메뉴 건너뛰기




Volumn 18, Issue 6, 2005, Pages 659-675

The ultrastructural basis of renal pathology in monoclonal gammopathies

Author keywords

AL amyloidosis; Cryoglobulinemia; Fanconi syndrome; Immunotactoid glomerulopathy; Light chain; Monoclonal gammopathy; Monoclonal immunoglobulin deposition disease

Indexed keywords

ANTINEOPLASTIC AGENT; APOLIPOPROTEIN A1; BORTEZOMIB; FIBRINOGEN; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN; LENALIDOMIDE; PROCOLLAGEN C PROTEINASE; TAMM HORSFALL GLYCOPROTEIN; THALIDOMIDE; TRANSFORMING GROWTH FACTOR BETA;

EID: 30644467493     PISSN: 11218428     EISSN: 17246059     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (45)

References (92)
  • 1
    • 0033927121 scopus 로고    scopus 로고
    • Renal manifestations of plasma cell dyscrasias. An appraisal from the patients' bedside to the research laboratory
    • Herrera GA. Renal manifestations of plasma cell dyscrasias. An appraisal from the patients' bedside to the research laboratory. Ann Diagn Pathol 2000; 4: 174-200.
    • (2000) Ann Diagn Pathol , vol.4 , pp. 174-200
    • Herrera, G.A.1
  • 2
    • 0034320619 scopus 로고    scopus 로고
    • Plasma cell dyscrasia-related glomerulopathies and Fanconi's syndrome: A molecular approach
    • Ronco P, Aucouturier P, Mougenot B. Plasma cell dyscrasia-related glomerulopathies and Fanconi's syndrome: a molecular approach. J Nephrol 2000; 13 (suppl 3): S34-44.
    • (2000) J Nephrol , vol.13 , Issue.SUPPL. 3
    • Ronco, P.1    Aucouturier, P.2    Mougenot, B.3
  • 6
    • 0035157924 scopus 로고    scopus 로고
    • Clathrin hub expression dissociates the actin-binding protein Hip1R from coated pits and disrupts their alignment with the actin cytoskeleton
    • Bennett EM, Chen CY, Engqvist-Goldstein AE, Drubin DG, Brodsky FM. Clathrin hub expression dissociates the actin-binding protein Hip1R from coated pits and disrupts their alignment with the actin cytoskeleton. Traffic 2001; 2: 851-8.
    • (2001) Traffic , vol.2 , pp. 851-858
    • Bennett, E.M.1    Chen, C.Y.2    Engqvist-Goldstein, A.E.3    Drubin, D.G.4    Brodsky, F.M.5
  • 7
    • 0034916160 scopus 로고    scopus 로고
    • Light chain deposition disease. A model of glomerulosclerosis defined at the molecular level
    • Ronco PM, Alyanakian MA, Mougenot B, Aucouturier P. Light chain deposition disease. A model of glomerulosclerosis defined at the molecular level. J Am Soc Nephrol 2001; 12: 1558-65.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 1558-1565
    • Ronco, P.M.1    Alyanakian, M.A.2    Mougenot, B.3    Aucouturier, P.4
  • 9
    • 0030139339 scopus 로고    scopus 로고
    • Molecular anatomy and the pathological expression of antibody light chains
    • Schiffer M. Molecular anatomy and the pathological expression of antibody light chains. Am J Pathol 1996; 148: 1339-44.
    • (1996) Am J Pathol , vol.148 , pp. 1339-1344
    • Schiffer, M.1
  • 10
    • 0026534711 scopus 로고
    • Induction in mice of human light-chain-associated amyloidosis
    • Solomon A, Weiss DT, Pepys MB. Induction in mice of human light-chain-associated amyloidosis. Am J Pathol 1992; 140: 629-37.
    • (1992) Am J Pathol , vol.140 , pp. 629-637
    • Solomon, A.1    Weiss, D.T.2    Pepys, M.B.3
  • 11
    • 0026432631 scopus 로고
    • Nephrotoxic potential of Bence-Jones proteins
    • Solomon A, Weiss DT, Kattine AA. Nephrotoxic potential of Bence-Jones proteins. N Engl J Med 1991; 324: 1845-51.
    • (1991) N Engl J Med , vol.324 , pp. 1845-1851
    • Solomon, A.1    Weiss, D.T.2    Kattine, A.A.3
  • 12
    • 0028208249 scopus 로고
    • Pathogenic potential of human monoclonal immunoglobulin light chains: Relationship of in vitro aggregation to in vivo deposition
    • Myatt EA, Westholm FA, Weiss DT, Solomon A, Schiffer M, Stevens FJ. Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo deposition. Proc Natl Acad Sci U S A 1994; 91: 3034-8.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3034-3038
    • Myatt, E.A.1    Westholm, F.A.2    Weiss, D.T.3    Solomon, A.4    Schiffer, M.5    Stevens, F.J.6
  • 13
    • 0028168934 scopus 로고
    • Overpresentation of the V kappa IV subgroup in light chain deposition disease
    • Denoroy L, Déret S, Aucouturier P. Overpresentation of the V kappa IV subgroup in light chain deposition disease. Immumol Lett 1994; 42: 63-6.
    • (1994) Immumol Lett , vol.42 , pp. 63-66
    • Denoroy, L.1    Déret, S.2    Aucouturier, P.3
  • 14
    • 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
    • Comenzo RL, Zhang Y, Martinez C, Osman Y, Herrera GA. The tropism of organ involvement in primary systemic amyloidosis: contributions of Ig V(L) germ line gene use and clonal plasma cell burden. Blood 2001; 98: 714-20.
    • (2001) Blood , vol.98 , pp. 714-720
    • Comenzo, R.L.1    Zhang, Y.2    Martinez, C.3    Osman, Y.4    Herrera, G.A.5
  • 16
    • 0032552958 scopus 로고    scopus 로고
    • Fragments of the constant region of immunoglobulin light chains are constituents of AL-amyloid proteins
    • Olsen KE, Sletten K, Westermark P. Fragments of the constant region of immunoglobulin light chains are constituents of AL-amyloid proteins. Biochem Biophys Res Commun 1998; 251: 642-7.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 642-647
    • Olsen, K.E.1    Sletten, K.2    Westermark, P.3
  • 18
    • 0030512066 scopus 로고    scopus 로고
    • Current concepts on the pathogenesis of systemic amyloidosis
    • Bellotti V, Merlini G. Current concepts on the pathogenesis of systemic amyloidosis. Nephrol Dial Transplant 1996; 11 (suppl 9): S53-62.
    • (1996) Nephrol Dial Transplant , vol.11 , Issue.SUPPL. 9
    • Bellotti, V.1    Merlini, G.2
  • 19
    • 0028818272 scopus 로고
    • Tertiary structure of an amyloid immunoglobulin light chain protein: A proposed model for amyloid fibril formation
    • Schorman N, Murrel JR, Liepnicks JJ, Benson MD. Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation. Proc Natl Acad Sci U S A 1995; 92: 9490-4.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9490-9494
    • Schorman, N.1    Murrel, J.R.2    Liepnicks, J.J.3    Benson, M.D.4
  • 20
    • 0029795249 scopus 로고    scopus 로고
    • Toward understanding the molecular pathogenesis of monoclonal immunoglobulin light-chain deposition
    • Bellotti V, Merlini G. Toward understanding the molecular pathogenesis of monoclonal immunoglobulin light-chain deposition. Nephrol Dial Transplant 1996; 11: 1708-11.
    • (1996) Nephrol Dial Transplant , vol.11 , pp. 1708-1711
    • Bellotti, V.1    Merlini, G.2
  • 21
    • 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 U S A 1994; 91: 5446-50.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 22
    • 0030590876 scopus 로고    scopus 로고
    • Structural and functional characterization of three human immunoglobulin kappa light chains with different pathologic implications
    • Bellotti V, Stoppini M, Mangione PP, Fornasieri A, Min L, Merlini G, Ferri G. Structural and functional characterization of three human immunoglobulin kappa light chains with different pathologic implications. Biochim Biophys Acta 1996; 1317: 161-7.
    • (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
  • 23
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrel RW, Lomas DA. Conformational disease. Lancet 1997; 350: 134-8.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrel, R.W.1    Lomas, D.A.2
  • 24
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a protein folding transition state
    • Vendruscolo M, Paci E, Dobson CM, Karplus M. Three key residues form a critical contact network in a protein folding transition state. Nature 2001; 409: 641-5.
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 25
    • 0030819311 scopus 로고    scopus 로고
    • Nodular pulmonary immunoglobulin light chain deposits with coexistent amyloid and non amyloid features in an HIV-infected patient
    • Stokes MB, Jagirdar J, Burchstin O, Kornacki S, Kumar A, Gallo G. Nodular pulmonary immunoglobulin light chain deposits with coexistent amyloid and non amyloid features in an HIV-infected patient. Mod Pathol 1997; 10: 1059-65.
    • (1997) Mod Pathol , vol.10 , pp. 1059-1065
    • Stokes, M.B.1    Jagirdar, J.2    Burchstin, O.3    Kornacki, S.4    Kumar, A.5    Gallo, G.6
  • 28
    • 0345136937 scopus 로고    scopus 로고
    • Molecular modeling of immunoglobulin light chains implicates hydrophobic residues in non-amyloid light chain deposition disease
    • Déret S, Chomilier J, Huang DB, Preud'Homme JL, Stevens FJ, Aucouturier P. Molecular modeling of immunoglobulin light chains implicates hydrophobic residues in non-amyloid light chain deposition disease. Protein Eng 1997; 10: 1191-7.
    • (1997) Protein Eng , vol.10 , pp. 1191-1197
    • Déret, S.1    Chomilier, J.2    Huang, D.B.3    Preud'Homme, J.L.4    Stevens, F.J.5    Aucouturier, P.6
  • 29
    • 0035011613 scopus 로고    scopus 로고
    • Monoclonal light chain-mesangial cell interactions: Early signaling events and subsequent pathologic effects
    • Russel WJ, Cardelli J, Harris E, Baier RJ, Herrera GA. Monoclonal light chain-mesangial cell interactions: early signaling events and subsequent pathologic effects. Lab Invest 2001; 81: 689-703.
    • (2001) Lab Invest , vol.81 , pp. 689-703
    • Russel, W.J.1    Cardelli, J.2    Harris, E.3    Baier, R.J.4    Herrera, G.A.5
  • 30
    • 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, Russel WI, Gu X, Cardelli J, Jones ML, Herrera GA. Different types of glomerulopathic light chains interact with mesangial cells using a common receptor but exhibit different intracellular trafficking patterns. Lab Invest 2004; 84: 440-51.
    • (2004) Lab Invest , vol.84 , pp. 440-451
    • Teng, J.1    Russel, W.I.2    Gu, X.3    Cardelli, J.4    Jones, M.L.5    Herrera, G.A.6
  • 32
    • 0029081404 scopus 로고
    • Pathogenesis of glomerulosclerosis in light chain deposition disease. Role for transforming growth factor-β
    • Zhu L, Herrera GA, Murphy-Ullrich JE, Huang Z-Q, Sanders PW. Pathogenesis of glomerulosclerosis in light chain deposition disease. Role for transforming growth factor-β. Am J Pathol 1995; 147: 375-85.
    • (1995) Am J Pathol , vol.147 , pp. 375-385
    • Zhu, L.1    Herrera, G.A.2    Murphy-Ullrich, J.E.3    Huang, Z.-Q.4    Sanders, P.W.5
  • 33
    • 0030803180 scopus 로고    scopus 로고
    • Immunoglobulin light chain alters mesangial cell calcium homeostasis
    • Zhu L, Herrera GA, White CR, Sanders PW. Immunoglobulin light chain alters mesangial cell calcium homeostasis. Am J Physiol 1997; 272: F319-24.
    • (1997) Am J Physiol , vol.272
    • Zhu, L.1    Herrera, G.A.2    White, C.R.3    Sanders, P.W.4
  • 34
    • 0032939741 scopus 로고    scopus 로고
    • Glomerulopathic light chain-mesangial cell interactions modulate in vitro extracellular matrix remodeling and reproduce mesangiopathic findings documented in vivo
    • Herrera GA, Russel WJ, Turbat-Herrera E, Tagouri YM, Sanders PW, Picken MM, Dempsey S. Glomerulopathic light chain-mesangial cell interactions modulate in vitro extracellular matrix remodeling and reproduce mesangiopathic findings documented in vivo. Ultrastruct Pathol 1999; 23: 107-26.
    • (1999) Ultrastruct Pathol , vol.23 , pp. 107-126
    • Herrera, G.A.1    Russel, W.J.2    Turbat-Herrera, E.3    Tagouri, Y.M.4    Sanders, P.W.5    Picken, M.M.6    Dempsey, S.7
  • 35
    • 0030996082 scopus 로고    scopus 로고
    • Integrated expression of glomerular extracellular matrix proteins and β1 integrins in monoclonal light chain-related diseases
    • Turbat-Herrera EA, Isaac J, Sanders PW, Truong LD, Herrera GA. Integrated expression of glomerular extracellular matrix proteins and β1 integrins in monoclonal light chain-related diseases. Mod Pathol 1997; 10: 485-95.
    • (1997) Mod Pathol , vol.10 , pp. 485-495
    • Turbat-Herrera, E.A.1    Isaac, J.2    Sanders, P.W.3    Truong, L.D.4    Herrera, G.A.5
  • 38
    • 0028970456 scopus 로고
    • Primary systemic amyloidosis: Clinical and laboratory features in 474 cases
    • Kyle RA, Gertz MA. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin Hematol 1995; 8: 45-59.
    • (1995) Semin Hematol , vol.8 , pp. 45-59
    • Kyle, R.A.1    Gertz, M.A.2
  • 39
    • 11244259223 scopus 로고    scopus 로고
    • Phenotypic transformation of mesangial cells precedes and is required for AL-amyloidogenesis
    • Bely M, Apathy D, (Eds). Budapest
    • Herrera GA, Russel WJ, Cardelli J. Phenotypic transformation of mesangial cells precedes and is required for AL-amyloidogenesis. In Bely M, Apathy D, (Eds). Proceeding of the IX International Symposium on Amyloidosis. Budapest: 2001; 267-72.
    • (2001) Proceeding of the IX International Symposium on Amyloidosis , pp. 267-272
    • Herrera, G.A.1    Russel, W.J.2    Cardelli, J.3
  • 40
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: Identification of a cellular activation mechanism
    • Lue LF, Walker DG, Brachova L, Beach TG, Rogers J, Schmidt AM, Stern DM, Yan SD. Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: identification of a cellular activation mechanism. Exp Neurol 2001; 171: 29-45.
    • (2001) Exp Neurol , vol.171 , pp. 29-45
    • Lue, L.F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 41
    • 0032235059 scopus 로고    scopus 로고
    • In vitro modulation of AL-Amyloid formation by human mesangial cells exposed to amyloidogenic light chains
    • Isaac J, Kerby JD, Russel 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: 238-46.
    • (1998) Amyloid , vol.5 , pp. 238-246
    • Isaac, J.1    Kerby, J.D.2    Russel, W.J.3    Dempsey, S.C.4    Sanders, P.W.5    Herrera, G.A.6
  • 42
    • 0029621914 scopus 로고
    • Light-heavy chain deposition disease progressing to multiple myeloma
    • Dalomi D, Weber D, Alexanian R. Light-heavy chain deposition disease progressing to multiple myeloma. Am J Hematol 1995; 50: 296-8.
    • (1995) Am J Hematol , vol.50 , pp. 296-298
    • Dalomi, D.1    Weber, D.2    Alexanian, R.3
  • 43
    • 0034986914 scopus 로고    scopus 로고
    • Abnormal immunoglobulin synthesis in monoclonal immunoglobulin light chain and light and heavy chain deposition disease
    • Buxbaum JN. Abnormal immunoglobulin synthesis in monoclonal immunoglobulin light chain and light and heavy chain deposition disease. Amyloid 2001; 8: 84-93.
    • (2001) Amyloid , vol.8 , pp. 84-93
    • Buxbaum, J.N.1
  • 47
    • 0029843823 scopus 로고    scopus 로고
    • Crescentic nodular glomerulosclerosis secondary to truncated immunoglobulin a deposition
    • Cheng I, Ho S, Chan D, Ng W, Chan K. Crescentic nodular glomerulosclerosis secondary to truncated immunoglobulin a deposition. Am J Kidney Dis 1996; 28: 283-8.
    • (1996) Am J Kidney Dis , vol.28 , pp. 283-288
    • Cheng, I.1    Ho, S.2    Chan, D.3    Ng, W.4    Chan, K.5
  • 48
    • 0033958256 scopus 로고    scopus 로고
    • Nodular glomerulosclerosis secondary to μ heavy chain deposits
    • Liapis H, Papadakis I, Nakoponjon L. Nodular glomerulosclerosis secondary to μ heavy chain deposits. Hum Pathol 2000; 31: 122-5.
    • (2000) Hum Pathol , vol.31 , pp. 122-125
    • Liapis, H.1    Papadakis, I.2    Nakoponjon, L.3
  • 49
    • 18244426233 scopus 로고    scopus 로고
    • Immunoglobulin γ3-heavy-chain deposition disease: Report of a case and relationship with hypocomplementemia
    • E2
    • Soma J, Sato K, Sakuma T, Saito H, Sato H, Sato T, Abbas A, Aucouturier P. Immunoglobulin γ3-heavy-chain deposition disease: report of a case and relationship with hypocomplementemia. Am J Kidney Dis 2004; 43: 10-6 E2.
    • (2004) Am J Kidney Dis , vol.43 , pp. 10-16
    • Soma, J.1    Sato, K.2    Sakuma, T.3    Saito, H.4    Sato, H.5    Sato, T.6    Abbas, A.7    Aucouturier, P.8
  • 50
    • 0023096246 scopus 로고
    • Assembly and secretion of heavy chains that do not associate post translationally with immunoglobulin heavy chain-binding protein
    • Hendershot L, Bole D, Kearney JF. Assembly and secretion of heavy chains that do not associate post translationally with immunoglobulin heavy chain-binding protein. J Cell Biol 1987; 104: 761-7.
    • (1987) J Cell Biol , vol.104 , pp. 761-767
    • Hendershot, L.1    Bole, D.2    Kearney, J.F.3
  • 56
    • 0018909663 scopus 로고
    • Adult Fanconi's syndrome with renal tubular acidosis in association with renal amyloidosis: Occurrence in a patient with chronic lymphocytic leukemia
    • Rochman J, Lichting C, Osterweill D, Tatarsky I, Eidelman S. Adult Fanconi's syndrome with renal tubular acidosis in association with renal amyloidosis: occurrence in a patient with chronic lymphocytic leukemia. Arch Intern Med 1980; 140: 1361-3.
    • (1980) Arch Intern Med , vol.140 , pp. 1361-1363
    • Rochman, J.1    Lichting, C.2    Osterweill, D.3    Tatarsky, I.4    Eidelman, S.5
  • 57
    • 0024417173 scopus 로고
    • Adult Fanconi syndrome in primary amyloidosis with lambda light-chain proteinuria
    • Rikitake O, Sakemi T, Yoshikawa Y, Nagano Y, Watanabe T. Adult Fanconi syndrome in primary amyloidosis with lambda light-chain proteinuria. Jpn J Med 1989; 28: 523-6.
    • (1989) Jpn J Med , vol.28 , pp. 523-526
    • Rikitake, O.1    Sakemi, T.2    Yoshikawa, Y.3    Nagano, Y.4    Watanabe, T.5
  • 58
    • 17144454246 scopus 로고    scopus 로고
    • Kappa light chain-associated Fanconi's syndrome: Molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals
    • Deret S, Denoroy L, Lamarine M, Vidal R, Mougenot B, Frangione B, Stevens FJ, Ronco PM, Aucouturier P. Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals. Protein Eng 1999; 12: 363-9.
    • (1999) Protein Eng , vol.12 , pp. 363-369
    • Deret, S.1    Denoroy, L.2    Lamarine, M.3    Vidal, R.4    Mougenot, B.5    Frangione, B.6    Stevens, F.J.7    Ronco, P.M.8    Aucouturier, P.9
  • 59
    • 0033228045 scopus 로고    scopus 로고
    • Inibition of Na-K-AT-Pase activity and gene expression by a myeloma light chain in proximal tubule cells
    • Guan S, El-Dahr S, Dipp S, Batuman V. Inibition of Na-K-AT-Pase activity and gene expression by a myeloma light chain in proximal tubule cells. J Investig Med 1999; 47: 496-501.
    • (1999) J Investig Med , vol.47 , pp. 496-501
    • Guan, S.1    El-Dahr, S.2    Dipp, S.3    Batuman, V.4
  • 60
    • 0028875578 scopus 로고
    • Insight into the biochemical mechanisms of maleic acid-induced Fanconi syndrome
    • Eiam-Ong S, Sphon M, Kurtzman NA, Sabatini S. Insight into the biochemical mechanisms of maleic acid-induced Fanconi syndrome. Kidney Int 1995; 48: 1542-8.
    • (1995) Kidney Int , vol.48 , pp. 1542-1548
    • Eiam-Ong, S.1    Sphon, M.2    Kurtzman, N.A.3    Sabatini, S.4
  • 61
    • 0032512094 scopus 로고    scopus 로고
    • Pathophysiology of progressive nephropathies. Review article
    • Remuzzi G, Bertani T. Pathophysiology of progressive nephropathies. Review article. N Engl J Med 1998; 339: 1448-56.
    • (1998) N Engl J Med , vol.339 , pp. 1448-1456
    • Remuzzi, G.1    Bertani, T.2
  • 63
    • 0024994777 scopus 로고
    • Frequency of light chain deposition nephropathy relative to renal amyloidosis and Bence-Jones cast nephropathy in a necropsy study of patients with myeloma
    • Iványi B. Frequency of light chain deposition nephropathy relative to renal amyloidosis and Bence-Jones cast nephropathy in a necropsy study of patients with myeloma. Arch Pathol Lab Med 1990; 114: 986-7.
    • (1990) Arch Pathol Lab Med , vol.114 , pp. 986-987
    • Iványi, B.1
  • 64
    • 0029564962 scopus 로고
    • Biochemical interaction of Tamm-Horsfall glycoprotein with Ig light chains
    • Huang Z-Q, Sanders PW. Biochemical interaction of Tamm-Horsfall glycoprotein with Ig light chains. Lab Invest 1995; 73: 810-7.
    • (1995) Lab Invest , vol.73 , pp. 810-817
    • Huang, Z.-Q.1    Sanders, P.W.2
  • 65
    • 0025353820 scopus 로고
    • Tamm-Horsfall protein-uromodulin
    • Kumar S, Muchmore A. Tamm-Horsfall protein-uromodulin. Kidney Int 1990; 37: 1395-401.
    • (1990) Kidney Int , vol.37 , pp. 1395-1401
    • Kumar, S.1    Muchmore, A.2
  • 66
    • 0025667675 scopus 로고
    • Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a phosphatidylinositol-linked membrane protein
    • Rindler MJ, Naik SS, Li N, Hoops TC, Peraldi MN. Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a phosphatidylinositol-linked membrane protein. J Biol Chem 1990; 265: 20784-9.
    • (1990) J Biol Chem , vol.265 , pp. 20784-20789
    • Rindler, M.J.1    Naik, S.S.2    Li, N.3    Hoops, T.C.4    Peraldi, M.N.5
  • 67
    • 0035016941 scopus 로고    scopus 로고
    • Mapping the binding domain of immunoglobulin light chains for Tamm-Horsfall protein
    • Ying WZ, Sanders PW. Mapping the binding domain of immunoglobulin light chains for Tamm-Horsfall protein. Am J Pathol 2001; 158: 1859-66.
    • (2001) Am J Pathol , vol.158 , pp. 1859-1866
    • Ying, W.Z.1    Sanders, P.W.2
  • 68
    • 0026607225 scopus 로고
    • Pathobiology of cast nephropathy from human Bence-Jones protein
    • Sanders PW, Booker BB. Pathobiology of cast nephropathy from human Bence-Jones protein. J Clin Invest 1992; 89: 630-9.
    • (1992) J Clin Invest , vol.89 , pp. 630-639
    • Sanders, P.W.1    Booker, B.B.2
  • 69
    • 0027142560 scopus 로고
    • Bence-Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation
    • Huang ZQ, Kirk KA, Connelly KG, Sanders PW. Bence-Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation. J Clin Invest 1993; 92: 2975-83.
    • (1993) J Clin Invest , vol.92 , pp. 2975-2983
    • Huang, Z.Q.1    Kirk, K.A.2    Connelly, K.G.3    Sanders, P.W.4
  • 70
    • 0021764692 scopus 로고
    • Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein
    • Williams J, Marshall RD. Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein. Carbohydr Res 1984; 134: 141-55.
    • (1984) Carbohydr Res , vol.134 , pp. 141-155
    • Williams, J.1    Marshall, R.D.2
  • 71
    • 0029564962 scopus 로고
    • Biochemical interaction between Tam-Horsfall glycoprotein and Ig light chains in the pathogenesis of cast nephropathy
    • Huang ZQ, Sanders P. Biochemical interaction between Tam-Horsfall glycoprotein and Ig light chains in the pathogenesis of cast nephropathy. Lab Invest 1995; 73: 810-7.
    • (1995) Lab Invest , vol.73 , pp. 810-817
    • Huang, Z.Q.1    Sanders, P.2
  • 72
    • 0028208249 scopus 로고
    • Pathogenic potential of human monoclonal immunoglobulin light chains: Relationship of in vitro aggregation to in vivo organ deposition
    • Myatt EA, Westholm FA, Weiss DT, Solomon A, Schiffer M, Stevens FJ. Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition. Proc Natl Acad Sci U S A 1994; 91: 3034-8.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3034-3038
    • Myatt, E.A.1    Westholm, F.A.2    Weiss, D.T.3    Solomon, A.4    Schiffer, M.5    Stevens, F.J.6
  • 73
    • 0030731168 scopus 로고    scopus 로고
    • The development of cast nephropathy in multiple myeloma
    • Iggo N, Winearls CG, Davies DR. The development of cast nephropathy in multiple myeloma. Q J Med 1997; 90: 653-6.
    • (1997) Q J Med , vol.90 , pp. 653-656
    • Iggo, N.1    Winearls, C.G.2    Davies, D.R.3
  • 74
    • 0015527724 scopus 로고
    • The binding of hydrogen and calcium ions by Tamm-Horsfall glycoprotein
    • Cleave AJ, Kent PW, Peacocke AR. The binding of hydrogen and calcium ions by Tamm-Horsfall glycoprotein. Biochim Biophys Acta 1972; 285: 208-23.
    • (1972) Biochim Biophys Acta , vol.285 , pp. 208-223
    • Cleave, A.J.1    Kent, P.W.2    Peacocke, A.R.3
  • 78
    • 0001834593 scopus 로고    scopus 로고
    • Spectrum of glomerular disease in type I cryoglobulinemia
    • Provot F, Bridoux F, Vanhille P. Spectrum of glomerular disease in type I cryoglobulinemia. J Am Soc Nephrol 2000; 11: 95A.
    • (2000) J Am Soc Nephrol , vol.11
    • Provot, F.1    Bridoux, F.2    Vanhille, P.3
  • 79
    • 0026586420 scopus 로고
    • Induction of "wire-loop" lesions by murine monoclonal IgG3 cryoglobulins
    • Lemoine R, Berney T, Shibata T. Induction of "wire-loop" lesions by murine monoclonal IgG3 cryoglobulins. Kidney Int 1992; 41: 65-72.
    • (1992) Kidney Int , vol.41 , pp. 65-72
    • Lemoine, R.1    Berney, T.2    Shibata, T.3
  • 81
    • 0034210619 scopus 로고    scopus 로고
    • Heavy and light chain primary structures control IgG3 nephritogenicity in an experimental model for cryocrystalglobulinemia
    • Rengers J-U, Touchard G, Decourt C, Deret S, Michel H, Cogné M. Heavy and light chain primary structures control IgG3 nephritogenicity in an experimental model for cryocrystalglobulinemia. Blood 2000; 95: 3467-72.
    • (2000) Blood , vol.95 , pp. 3467-3472
    • Rengers, J.-U.1    Touchard, G.2    Decourt, C.3    Deret, S.4    Michel, H.5    Cogné, M.6
  • 83
    • 0030730723 scopus 로고    scopus 로고
    • Glycosylation is influential in murine IgG3 self-association
    • Panka DJ. Glycosylation is influential in murine IgG3 self-association. Mol Immunol 1997; 34: 593-8.
    • (1997) Mol Immunol , vol.34 , pp. 593-598
    • Panka, D.J.1
  • 85
    • 0037379132 scopus 로고    scopus 로고
    • Fibrillary and immunotactoid glomerulonephritis: Distinct entities with different clinical and pathologic features
    • Rosenstock JL, Markowitz GS, Valeri AM, Sacchi G, Appel GB, D'Agati VD. Fibrillary and immunotactoid glomerulonephritis: distinct entities with different clinical and pathologic features. Kidney Int 2003; 63: 1450-61.
    • (2003) Kidney Int , vol.63 , pp. 1450-1461
    • Rosenstock, J.L.1    Markowitz, G.S.2    Valeri, A.M.3    Sacchi, G.4    Appel, G.B.5    D'Agati, V.D.6
  • 86
    • 0031820563 scopus 로고    scopus 로고
    • Fibrillary glomerulopathy
    • Brady HR. Fibrillary glomerulopathy. Kidney Int 1998; 53: 1421-9.
    • (1998) Kidney Int , vol.53 , pp. 1421-1429
    • Brady, H.R.1
  • 87
    • 0036405058 scopus 로고    scopus 로고
    • Fibrillary glomerulonephritis and immunotactoid (microtubular) glomerulopathy are associated with distinct immunologic features
    • Bridoux F, Hugue V, Coldefy O, Goujon JM, Bauwens M, Sechet A, Preud'Homme JL, Touchard G. Fibrillary glomerulonephritis and immunotactoid (microtubular) glomerulopathy are associated with distinct immunologic features. Kidney Int 2002; 62: 1764-75.
    • (2002) Kidney Int , vol.62 , pp. 1764-1775
    • Bridoux, F.1    Hugue, V.2    Coldefy, O.3    Goujon, J.M.4    Bauwens, M.5    Sechet, A.6    Preud'Homme, J.L.7    Touchard, G.8
  • 88
    • 0028252156 scopus 로고
    • Glomerulonephritis with organized micrombular monoclonal immunoglobulin deposits
    • Touchard G, Bauwens M, Goujon JM. Glomerulonephritis with organized micrombular monoclonal immunoglobulin deposits. Adv Nephrol Necker Hosp 1994; 23: 149-75.
    • (1994) Adv Nephrol Necker Hosp , vol.23 , pp. 149-175
    • Touchard, G.1    Bauwens, M.2    Goujon, J.M.3
  • 89
    • 0032714322 scopus 로고    scopus 로고
    • Fibrillary-immunotactoid glomerulopathy with renal deposits of IgAλ: A rare cause of glomerulonephritis
    • Van Ginneken EE, Assmann KJ, Koolen MI. Fibrillary-immunotactoid glomerulopathy with renal deposits of IgAλ: a rare cause of glomerulonephritis. Clin Nephrol 1999; 52: 383-9.
    • (1999) Clin Nephrol , vol.52 , pp. 383-389
    • Van Ginneken, E.E.1    Assmann, K.J.2    Koolen, M.I.3
  • 90
    • 0033040166 scopus 로고    scopus 로고
    • Paraneoplastic glomerulopathies: New insights into an old entity
    • Ronco PM. Paraneoplastic glomerulopathies: new insights into an old entity. Kidney Int 1999; 56: 355-77.
    • (1999) Kidney Int , vol.56 , pp. 355-377
    • Ronco, P.M.1
  • 91
    • 0347992788 scopus 로고    scopus 로고
    • Proliferative glomerulonephritis with monoclonal IgG deposits. A distinct entity mimicking immunocomplex glomerulonephritis
    • Nasr SH, Markowitz GS, Stokes MB. Proliferative glomerulonephritis with monoclonal IgG deposits. A distinct entity mimicking immunocomplex glomerulonephritis. Kidney Int 2004; 65: 85-96.
    • (2004) Kidney Int , vol.65 , pp. 85-96
    • Nasr, S.H.1    Markowitz, G.S.2    Stokes, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.