Immunoglobulin Light Chains and the Kidney: An Overview

References

• Gallo G, Picken M, Buxbaum J, Frangione B. The spectrum of monoclonal immunoglobulin deposition disease associated with immunocytic dyscrasias. Semin Hematol. 1989; 26: 234–245
   PubMed Web of Science ®Google Scholar
• Kyle R A. Kidney in multiple myeloma and related disorders. The Kidney in Plasma Cell Dyscrasias, L Minetti, G ďAmico, C Ponticelli. Kluwer Academic Publishers, Dordrecht/Boston/London 1988; 141–151
   Google Scholar
• Sanders P W, Herrera G A, Kirk K A, Old C W, Galla J H. Spectrum of glomerular and tubulointerstitial renal lesions associated with monotypical immunoglobulin light chain deposition. Lab Invest. 1991; 64: 527–537
   PubMed Web of Science ®Google Scholar
• Pirani C L, Silva F, ďAgati V, Chander P, Striker L MM. Renal lesions in plasma cell dyscrasias: Ultrastructural observations. Am J Kidney Dis. 1987; 10: 208–221
   PubMed Web of Science ®Google Scholar
• Frangione B. Systemic and cerebral amyloidosis. Ann Med. 1989; 21: 69–72
   PubMed Web of Science ®Google Scholar
• Husby G, Araki S, Benditt E, Benson M, Cohen A S, Frangione B, Glenner G G, Natvig J B, Westermark P. The 1990 guidelines for nomenclature and classification of amyloid and amyloidosis. Amyloid and Amyloidosis 1990, J B Natvig, O Forre, G Husby, A Huse-Bekk, B Skogen, K Sletten, P Westermark. Kluwer Academic Publishers, Dordrecht, Boston, London 1991; 7–11
   Google Scholar
• Benson M. Developments in the understanding of amyloid nephropathy. Presented at the 25th Annual Meeting of the American Society of Nephrology, Baltimore, MD, 1992, M D Benson, J Liepnieks, T Vemichi, G Wheeler, Hereditary renal amyloidosis associated with a mutant α-brogen a-chain. Nature Genetics. 1993;3: 252–255.
   Google Scholar
• Gallo G, Picken M M, Frangione B, Buxbaum J. Nonamy-loidotic monoclonal immunoglobulin deposits lack amyloid P component. Mod Pathol. 1988; 1: 453–456
   PubMedGoogle Scholar
• Korbet S M, Schwartz M M, Rosenberg B F, Sibley R K, Lewis E J. Immunotactoid glomerulopathy. Medicine 1985; 64: 228–243
   PubMed Web of Science ®Google Scholar
• Esparza A R, Chazan J A, Nayak R N, Cavallo T. Fibrillary (immunotactoid) glomerulopathy. A possible role for kappa light chain in its etiology and/or pathogenesis. Am J Surg Pathol. 1991; 7: 632–643
   Google Scholar
• Alpers C E. Immunotactoid (microtubular) glomerulopathy: an entity distinct from fibrillary glomerulonephritis?. Am J Kidney Dis. 1992; 19: 185–191
   PubMed Web of Science ®Google Scholar
• Yang G CH, Nieto R, Stachura I, Gallo G R. Ultrastructural immunohistochemical localization of polyclonal IgG, C3, and amyloid P component on the Congo red-negative amyloid-like fibrils of fibrillary glomerulopathy. Am J Pathol. 1992; 141: 409–419
   PubMedGoogle Scholar
• Herrera G A, Paul R, Turbat-Herrera E A, Work J, Viale G, Dell'Orto P, Lott R L, Colombi R, Old C W, Leyrly R H, Coggi G. Ultrastructural immunolabeling in the diagnosis of light-chain related renal disease. Pathol Immunopathol Res. 1986; 5: 170
   PubMedGoogle Scholar
• Picken M M, Frangione B, Barlogie B, Luna M, Gallo G. Light chain deposition disease derived from K, light chain subgroup. Biochemical characterization. Am J Pathol. 1989; 134: 749–754
   PubMed Web of Science ®Google Scholar
• Cogne M, Preuďhomme J L, Bauwens M, Touchard G, Aucouturier P. Structure of a monoclonal kappa light chain VKiv subgroup in the kidney and plasma cells in light chain deposition disease. J Clin Invest. 1991; 87: 2188–2190
   Web of Science ®Google Scholar
• Khamlichi A A, Aucouturier P, Silvain C, Bauwens M, Touchard, Preuďhomme J L, Nau F, Cogne M. Primary structure of a monoclonal K chain in myeloma with light chain deposition disease. Clin Exp Immunol. 1992; 87: 122–126
   PubMed Web of Science ®Google Scholar
• Li J J, McAdam K PWJ. Human amyloid P component. An elastase inhibitor. Scand J Immunol. 1984; 20: 219–226
   PubMed Web of Science ®Google Scholar
• Abraham C R, Selkoe D J, Potter H. Immunochemical identification of the serine protease inhibitor α1-antichymo-trypsin in the brain amyloid deposits of Alzheimer's disease. Cell 1988; 52: 487–501
   PubMed Web of Science ®Google Scholar
• Picken M M, Larrondo-Lillo M, Coria F, Gallo G R, Shelanski M L, Frangione B. Distribution of the protease inhibitor α1,-antichymotrypsis in cerebral and systemic amyloid. J Neuropathol Exp Neurol. 1990; 49: 41–48
   PubMed Web of Science ®Google Scholar
• Campistol J M, Shirahama T, Abraham C, Bernard D, Cohen A S, Skinner M. Immunochemical demonstration of plasma proteinase inhibitors in β2-microglobulin amyloid deposits. Presented at the 25th Annual Meeting of the American Society of Nephrology, Baltimore, MD, 1992, 375A
   Google Scholar
• Shirahama T, Miura K, Ju S T, Kisilevsky R, Gruys E, Cohen A S. Amyloid enhancing factor-loaded macrophages in amyloid fibril formation. Lab Invest. 1990; 62: 61
   PubMed Web of Science ®Google Scholar
• Picken M M, Gallo G R, Frangione B. Amyloid enhancing factor and inflammatory reaction. Lab Invest. 1990; 63: 586
   PubMedGoogle Scholar
• Feiner H, Gallo G. Ultrastructure in glomerulonephritis associated with cryoglobulinemia. Am J Pathol. 1977; 88: 145–162
   PubMed Web of Science ®Google Scholar
• Churg J, Grishman E. Ultrastructure of immune deposits in renal glomeruli. Ann Intern Med. 1972; 76: 479
   PubMed Web of Science ®Google Scholar
• Hachimi K HE, Verga L, Giaccone G, Tagliavini F, Frangione B, Bugiani O, Foncini J P. Relationship between non-fibrillary amyloid precursors and cell processes in the cortical neuropil of Alzheimer patients. Neuroscience Lett. 1991; 129: 119–122
   PubMedGoogle Scholar