai W., Bottomley S.P. Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition. Biochemistry 2004, 43:9834-9839.
    • (2004) Biochemistry , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 32
    • 0035834481 scopus 로고    scopus 로고
    • Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state
    • Tew D.J., Bottomley S.P. Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. J. Mol. Biol. 2001, 313:1161-1169.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1161-1169
    • Tew, D.J.1    Bottomley, S.P.2
  • 33
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little of stability of barnase
    • Sali D., Bycroft M., Fersht A.R. Surface electrostatic interactions contribute little of stability of barnase. J. Mol. Biol. 1991, 220:779-788.
    • (1991) J. Mol. Biol. , vol.220 , pp. 779-788
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 34
    • 34447522226 scopus 로고    scopus 로고
    • The mechanism of the amyloidogenic conversion of T7 endonuclease I
    • Guo Z., Eisenberg D. The mechanism of the amyloidogenic conversion of T7 endonuclease I. J. Biol. Chem. 2007, 282:14968-14974.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14968-14974
    • Guo, Z.1    Eisenberg, D.2
  • 35
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease
    • Chow M.K., Ellisdon A.M., Cabrita L.D., Bottomley S.P. Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 2004, 279:47643-47651.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 36
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon A.M., Thomas B., Bottomley S.P. The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 2006, 281:16888-16896.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 37
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann S., Glockshuber R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 1999, 38:3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 38
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki W., Petersen R.B., Gambetti P., Surewicz W.K. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 1998, 273:31048-31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 39
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 1986, 131:266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 41
    • 0034665989 scopus 로고    scopus 로고
    • Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsin
    • Pearce M.C., Rubin H., Bottomley S.P. Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsin. J. Biol. Chem. 2000, 275:28513-28518.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28513-28518
    • Pearce, M.C.1    Rubin, H.2    Bottomley, S.P.3
  • 43
    • 0347753712 scopus 로고    scopus 로고
    • Physical characterization of serpin conformations
    • Dafforn T.R., Pike R.N., Bottomley S.P. Physical characterization of serpin conformations. Methods 2004, 32:150-158.
    • (2004) Methods , vol.32 , pp. 150-158
    • Dafforn, T.R.1    Pike, R.N.2    Bottomley, S.P.3
  • 45
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: the Job plot
    • Huang C.Y. Determination of binding stoichiometry by the continuous variation method: the Job plot. Methods Enzymol. 1982, 87:509-525.
    • (1982) Methods Enzymol. , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 46
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 1971, 10:3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.