메뉴 건너뛰기




Volumn 72, Issue 2, 2008, Pages 684-692

Influence of the germline sequence on the thermodynamic stability and fibrillogenicity of human lambda 6 light chains

Author keywords

Amyloid; Cation ; Fibrillogenesis; Light chain

Indexed keywords

IMMUNOGLOBULIN LIGHT CHAIN; RECOMBINANT PROTEIN;

EID: 46449138131     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21934     Document Type: Article
Times cited : (60)

References (44)
  • 1
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)
    • Solomon A, Weiss DT. Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis). Amyloid 1995;2:269-279.
    • (1995) Amyloid , vol.2 , pp. 269-279
    • Solomon, A.1    Weiss, D.T.2
  • 3
    • 0019951737 scopus 로고
    • Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda)
    • Solomon A, Frangione B, Franklin EC. Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda). J Clin Invest 1982;70:453-460.
    • (1982) J Clin Invest , vol.70 , pp. 453-460
    • Solomon, A.1    Frangione, B.2    Franklin, E.C.3
  • 4
    • 0028351369 scopus 로고
    • Preferential expression of human-lambda light chain variable-region subgroups in multiple myeloma, AL amyloidosis, and Waldenstrom's macroglobulinemia
    • Ozaki S, Abe M, Wolfenbarger D, Weiss DT, Solomon A. Preferential expression of human-lambda light chain variable-region subgroups in multiple myeloma, AL amyloidosis, and Waldenstrom's macroglobulinemia. Clin Immunol Immunopathol 1994;71:183-189.
    • (1994) Clin Immunol Immunopathol , vol.71 , pp. 183-189
    • Ozaki, S.1    Abe, M.2    Wolfenbarger, D.3    Weiss, D.T.4    Solomon, A.5
  • 6
    • 0036682487 scopus 로고    scopus 로고
    • Analysis of Vλ-Jλ expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (λIII) as a new amyloid-associated germline gene segment
    • Perfetti V, Casarini S, Palladini G, Vignarelli MC, Klersy C, Diegoli M, Ascari E, Merlini G. Analysis of Vλ-Jλ expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (λIII) as a new amyloid-associated germline gene segment. Blood 2002;100:948-953.
    • (2002) Blood , vol.100 , pp. 948-953
    • Perfetti, V.1    Casarini, S.2    Palladini, G.3    Vignarelli, M.C.4    Klersy, C.5    Diegoli, M.6    Ascari, E.7    Merlini, G.8
  • 7
    • 0038264427 scopus 로고    scopus 로고
    • Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL)
    • Abraham RS, Geyer SM, Price-Troska TL, Allmer C, Kyle RA, Gerzt MA, Fonseca R. Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003;101:3801-3808.
    • (2003) Blood , vol.101 , pp. 3801-3808
    • Abraham, R.S.1    Geyer, S.M.2    Price-Troska, T.L.3    Allmer, C.4    Kyle, R.A.5    Gerzt, M.A.6    Fonseca, R.7
  • 12
    • 0345426278 scopus 로고    scopus 로고
    • Thermodynamic instability of human λ6 light chain: Correlation with fibrillogenicity
    • Wall J, Schell M, Murphy C, Hrncic R, Stevens FJ, Solomon A. Thermodynamic instability of human λ6 light chain: correlation with fibrillogenicity. Biochemistry 1999;38:14101-14108.
    • (1999) Biochemistry , vol.38 , pp. 14101-14108
    • Wall, J.1    Schell, M.2    Murphy, C.3    Hrncic, R.4    Stevens, F.J.5    Solomon, A.6
  • 13
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light chain amyloidosis
    • Hurle MR, Helms LR, Li L, Chan W, Wetzel R. A role for destabilizing amino acid replacements in light chain amyloidosis. Proc Natl Acad Sci USA 1994;91:5446-5450.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 16
    • 1442302320 scopus 로고    scopus 로고
    • Toward understanding the structure-function relationship of human amyloid disease
    • Dealwis C, Wall JS. Toward understanding the structure-function relationship of human amyloid disease. Curr Drug Targets 2004;5:159-171.
    • (2004) Curr Drug Targets , vol.5 , pp. 159-171
    • Dealwis, C.1    Wall, J.S.2
  • 17
    • 3142641190 scopus 로고    scopus 로고
    • Structural basis of light chain amyloidogenicity: Comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vλ6 proteins
    • Wall JS, Gupta V, Wilkerson M, Schell M, Loris R, Adams P, Solomon A, Stevens F, Dealwis C. Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vλ6 proteins. J Mol Recognit 2004;17:323-331.
    • (2004) J Mol Recognit , vol.17 , pp. 323-331
    • Wall, J.S.1    Gupta, V.2    Wilkerson, M.3    Schell, M.4    Loris, R.5    Adams, P.6    Solomon, A.7    Stevens, F.8    Dealwis, C.9
  • 18
    • 30344437893 scopus 로고    scopus 로고
    • The CDR1 of the human λVI light chains adopts a new canonical structure
    • del Pozo Yauner L, Ortiz E, Becerril B. The CDR1 of the human λVI light chains adopts a new canonical structure. Proteins 2006;62:122-129.
    • (2006) Proteins , vol.62 , pp. 122-129
    • del Pozo Yauner, L.1    Ortiz, E.2    Becerril, B.3
  • 19
    • 0027050148 scopus 로고
    • Recursive PCR: A novel technique for total gene synthesis
    • Prodromou C, Pearl LH. Recursive PCR: a novel technique for total gene synthesis. Protein Eng 1992;5:827-829.
    • (1992) Protein Eng , vol.5 , pp. 827-829
    • Prodromou, C.1    Pearl, L.H.2
  • 23
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenyl-methanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenyl-methanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 1988;27:8063-8074.
    • (1988) Biochemistry , vol.27 , pp. 8063-8074
    • Santoro, M.M.1    Bolen, D.W.2
  • 24
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, editor, Oxford: IRL Press;
    • Pace CN, Shirley BA, Thomson JA. Measuring the conformational stability of a protein. In: Creighton TE, editor. Protein structure: a practical approach. Oxford: IRL Press; 1989. pp 311-330.
    • (1989) Protein structure: A practical approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 25
    • 0031434523 scopus 로고    scopus 로고
    • An alternative approach in the structure-based predictions of the thermodynamic of protein unfolding
    • Milardi D, la Rosa C, Fasone S, Grasso D. An alternative approach in the structure-based predictions of the thermodynamic of protein unfolding. Biophys Chem 1997;69:43-51.
    • (1997) Biophys Chem , vol.69 , pp. 43-51
    • Milardi, D.1    la Rosa, C.2    Fasone, S.3    Grasso, D.4
  • 26
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescen dye, thioflavin T1
    • Naiki H, Higuchi K, Hosokawa M, Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescen dye, thioflavin T1. Anal Biochem 1989;177:244-249.
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 27
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrilogenesis
    • Wall J, Murphy CL, Solomon A. In vitro immunoglobulin light chain fibrilogenesis. Methods Enzymol 1999;309:204-216.
    • (1999) Methods Enzymol , vol.309 , pp. 204-216
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 28
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk WE, Jacob RF and Mason RP. Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol 1999;309:285-305.
    • (1999) Methods Enzymol , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 31
    • 33745698477 scopus 로고    scopus 로고
    • The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein
    • McLaughlin RW, De Stigter JK, Sikkink LA, Baden EM, Ramirez-Alvarado M. The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein. Protein Sci 2006;15:1710-1722.
    • (2006) Protein Sci , vol.15 , pp. 1710-1722
    • McLaughlin, R.W.1    De Stigter, J.K.2    Sikkink, L.A.3    Baden, E.M.4    Ramirez-Alvarado, M.5
  • 32
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN
    • Souillac PO, Uversky VN, Fink AL. Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN. Biochemistry 2003;42:8094-8104.
    • (2003) Biochemistry , vol.42 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 34
    • 0033865983 scopus 로고    scopus 로고
    • Binding of nascent collagen by amyloidogenic light chains and amyloid fibrillogenesis in monolayers of human fibrocytes
    • Harris DL, King E, Ramsland PA, Edmundson AB. Binding of nascent collagen by amyloidogenic light chains and amyloid fibrillogenesis in monolayers of human fibrocytes. J Mol Recognit 2000;13:198-212.
    • (2000) J Mol Recognit , vol.13 , pp. 198-212
    • Harris, D.L.1    King, E.2    Ramsland, P.A.3    Edmundson, A.B.4
  • 35
    • 0032235059 scopus 로고    scopus 로고
    • In vitro modulation of AL-amyloid formation by human mesangial cells exposed to amyloidogenic light chains
    • Issac J, Kerby JD, Russell WJ, Dempsey SC, Sanders PW, Herrera GA. In vitro modulation of AL-amyloid formation by human mesangial cells exposed to amyloidogenic light chains. Amyloid 1998;5:238-246.
    • (1998) Amyloid , vol.5 , pp. 238-246
    • Issac, J.1    Kerby, J.D.2    Russell, W.J.3    Dempsey, S.C.4    Sanders, P.W.5    Herrera, G.A.6
  • 36
    • 2342459810 scopus 로고    scopus 로고
    • Different types of glomerulopathic light chains interact with mesangial cells using a common receptor but exhibit different intracellular trafficking patterns
    • Teng J, Russell WJ, Gu X, Cardelli J, Lamar-Jones M, Herrera G. Different types of glomerulopathic light chains interact with mesangial cells using a common receptor but exhibit different intracellular trafficking patterns. Lab Invest 2004;84:440-451.
    • (2004) Lab Invest , vol.84 , pp. 440-451
    • Teng, J.1    Russell, W.J.2    Gu, X.3    Cardelli, J.4    Lamar-Jones, M.5    Herrera, G.6
  • 37
    • 0028153795 scopus 로고
    • Planar stacking interactions of arginine and aromatic side-chains in proteins
    • Flocco MM, Mowbray SL. Planar stacking interactions of arginine and aromatic side-chains in proteins. J Mol Biol 1994;235:709-717.
    • (1994) J Mol Biol , vol.235 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 40
  • 42
    • 0037642529 scopus 로고    scopus 로고
    • Local and long-range structural effects caused by the removal of the N-terminal polypeptide fragment from immunoglobulin L chain λ
    • Krol M, Roterman I, Piekarska B, Konieczny L, Rybarska J, Stopa B. Local and long-range structural effects caused by the removal of the N-terminal polypeptide fragment from immunoglobulin L chain λ. Biopolymers 2003;69:189-200.
    • (2003) Biopolymers , vol.69 , pp. 189-200
    • Krol, M.1    Roterman, I.2    Piekarska, B.3    Konieczny, L.4    Rybarska, J.5    Stopa, B.6
  • 43
    • 33846781607 scopus 로고    scopus 로고
    • Localization of a conformational epitope common to nonnative and fibrillar immunoglobulin light chains
    • O'nuallain B, Allen A, Kennel SJ, Weiss DT, Solomon A, Wall JS. Localization of a conformational epitope common to nonnative and fibrillar immunoglobulin light chains. Biochemistry 2007;46:1240-1247.
    • (2007) Biochemistry , vol.46 , pp. 1240-1247
    • O'nuallain, B.1    Allen, A.2    Kennel, S.J.3    Weiss, D.T.4    Solomon, A.5    Wall, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.