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Volumn 1814, Issue 3, 2011, Pages 409-419

A novel approach for the purification and proteomic analysis of pathogenic immunoglobulin free light chains from serum

Author keywords

Amyloidosis; Immunoglobulin free light chains; Immunoprecipitation; Post translational modifications; Proteomics

Indexed keywords

AGAROSE; IMMUNOGLOBULIN KAPPA CHAIN; IMMUNOGLOBULIN LAMBDA CHAIN; TRYPTOPHAN;

EID: 78751642693     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.12.012     Document Type: Article
Times cited : (37)

References (33)
  • 2
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • DOI 10.1056/NEJMra023144
    • G. Merlini, and V. Bellotti Molecular mechanisms of amyloidosis N. Engl. J. Med. 349 2003 583 596 (Pubitemid 36951371)
    • (2003) New England Journal of Medicine , vol.349 , Issue.6 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 5
    • 0033855656 scopus 로고    scopus 로고
    • Review: Immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability
    • V. Bellotti, P. Mangione, and G. Merlini Review: Immunoglobulin light chain amyloidosis-the archetype of structural and pathogenic variability J. Struct. Biol. 130 2000 280 289
    • (2000) J. Struct. Biol. , vol.130 , pp. 280-289
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 6
    • 0032576990 scopus 로고    scopus 로고
    • Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: Kappa IV immunoglobulin light chain
    • DOI 10.1006/bbrc.1998.8515
    • K.E. Olsen, K. Sletten, and P. Westermark Extended analysis of Al-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain Biochem. Biophys. Res. Commun. 245 1998 713 716 (Pubitemid 28413983)
    • (1998) Biochemical and Biophysical Research Communications , vol.245 , Issue.3 , pp. 713-716
    • Olsen, K.E.1    Sletten, K.2    Westermark, P.3
  • 7
    • 37049002704 scopus 로고    scopus 로고
    • Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic κ1 immunoglobulin light chains
    • DOI 10.1021/bi7013773
    • L.H. Connors, Y. Jiang, M. Budnik, R. Theberge, T. Prokaeva, K.L. Bodi, D.C. Seldin, C.E. Costello, and M. Skinner Heterogeneity in primary structure, post-translational modifications, and germline gene usage of nine full-length amyloidogenic kapp a1 immunoglobulin light chains Biochemistry 46 2007 14259 14271 (Pubitemid 350250319)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14259-14271
    • Connors, L.H.1    Jiang, Y.2    Budnik, M.3    Theberge, R.4    Prokaeva, T.5    Bodi, K.L.6    Seldin, D.C.7    Costello, C.E.8    Skinner, M.9
  • 9
    • 58849090503 scopus 로고    scopus 로고
    • Free light chains in plasma of patients with light chain amyloidosis and non-amyloid light chain deposition disease. High proportion and heterogeneity of disulfide-linked monoclonal free light chains as pathogenic features of amyloid disease
    • B. Kaplan, M. Ramirez-Alvarado, L. Sikkink, S. Golderman, A. Dispenzieri, A. Livneh, and G. Gallo Free light chains in plasma of patients with light chain amyloidosis and non-amyloid light chain deposition disease. High proportion and heterogeneity of disulfide-linked monoclonal free light chains as pathogenic features of amyloid disease Br. J. Haematol. 144 2009 705 715
    • (2009) Br. J. Haematol. , vol.144 , pp. 705-715
    • Kaplan, B.1    Ramirez-Alvarado, M.2    Sikkink, L.3    Golderman, S.4    Dispenzieri, A.5    Livneh, A.6    Gallo, G.7
  • 10
    • 39849107358 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of plasma monoclonal free light chains in amyloidosis and multiple myeloma: A pilot study of intact and truncated forms of light chains and their charge properties
    • DOI 10.1515/CCLM.2008.068
    • B. Kaplan, M. Ramirez-Alvarado, A. Dispenzieri, S.R. Zeldenrust, N. Leung, A. Livneh, and G. Gallo Isolation and biochemical characterization of plasma monoclonal free light chains in amyloidosis and multiple myeloma: a pilot study of intact and truncated forms of light chains and their charge properties Clin. Chem. Lab. Med. 46 2008 335 341 (Pubitemid 351317768)
    • (2008) Clinical Chemistry and Laboratory Medicine , vol.46 , Issue.3 , pp. 335-341
    • Kaplan, B.1    Ramirez-Alvarado, M.2    Dispenzieri, A.3    Zeldenrust, S.R.4    Leung, N.5    Livneh, A.6    Gallo, G.7
  • 13
    • 0010739537 scopus 로고    scopus 로고
    • Inverse polymerase chain reaction for cloning complete human immunoglobulin variable regions and leaders conserving the original sequence
    • DOI 10.1006/abio.1996.0297
    • V. Perfetti, M. Sassano, P. Ubbiali, M.C. Vignarelli, E. Arbustini, A. Corti, and G. Merlini Inverse polymerase chain reaction for cloning complete human immunoglobulin variable regions and leaders conserving the original sequence Anal. Biochem. 239 1996 107 109 (Pubitemid 26256290)
    • (1996) Analytical Biochemistry , vol.239 , Issue.1 , pp. 107-109
    • Perfetti, V.1    Sassano, M.2    Ubbiali, P.3    Vignarelli, M.C.4    Arbustini, E.5    Corti, A.6    Merlini, G.7
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 21744435256 scopus 로고    scopus 로고
    • Identification of proteins released by pancreatic cancer cells by multidimensional protein identification technology: A strategy for identification of novel cancer markers
    • DOI 10.1096/fj.04-3000fje
    • P. Mauri, A. Scarpa, A.C. Nascimbeni, L. Benazzi, E. Parmagnani, A. Mafficini, M. Della Peruta, C. Bassi, K. Miyazaki, and C. Sorio Identification of proteins released by pancreatic cancer cells by multidimensional protein identification technology: a strategy for identification of novel cancer markers FASEB J. 19 2005 1125 1127 (Pubitemid 40946439)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1125-1127
    • Mauri, P.1    Scarpa, A.2    Nascimbeni, A.C.3    Benazzi, L.4    Parmagnani, E.5    Mafficini, A.6    Della Peruta, M.7    Bassi, C.8    Miyazaki, K.9    Sorio, C.10
  • 16
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • M.P. Washburn, D. Wolters, and J.R. Yates III Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 19 2001 242 247 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 18
    • 0029111662 scopus 로고
    • Structural and functional properties of human lambda-light-chain variable-region subgroups
    • A. Solomon, and D.T. Weiss Structural and functional properties of human lambda-light-chain variable-region subgroups Clin. Diagn. Lab. Immunol. 2 1995 387 394
    • (1995) Clin. Diagn. Lab. Immunol. , vol.2 , pp. 387-394
    • Solomon, A.1    Weiss, D.T.2
  • 19
    • 0035437144 scopus 로고    scopus 로고
    • The tropism of organ involvement in primary systemic amyloidosis: Contributions of Ig V(L) germ line gene use and clonal plasma cell burden
    • R.L. Comenzo, Y. Zhang, C. Martinez, K. Osman, and G.A. Herrera The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig V(L) germ line gene use and clonal plasma cell burden Blood 98 2001 714 720
    • (2001) Blood , vol.98 , pp. 714-720
    • Comenzo, R.L.1    Zhang, Y.2    Martinez, C.3    Osman, K.4    Herrera, G.A.5
  • 20
    • 0016998398 scopus 로고
    • Polymeric forms of free light chains in serum from normal individuals and from patients with renal diseases
    • K. Solling Polymeric forms of free light chains in serum from normal individuals and from patients with renal diseases Scand. J. Clin. Lab. Invest. 36 1976 447 452
    • (1976) Scand. J. Clin. Lab. Invest. , vol.36 , pp. 447-452
    • Solling, K.1
  • 21
    • 0018904899 scopus 로고
    • Light chain polymerism in normal individuals, in patients with severe proteinuria and in normals with inhibited tubular protein reabsorption by lysine
    • K. Solling Light chain polymerism in normal individuals in patients with severe proteinuria and in normals with inhibited tubular protein reabsorption by lysine Scand. J. Clin. Lab. Invest. 40 1980 129 134 (Pubitemid 10132134)
    • (1980) Scandinavian Journal of Clinical and Laboratory Investigation , vol.40 , Issue.2 , pp. 129-134
    • Solling, K.1
  • 23
    • 77953911347 scopus 로고    scopus 로고
    • Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
    • I. Perdivara, L.J. Deterding, M. Przybylski and K.B. Tomer, Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification?, J. Am. Soc. Mass. Spectrom. 21 1114-7.
    • J. Am. Soc. Mass. Spectrom. , vol.21 , pp. 1114-1147
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 24
    • 2342525940 scopus 로고    scopus 로고
    • Human Amyloidogenic Light Chains Directly Impair Cardiomyocyte Function Through an Increase in Cellular Oxidant Stress
    • DOI 10.1161/01.RES.0000126569.75419.74
    • D.A. Brenner, M. Jain, D.R. Pimentel, B. Wang, L.H. Connors, M. Skinner, C.S. Apstein, and R. Liao Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress Circ. Res. 94 2004 1008 1010 (Pubitemid 38579694)
    • (2004) Circulation Research , vol.94 , Issue.8 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3    Wang, B.4    Connors, L.H.5    Skinner, M.6    Apstein, C.S.7    Liao, R.8
  • 25
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 26
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine α-crystallin
    • E.L. Finley, J. Dillon, R.K. Crouch, and K.L. Schey Identification of tryptophan oxidation products in bovine alpha-crystallin Protein Sci. 7 1998 2391 2397 (Pubitemid 28506955)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 28
    • 0014877288 scopus 로고
    • Conformational significance of the intrachain disulfide linkages in immunoglobulins
    • G.W. Litman, R.A. Good, D. Frommel, and A. Rosenberg Conformational significance of the intrachain disulfide linkages in immunoglobulins Proc. Natl Acad. Sci. USA 67 1970 1085 1092
    • (1970) Proc. Natl Acad. Sci. USA , vol.67 , pp. 1085-1092
    • Litman, G.W.1    Good, R.A.2    Frommel, D.3    Rosenberg, A.4
  • 29
    • 0022332420 scopus 로고
    • Immunoglobulin disulfide bridges: Theme and variations
    • DOI 10.1007/BF01119910
    • L.A. Steiner Immunoglobulin disulfide bridges: theme and variations Biosci. Rep. 5 1985 973 989 (Pubitemid 16153500)
    • (1985) Bioscience Reports , vol.5 , Issue.10-11 , pp. 973-989
    • Steiner, L.A.1
  • 30
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • J.A. Vrana, J.D. Gamez, B.J. Madden, J.D. Theis, H.R. Bergen III, and A. Dogan Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens Blood 114 2009 4957 4959
    • (2009) Blood , vol.114 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3    Theis, J.D.4    Bergen III, H.R.5    Dogan, A.6
  • 32
    • 0026739326 scopus 로고
    • Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG
    • M.R. Wilson, and S.B. Easterbrook-Smith Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG Biochim. Biophys. Acta 1159 1992 319 326
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 319-326
    • Wilson, M.R.1    Easterbrook-Smith, S.B.2


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