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Volumn 13, Issue 4, 2000, Pages 198-212

Binding of nascent collagen by amyloidogenic light chains and amyloid fibrillogenesis in monolayers of human fibrocytes

Author keywords

AL amyloidosis; Amyloid; Amyloidogenic light (L) chains; Bence Jones proteins; Collagen; Multiple myeloma

Indexed keywords

AMMONIUM SULFATE; BENCE JONES PROTEIN; BINDING KINETICS; COLLAGEN; CULTURE MEDIUM; ENZYME SUBSTRATE; EXTRACELLULAR MATRIX; FIBRIL; FIBROBLAST; HUMAN CELL CULTURE; HUMAN; LIGAND; MONOLAYER; MYELOMA CELL; URINE;

EID: 0033865983     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/1099-1352(200007/08)13:4<198::AID-JMR499>3.0.CO;2-D     Document Type: Article
Times cited : (29)

References (65)
  • 1
    • 0021352748 scopus 로고
    • Studies of heart. XXIV. Inhibitory effect of antiarrhythmic peptide (AAP) on experimental thromboses
    • Aonuma S, Kohama Y, Makino T, Hattori K, Kawahara Y. 1984. Studies of heart. XXIV. Inhibitory effect of antiarrhythmic peptide (AAP) on experimental thromboses. Chem. Pharm. Bull. (Tokyo) 32: 219-227.
    • (1984) Chem. Pharm. Bull. (Tokyo) , vol.32 , pp. 219-227
    • Aonuma, S.1    Kohama, Y.2    Makino, T.3    Hattori, K.4    Kawahara, Y.5
  • 2
    • 0030590876 scopus 로고    scopus 로고
    • Structural and functional characterization of three human immunoglobulin kappa light chains with different pathological implications
    • Bellotti V, Stoppini M, Mangione PP, Fornasieri A, Min L, Merlini G, Ferri G. 1996. Structural and functional characterization of three human immunoglobulin kappa light chains with different pathological implications. Biochim. Biophys. Acta 1317: 161-167.
    • (1996) Biochim. Biophys. Acta , vol.1317 , pp. 161-167
    • Bellotti, V.1    Stoppini, M.2    Mangione, P.P.3    Fornasieri, A.4    Min, L.5    Merlini, G.6    Ferri, G.7
  • 3
    • 0001444863 scopus 로고
    • A refinement of crystal structure of azobenzene
    • Brown C. 1966. A refinement of crystal structure of azobenzene. Acta. Crystallogr. 21: 146-152.
    • (1966) Acta. Crystallogr. , vol.21 , pp. 146-152
    • Brown, C.1
  • 5
    • 0025259913 scopus 로고
    • Monoclonal immunoglobulin deposition disease: Light chain and light and heavy chains deposition diseases and their relation to light chain amyloidosis; clinical features, immunopathology, and molecular analysis
    • Buxbaum JN, Chuba JV, Hellman GC, Solomon A, Gallo GR. 1990. Monoclonal immunoglobulin deposition disease: light chain and light and heavy chains deposition diseases and their relation to light chain amyloidosis; clinical features, immunopathology, and molecular analysis. Ann. Intern. Med. 112: 455-464.
    • (1990) Ann. Intern. Med. , vol.112 , pp. 455-464
    • Buxbaum, J.N.1    Chuba, J.V.2    Hellman, G.C.3    Solomon, A.4    Gallo, G.R.5
  • 6
    • 0019400140 scopus 로고
    • Renal handling and pathophysiology of Bence-Jones proteins
    • Clyne DH, Pollak VE. 1981. Renal handling and pathophysiology of Bence-Jones proteins. Contrib. Nephrol. 24: 78-87.
    • (1981) Contrib. Nephrol. , vol.24 , pp. 78-87
    • Clyne, D.H.1    Pollak, V.E.2
  • 7
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W, Kelly JW. 1992. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31: 8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 8
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly ML. 1983a. Analytical molecular surface calculation. J. Appl. Crystallogr. 16: 548-558.
    • (1983) J. Appl. Crystallogr. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 9
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML. 1983b. Solvent-accessible surfaces of proteins and nucleic acids. Science 221: 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 11
    • 0022487844 scopus 로고
    • Three-dimensional analyses of the binding of synthetic chemotactic and opioid peptides in the Mcg light chain dimer
    • Porter, R. & Whelan, J., eds., Wiley, Chichester
    • Edmundson AB, Ely KR. 1986. Three-dimensional analyses of the binding of synthetic chemotactic and opioid peptides in the Mcg light chain dimer. In Synthetic Peptides as Antigens (Ciba Foundation Symposium 119) (Porter, R. & Whelan, J., eds.), pp. 107-129. Wiley, Chichester.
    • (1986) Synthetic Peptides As Antigens (Ciba Foundation Symposium 119) , pp. 107-129
    • Edmundson, A.B.1    Ely, K.R.2
  • 12
    • 0031862463 scopus 로고    scopus 로고
    • Treatment of osteoarthritis with aspartame
    • Edmundson AB, Manion CV. 1998. Treatment of osteoarthritis with aspartame. Clin. Pharmac. Ther 63: 580-593.
    • (1998) Clin. Pharmac. Ther , vol.63 , pp. 580-593
    • Edmundson, A.B.1    Manion, C.V.2
  • 13
    • 0001447689 scopus 로고
    • Structure and binding properties of a λ-type Bence-Jones dimer
    • Brent, L. & Holborow, J., eds., North-Holland, Amsterdam
    • Edmundson AB, Ely KR, Girling RL, Abola EE, Schiffer M, Westholm FA. 1974a. Structure and binding properties of a λ-type Bence-Jones dimer. In Progress in Immunology II (Brent, L. & Holborow, J., eds.), Vol. 1, pp. 103-113. North-Holland, Amsterdam.
    • (1974) Progress in Immunology II , vol.1 , pp. 103-113
    • Edmundson, A.B.1    Ely, K.R.2    Girling, R.L.3    Abola, E.E.4    Schiffer, M.5    Westholm, F.A.6
  • 15
    • 0016721052 scopus 로고
    • Rotational allomerism and divergent evolution of domains in immunoglobulin light chains
    • Edmundson AB, Ely KR, Abola EE, Schiffer M, Panagiotopoulos N. 1975. Rotational allomerism and divergent evolution of domains in immunoglobulin light chains. Biochemistry 14: 3953-3961.
    • (1975) Biochemistry , vol.14 , pp. 3953-3961
    • Edmundson, A.B.1    Ely, K.R.2    Abola, E.E.3    Schiffer, M.4    Panagiotopoulos, N.5
  • 16
    • 0021258474 scopus 로고
    • A search for site-filling ligands in the Mcg Bence-Jones dimer: Crystal binding studies of fluorescent compounds
    • Edmundson AB, Ely KR, Herron JN. 1984 A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compounds. Mol. Immunol. 21: 561-576.
    • (1984) Mol. Immunol. , vol.21 , pp. 561-576
    • Edmundson, A.B.1    Ely, K.R.2    Herron, J.N.3
  • 17
    • 0023226209 scopus 로고
    • The binding of opioid peptides to the Mcg light chain dimer: Flexible keys and adjustable locks
    • Edmundson AB, Ely KR, Herron JN, Cheson BD. 1987. The binding of opioid peptides to the Mcg light chain dimer: flexible keys and adjustable locks. Mol. Immunol. 24: 915-935.
    • (1987) Mol. Immunol. , vol.24 , pp. 915-935
    • Edmundson, A.B.1    Ely, K.R.2    Herron, J.N.3    Cheson, B.D.4
  • 18
    • 0024566188 scopus 로고
    • Cocrystallization of an immunoglobulin light chain dimer with bis(dinitrophenyl) lysine: Tandem binding of two ligands, one with and one without accompanying conformational changes in the protein
    • Edmundson AB, Ely KR, He XM, Herron JN. 1989a. Cocrystallization of an immunoglobulin light chain dimer with bis(dinitrophenyl) lysine: tandem binding of two ligands, one with and one without accompanying conformational changes in the protein. Mol. Immunol. 26: 207-220.
    • (1989) Mol. Immunol. , vol.26 , pp. 207-220
    • Edmundson, A.B.1    Ely, K.R.2    He, X.M.3    Herron, J.N.4
  • 21
    • 0002098803 scopus 로고
    • Three-dimensional aspects of IgG structure and function
    • Zanetti, M. & Capra, J. D., eds., Harvard Academic, Luxembourg
    • Edmundson AB, Guddat LW, Rosauer RA, Andersen KN, Shan L, Fan Z-C. 1995. Three-dimensional aspects of IgG structure and function. In The Antibodies (Zanetti, M. & Capra, J. D., eds.), Vol. 1, pp. 41-100. Harvard Academic, Luxembourg.
    • (1995) The Antibodies , vol.1 , pp. 41-100
    • Edmundson, A.B.1    Guddat, L.W.2    Rosauer, R.A.3    Andersen, K.N.4    Shan, L.5    Fan, Z.-C.6
  • 23
    • 0013974518 scopus 로고
    • On the origin of amyloid; study of an amyloid tumor in multiple myeloma
    • Gafni J, Merker H-J, Shibolet S, Sohar E, Heller H. 1966. On the origin of amyloid; study of an amyloid tumor in multiple myeloma. Ann. Intern. Med. 65: 1031-1044.
    • (1966) Ann. Intern. Med. , vol.65 , pp. 1031-1044
    • Gafni, J.1    Merker, H.-J.2    Shibolet, S.3    Sohar, E.4    Heller, H.5
  • 24
    • 0017168698 scopus 로고
    • Simultaneous synthesis of types I and III collagen by fibroblasts in culture
    • Gay S, Martin GR, Muller PK, Timpl R, Kuhn K. 1976. Simultaneous synthesis of types I and III collagen by fibroblasts in culture. Proc. Natl Acad. Sci. USA 73: 4037-4040.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 4037-4040
    • Gay, S.1    Martin, G.R.2    Muller, P.K.3    Timpl, R.4    Kuhn, K.5
  • 25
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis; the β-fibrilloses
    • Glenner GG. 1980. Amyloid deposits and amyloidosis; the β-fibrilloses. N. Engl. J. Med. 302: 1283-1292.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 27
    • 0015219685 scopus 로고
    • Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analyses
    • Glenner GG, Terry W, Harada M, Isersky C, Page D. 1971b. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science 172: 1150-1151.
    • (1971) Science , vol.172 , pp. 1150-1151
    • Glenner, G.G.1    Terry, W.2    Harada, M.3    Isersky, C.4    Page, D.5
  • 28
    • 0343373666 scopus 로고
    • Lichen amyloidosis; histochemical and electron microscopic studies
    • Hashimoto K, Gross BG, Lever WF. 1965. Lichen amyloidosis; histochemical and electron microscopic studies. J. Invest. Derm. 45: 204-219.
    • (1965) J. Invest. Derm. , vol.45 , pp. 204-219
    • Hashimoto, K.1    Gross, B.G.2    Lever, W.F.3
  • 29
    • 0029966282 scopus 로고    scopus 로고
    • Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis
    • Helms LR, Wetzel R. 1996. Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. J. Mol. Biol. 257: 77-86.
    • (1996) J. Mol. Biol. , vol.257 , pp. 77-86
    • Helms, L.R.1    Wetzel, R.2
  • 30
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson WA. 1985. Stereochemically restrained refinement of macromolecular structures. Meth. Enzymol. 115: 252-270.
    • (1985) Meth. Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 31
    • 0020966417 scopus 로고
    • Renal lesions in multiple myeloma: Their relationship to associated protein abnormalities
    • Hill GS, Morel-Maroger L, Mery JP, Brouet JC, Mignon F. 1983. Renal lesions in multiple myeloma: their relationship to associated protein abnormalities Am. J. Kidney Dis. 2: 423-438.
    • (1983) Am. J. Kidney Dis. , vol.2 , pp. 423-438
    • Hill, G.S.1    Morel-Maroger, L.2    Mery, J.P.3    Brouet, J.C.4    Mignon, F.5
  • 32
    • 0027142560 scopus 로고
    • Bence-Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation
    • Huang Z-Q, Kirk KA, Connelly KG, Sanders PW. 1993. Bence-Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation. J. Clin. Invest. 92: 2975-2383.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2975-12383
    • Huang, Z.-Q.1    Kirk, K.A.2    Connelly, K.G.3    Sanders, P.W.4
  • 33
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle MR, Helms LR, Li L, Chan W, Wetzel R. 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl Acad. Sci. USA 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
  • 34
    • 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
  • 35
    • 0020964586 scopus 로고
    • Amyloidosis: A familiar problem in the light of current pathogenetic developments
    • Kisilevsky R. 1983. Amyloidosis: a familiar problem in the light of current pathogenetic developments. Lab. Invest. 49: 381-390.
    • (1983) Lab. Invest. , vol.49 , pp. 381-390
    • Kisilevsky, R.1
  • 37
    • 0015009309 scopus 로고
    • The nature of the collagen synthesized by cultured human fibroblasts
    • Layman DL, McGoodwin EB, Martin GR. 1971. The nature of the collagen synthesized by cultured human fibroblasts. Proc. Natl Acad. Sci. USA 68: 454-458.
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 454-458
    • Layman, D.L.1    McGoodwin, E.B.2    Martin, G.R.3
  • 38
    • 0015644626 scopus 로고
    • Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence-Jones proteins by proteolysis
    • Linke RP, Zucker-Franklin D, Franklin EC. 1973. Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence-Jones proteins by proteolysis. J. Immunol. 111: 10-23.
    • (1973) J. Immunol. , vol.111 , pp. 10-23
    • Linke, R.P.1    Zucker-Franklin, D.2    Franklin, E.C.3
  • 39
    • 0000680118 scopus 로고
    • Refinement of crystal-structure of cisazobenzene
    • Mostad A, Romming C. 1971. Refinement of crystal-structure of cisazobenzene. Acta Chem. Scand. 25: 3561.
    • (1971) Acta Chem. Scand. , vol.25 , pp. 3561
    • Mostad, A.1    Romming, C.2
  • 41
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot D, Loll PJ, Garavito RM. 1994. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367: 243-249.
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 45
    • 0002908272 scopus 로고
    • TURBO-FRODO molecular graphics program
    • Graphics, S., ed., Silicon Graphics, Mountain View, CA
    • Roussel A, Cambillau C. 1989. TURBO-FRODO molecular graphics program. In Silicon Graphics Geometry Partner Directory (Fall 1989) (Graphics, S., ed,), pp. 77-78. Silicon Graphics, Mountain View, CA.
    • (1989) Silicon Graphics Geometry Partner Directory (Fall 1989) , pp. 77-78
    • Roussel, A.1    Cambillau, C.2
  • 47
    • 0015933642 scopus 로고
    • Synthesis of (pro-hyp-gly)n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxypyroline
    • Sakakibara S, Inouye K, Shudo K, Kishida Y, Kobayashi Y, Prockop D. 1973. Synthesis of (pro-hyp-gly)n of defined molecular weights. Evidence for the stabilization of collagen triple helix by hydroxypyroline. Biochim. Biophys. Acta 303: 198-202.
    • (1973) Biochim. Biophys. Acta , vol.303 , pp. 198-202
    • Sakakibara, S.1    Inouye, K.2    Shudo, K.3    Kishida, Y.4    Kobayashi, Y.5    Prockop, D.6
  • 48
    • 0015549030 scopus 로고
    • Fibrillar assemblage of variable segments of immunoglobulin light chains: An electron microscopic study
    • Shirahama T, Benson MD, Cohen AS, Tanaka A. 1973. Fibrillar assemblage of variable segments of immunoglobulin light chains: an electron microscopic study. J. Immunol. 110: 21-30.
    • (1973) J. Immunol. , vol.110 , pp. 21-30
    • Shirahama, T.1    Benson, M.D.2    Cohen, A.S.3    Tanaka, A.4
  • 49
    • 0020059082 scopus 로고
    • Bence-Jones proteins: Malignant or benign?
    • Solomon A. 1982. Bence-Jones proteins: malignant or benign? N. Engl. J. Med. 306: 605-607.
    • (1982) N. Engl. J. Med. , vol.306 , pp. 605-607
    • Solomon, A.1
  • 50
    • 0022272516 scopus 로고
    • Light chains of human immunoglobulins
    • Solomon A. 1985. Light chains of human immunoglobulins. Meth. Enzymol. 116: 101-121.
    • (1985) Meth. Enzymol. , vol.116 , pp. 101-121
    • Solomon, A.1
  • 51
    • 0014690568 scopus 로고
    • Bence-Jones proteins and light chains of immunoglobulins. I. Formation and characterization of amino-terminal (variant) and carboxyl-terminal (constant) halves
    • Solomon A, McLaughlin CL. 1969. Bence-Jones proteins and light chains of immunoglobulins. I. Formation and characterization of amino-terminal (variant) and carboxyl-terminal (constant) halves. J. Biol. Chem. 244: 3393-3404.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3393-3404
    • Solomon, A.1    McLaughlin, C.L.2
  • 52
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)
    • Solomon A, Weiss DT. 1995. Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis). Amyloid: Int. J. Exp. Clin. Invest. 2: 269-279.
    • (1995) Amyloid: Int. J. Exp. Clin. Invest. , vol.2 , pp. 269-279
    • Solomon, A.1    Weiss, D.T.2
  • 54
    • 0026432631 scopus 로고
    • Nephrotoxic potential of Bence-Jones proteins
    • Solomon A, Weiss DT, Kattine AA. 1991. Nephrotoxic potential of Bence-Jones proteins. N. Engl. J. Med. 324: 1845-1851.
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1845-1851
    • Solomon, A.1    Weiss, D.T.2    Kattine, A.A.3
  • 55
    • 0026534711 scopus 로고
    • Induction in mice of human light-chain-associated amyloidosis
    • Solomon A, Weiss DT, Pepys MB. 1992a. Induction in mice of human light-chain-associated amyloidosis. Am. J. Pathol. 140: 629-637.
    • (1992) Am. J. Pathol. , vol.140 , pp. 629-637
    • Solomon, A.1    Weiss, D.T.2    Pepys, M.B.3
  • 60
    • 0025117402 scopus 로고
    • Amyloidosis: A final common pathway for protein deposition in tissues
    • Stone MJ. 1990. Amyloidosis: a final common pathway for protein deposition in tissues. Blood 75: 531-545.
    • (1990) Blood , vol.75 , pp. 531-545
    • Stone, M.J.1
  • 62
    • 0015276441 scopus 로고
    • Polymer formation during the degradation of human light chain and Bence-Jones proteins by an extract of the lysosomal fraction of normal human kidney
    • Tan M, Epstein W. 1972. Polymer formation during the degradation of human light chain and Bence-Jones proteins by an extract of the lysosomal fraction of normal human kidney. Immunochemistry 9: 9-16.
    • (1972) Immunochemistry , vol.9 , pp. 9-16
    • Tan, M.1    Epstein, W.2
  • 63
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall J, Murphy CL, Solomon A. 1999a. In vitro immunoglobulin light chain fibrillogenesis. Meth. Enzymol. 309: 204-217.
    • (1999) Meth. Enzymol. , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 64
    • 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 FJ, Solomon A. 1999b. Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 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
  • 65
    • 75449133148 scopus 로고
    • Binding studies of a series of peptides for use in protein chemistry: A model
    • Wünsch EK, Heidrich JG. 1963. Binding studies of a series of peptides for use in protein chemistry: a model. Hoppe-Seyler's Z. Physiol. Chem. 333: 149-162.
    • (1963) Hoppe-Seyler's Z. Physiol. Chem. , vol.333 , pp. 149-162
    • Wünsch, E.K.1    Heidrich, J.G.2


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