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Volumn 135, Issue 1-3, 2008, Pages 25-31

Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain

Author keywords

Amyloid; Hofmeister salts; Immunoglobulin light chain; Light Chain Amyloidosis; Protein stability

Indexed keywords

AL 12 PROTEIN; AMYLOID; IMMUNOGLOBULIN LIGHT CHAIN; ION; SODIUM CHLORIDE; SULFATE;

EID: 43049148991     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.02.019     Document Type: Article
Times cited : (47)

References (31)
  • 2
    • 0030830020 scopus 로고    scopus 로고
    • Domain stability in immunoglobulin light chain deposition disorders
    • Wetzel R. Domain stability in immunoglobulin light chain deposition disorders. Adv. Protein. Chem. 50 (1997) 183-242
    • (1997) Adv. Protein. Chem. , vol.50 , pp. 183-242
    • Wetzel, R.1
  • 3
    • 0033807726 scopus 로고    scopus 로고
    • Four structural risk factors identify most fibril-forming kappa light chains
    • Stevens F.J. Four structural risk factors identify most fibril-forming kappa light chains. Amyloid 7 (2000) 200-211
    • (2000) Amyloid , vol.7 , pp. 200-211
    • Stevens, F.J.1
  • 4
    • 0345426278 scopus 로고    scopus 로고
    • Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity.
    • Wall J., Schell M., Murphy C., Hrncic R., Stevens F.J., and Solomon A. Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 38 (1999) 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
  • 8
    • 2642544056 scopus 로고    scopus 로고
    • Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy
    • Zhu M., Han S., Zhou F., Carter S.A., and Fink A.L. Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy. J. Biol. Chem. 279 (2004) 24452-24459
    • (2004) J. Biol. Chem. , vol.279 , pp. 24452-24459
    • Zhu, M.1    Han, S.2    Zhou, F.3    Carter, S.A.4    Fink, A.L.5
  • 9
    • 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 R.W., De Stigter J.K., Sikkink L.A., Baden E.M., and 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. 15 (2006) 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
  • 10
    • 0037369167 scopus 로고    scopus 로고
    • Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro
    • Ramirez-Alvarado M., Cocco M.J., and Regan L. Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro. Protein. Sci. 12 (2003) 567-576
    • (2003) Protein. Sci. , vol.12 , pp. 567-576
    • Ramirez-Alvarado, M.1    Cocco, M.J.2    Regan, L.3
  • 11
    • 13444269021 scopus 로고    scopus 로고
    • Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability
    • Raman B., Chatani E., Kihara M., Ban T., Sakai M., Hasegawa K., Naiki H., Rao C.M., and Goto Y. Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability. Biochemistry 44 (2005) 1288-1299
    • (2005) Biochemistry , vol.44 , pp. 1288-1299
    • Raman, B.1    Chatani, E.2    Kihara, M.3    Ban, T.4    Sakai, M.5    Hasegawa, K.6    Naiki, H.7    Rao, C.M.8    Goto, Y.9
  • 12
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • Alexandrescu A.T. Amyloid accomplices and enforcers. Protein. Sci. 14 (2005) 1-12
    • (2005) Protein. Sci. , vol.14 , pp. 1-12
    • Alexandrescu, A.T.1
  • 13
    • 0038575444 scopus 로고    scopus 로고
    • Functional structure and composition of the extracellular matrix
    • Bosman F.T., and Stamenkovic I. Functional structure and composition of the extracellular matrix. J. Pathol. 200 (2003) 423-438
    • (2003) J. Pathol. , vol.200 , pp. 423-438
    • Bosman, F.T.1    Stamenkovic, I.2
  • 14
    • 0022004144 scopus 로고
    • Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study.
    • Snow A.D., and Kisilevsky R. Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study. Lab. Invest. 53 (1985) 37-44
    • (1985) Lab. Invest. , vol.53 , pp. 37-44
    • Snow, A.D.1    Kisilevsky, R.2
  • 15
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro
    • Cohlberg J.A., Li J., Uversky V.N., and Fink A.L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry 41 (2002) 1502-1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 16
    • 2442675503 scopus 로고    scopus 로고
    • Inhibition of amyloid A amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2-deoxy-alpha- and beta-d-glucose: implications for the treatment of various amyloidoses
    • Kisilevsky R., Szarek W.A., Ancsin J.B., Elimova E., Marone S., Bhat S., and Berkin A. Inhibition of amyloid A amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2-deoxy-alpha- and beta-d-glucose: implications for the treatment of various amyloidoses. Am. J. Pathol. 164 (2004) 2127-2137
    • (2004) Am. J. Pathol. , vol.164 , pp. 2127-2137
    • Kisilevsky, R.1    Szarek, W.A.2    Ancsin, J.B.3    Elimova, E.4    Marone, S.5    Bhat, S.6    Berkin, A.7
  • 17
    • 0042703654 scopus 로고    scopus 로고
    • Amyloidogenesis: historical and modern observations point to heparan sulfate protoglycans as a major culprit
    • Ancsin J.B. Amyloidogenesis: historical and modern observations point to heparan sulfate protoglycans as a major culprit. Amyloid 10 (2003) 67-79
    • (2003) Amyloid , vol.10 , pp. 67-79
    • Ancsin, J.B.1
  • 18
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: salt and solvent effects on interfacial phenomena
    • Cacace M.G., Landau E.M., and Ramsden J.J. The Hofmeister series: salt and solvent effects on interfacial phenomena. Q Rev Biophys 30 (1997) 241-277
    • (1997) Q Rev Biophys , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 19
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophys. J. 71 (1996) 2056-2063
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 20
    • 43049107618 scopus 로고
    • The surface tension of protein solutions. Part III
    • Johnston J.H. The surface tension of protein solutions. Part III. Biochem. J. 21 (1927) 1314-1328
    • (1927) Biochem. J. , vol.21 , pp. 1314-1328
    • Johnston, J.H.1
  • 21
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamic stability of human prion protein
    • Apetri A.C., and Surewicz W.K. Atypical effect of salts on the thermodynamic stability of human prion protein. J. Biol. Chem. 278 (2003) 22187-22192
    • (2003) J. Biol. Chem. , vol.278 , pp. 22187-22192
    • Apetri, A.C.1    Surewicz, W.K.2
  • 22
    • 27744488083 scopus 로고    scopus 로고
    • Evaluation of Hofmeister effects on the kinetic stability of proteins
    • Broering J.M., and Bommarius A.S. Evaluation of Hofmeister effects on the kinetic stability of proteins. J. Phys. Chem. 109 (2005) 20612-20619
    • (2005) J. Phys. Chem. , vol.109 , pp. 20612-20619
    • Broering, J.M.1    Bommarius, A.S.2
  • 23
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation
    • Munishkina L.A., Henriques J., Uversky V.N., and Fink A.L. Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 43 (2004) 3289-3300
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Uversky, V.N.3    Fink, A.L.4
  • 24
    • 35148899284 scopus 로고    scopus 로고
    • Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Ab(1-40) amyloid fibrils
    • Klement K., Wieligmann K., Meinhardt J., Hortschansky P., Richter W., and Fandrich M. Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Ab(1-40) amyloid fibrils. JMB 373 (2007) 1321-1333
    • (2007) JMB , vol.373 , pp. 1321-1333
    • Klement, K.1    Wieligmann, K.2    Meinhardt, J.3    Hortschansky, P.4    Richter, W.5    Fandrich, M.6
  • 25
    • 0038264427 scopus 로고    scopus 로고
    • Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL)
    • Abraham R.S., Geyer S.M., Price-Troska T.L., Allmer C., Kyle R.A., Gertz M.A., and Fonseca R. Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 101 (2003) 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    Gertz, M.A.6    Fonseca, R.7
  • 26
  • 27
    • 0001688829 scopus 로고
    • Excited-state properties of the indole chromophore: electronic transition moment directions from linear dichroism measurements: effect of methyl and methoxy substitutents.
    • Albinsson B., and Nordeen B. Excited-state properties of the indole chromophore: electronic transition moment directions from linear dichroism measurements: effect of methyl and methoxy substitutents. J. Phys. Chem 96 (1992) 6204-6212
    • (1992) J. Phys. Chem , vol.96 , pp. 6204-6212
    • Albinsson, B.1    Nordeen, B.2
  • 28
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado M., Merkel J.S., and Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 8979-8984
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 29
    • 0031895939 scopus 로고    scopus 로고
    • Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation
    • Castillo G.M., Cummings J.A., Yang W., Judge M.E., Sheardown M.J., Rimvall K., Bondo Hansen J., and Snow A.D. Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. Diabetes 47 (1998) 612-620
    • (1998) Diabetes , vol.47 , pp. 612-620
    • Castillo, G.M.1    Cummings, J.A.2    Yang, W.3    Judge, M.E.4    Sheardown, M.J.5    Rimvall, K.6    Bondo Hansen, J.7    Snow, A.D.8
  • 30
    • 33846080680 scopus 로고
    • Surface potentials of aqueous electrolyte solutions
    • Jarvis N.L., and Scheiman M.A. Surface potentials of aqueous electrolyte solutions. J. Phys. Chem. 72 (1968) 74-78
    • (1968) J. Phys. Chem. , vol.72 , pp. 74-78
    • Jarvis, N.L.1    Scheiman, M.A.2
  • 31
    • 0015520434 scopus 로고
    • The effects of salts on the free energies of nonpolar groups in model peptides
    • Nandi P.K., and Robinson D.R. The effects of salts on the free energies of nonpolar groups in model peptides. J. Am. Chem. Soc. 94 (1972) 1308-1315
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 1308-1315
    • Nandi, P.K.1    Robinson, D.R.2


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