The mesangium as a target for glomerulopathic light and heavy chains: Pathogenic considerations in light and heavy chain-mediated glomerular damage

Contributions to Nephrology

Volumn 153, Issue , 2007, Pages 116-134

  Keeling, John ^a   Herrera, Guillermo A ^a  

^a SAINT LOUIS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN;

AMYLOIDOSIS; ANIMAL; DISEASE MODEL; GLOMERULONEPHRITIS; HUMAN; IMMUNOLOGY; KIDNEY DISEASE; MESANGIUM; PARAPROTEINEMIA; PATHOLOGY; PATHOPHYSIOLOGY; PHYSIOLOGY; REVIEW;

AMYLOIDOSIS; ANIMALS; DISEASE MODELS, ANIMAL; GLOMERULAR MESANGIUM; GLOMERULONEPHRITIS; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN LIGHT CHAINS; KIDNEY DISEASES; PARAPROTEINEMIAS;

EID: 33751536045     PISSN: 03025144     EISSN: None     Source Type: Book Series    
DOI: 10.1159/000096764     Document Type: Review

References (82)

1. Johnson RJ, Floege J, Yoshimura A, et al: The activated mesangial cell: a glomerular 'myofibroblast'? J Am Soc Nephrol 1992;2:S190-S197.
2. Davies M: The mesangial cell: a tissue culture view. Kidney Int 1994;45:320-327.
3. Inkyo-Hayasaka K, Sakai T, Kobayashi N, et al: Three-dimensional anaylsis of the whole mesangium in the rat. Kidney Int 1996;50:67-683.
4. Schlondorff D: Roles of the mesangium in glomerular function. Kidney Int 1996;49:1583-1585.
5. Herrera GA: Renal manifestations of plasma cell dyscrasias: an appraisal from the patient's bedside to the research laboratory. Ann Diagn Pathol 2000;4:174-200.
6. Bellotti V, Mangione P, Merlini G: Review: immunoglobulin light chain amyloidosis - the archetype of structural and pathogenic variability. J Struct Biol 2000;130:280-289.
7. Abraham RS, Geyer SM, Price-Troska TL, et al: Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003;101:3801-3808.
8. Preud'homme JL, Aucouturier P, Touchard, et al: Monoclonal immunoglobulin deposition disease (Randall type). Relationship with structural abnormalities of immunoglobulin chains. Kidney Int 1994;46:965-972.
9. Nyquist J, Ramstad HM, Sletten K, et al: Structural studies of two carbohydrate-containing immunoglobulin-kappa-light chain amyloid fibril-proteins of the variable group 1; in Kisilevsky R, Benson MD, Frangione B, Gsuldie J, Muckle TJ, Young ID (eds): Amyloid and Amyloidosis. New York, Partenton Pub., 1993, pp 247-249.
10. Wetzel R: Domain stability in immunoglobulin light chain deposition disorders. Adv Protein Chem 1997;50:183-242.
11. Stevens FJ, Myatt EA, Chang C-H, et al: A molecular model for self-assembly of amyloid fibrils: immunoglobulin light chains. Biochem 1995;34:10697-10702.
12. Omtvedt LA, Bailey D, Renouf DV, et al: Glycosylated of immunoglobin light chains associated with amyloidosis. Amyloid 2000;7:227-244.
13. Khamlichi AA, Aucouturier P, Preud'homme JL, et al: Structure of abnormal heavy chains in human heavy-chain-deposition disease. Eur J Biochem 1995;229:54-60.
14. Cogne M, Silvain C, Khamlichi AA, Preud'homme JL: Structurally abnormal immunoglobins in human immunoproliferative disorders. Blood 1992;79:2181-2195.
15. Ronco PM, Aucouturier P: The molecular bases of plasma cell dyscrasia-related diseases. Nephrol Dial Transplant 1999;14:4-8.
16. Hendershot L, Bole D, Kohler G, et al: Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J Cell Biol 1987;104:761-767.
17. Solomon A, Frangione B, Franklin EC: Bence Jones proteins and light chain of immunoglobulins. Preferential association of the λ VI subgroup of human light chains with amyloidosis AL. J Clin Invest 1982;70:453-460.
18. L germ line gene use and clonal plasma cell burden. Blood 2001;98:714-720.
19. von Gise H, Christ H, Bohle A: Early glomerular lesions in amyloidosis. Electronmicroscopic findings. Virchows Arch A Pathol Anat Histol 1981;390:259-272.
20. Herrera GA, Russell WJ, Isaac J, et al: Glomerulopathic light chain-mesangial cell interactions modulate in vitro extracellular matrix remodeling and reproduce mesangiopathic findings documented in vivo. Ultrastruct Pathol 1999;23:107-126.
21. Herrera G: Renal manifestations of plasma cell dyscrasias: an appraisal from the patient's bedside to the research laboratory. Ann Diagn Pathol 2000;4:174-200.
22. Tagouri YM, Sanders PW, Picken MM, Siegal GP, Kerby JD, Herrera GA: In vitro AL-amyloid formation by rat and human mesangial cells. Lab Invest 1996;74:290-302.
23. Isaac J, Kerby J, Russell W, Dempsey S, et al: In vitro modulation of AL-amyloid formation by human mesangial cells exposed to amyloidogenic light chains. Amyloid 1998;5:238-246.
24. Hrncic R, Wall J, Wolfenbarger DA, et al: Antibody-mediated resolution of light chain-associated amyloid deposits. Am J Pathol 2000;157:1239-1246.
25. Kapadia SB: Multiple myeloma: a clinicopathologic study of 62 consecutively autopsied cases. Medicine (Baltimore) 1980;59:380-392.
26. 1 integrins in monoclonal light chain-related renal diseases. Mod Pathol 1997;10:485-195.
27. Sanders PW, Herrera GA, Kirk KA, et al: Spectrum of glomerular and tubulointerstitial renal lesions associated with monotypical immunoglobulin light chain deposition. Lab Invest 1991;64:527-537.
28. Kyle RA: Multiple myeloma: review of 869 cases. Mayo Clin Proc 1975;50:29-40.
29. Schnaper HW, Kopp JB, Poncelet AC, et al: Increased expression of extracellular matrix proteins and decreased expression of matrix proteases after serial passage of glomerular mesangial cells. J Cell Sci 1996;109:2521-2528.
30. Johnson RJ: The glomerular response to injury: progression or resolution. Kidney Int 1994;45:1769-1782.
31. Keeling J, Herrera GA: MMP-7 expression and the accumulation of tenascin in light chain deposition disease mesangial nodules. J Am Soc Nephrol 2005;16:663A.
32. Ronco PM, Alyanakian M-A, Mougenot B, et al: Light chain deposition disease: a model of glomerulosclerosis defined at the molecular level. J Am Soc Nephrol 2001;12:1558-1565.
33. Darby I, Skalli O, Gabbiani G: α-Smooth muscle actin is transiently expressed by myofibroblasts during experimental wound healing. Lab Invest 1990;63:21-29.
34. Watanabe S, Yoshimura A, Inui K, et al: Acquisition of the monocyte/macrophage phenotype in human mesangial cells. J Lab Clin Med 2001;138:193-199.
35. Herrera GA, Russell WJ, Cardelli J: Phenotypic transformation of mesangial cells precedes and is required for AL-amyloidogenesis in amyloid and amyloidosis; in Bely Miklos AA (ed): The Proceedings of the IXth International Symposium on Amyloidosis. Budapest, Hungary, David Apathy, 2001, pp 267-272.
36. Striker LJ, Doi T, Elliot S, et al: The contribution of glomerular mesangial cells to progressive glomerulosclerosis. Semin Nephrol 1989;9:318-328.
37. Keeling J, Teng J, Herrera GA: AL-amyloidosis and light chain deposition disease light chains induce divergent phenotypic transformations of human mesangial cells. Lab Invest 2004;84:1322-1338.
38. Shirahama T, Cohen AS: An analysis of the close relationship of lysosomes to early deposits of amyloid. Am J Pathol 1973;73:97-114.
39. Shirahama T, Cohen AS: Intralysosomal formation of amyloid fibrils. Am J Pathol 1975;81:101-116.
40. Bohne S, Sletten K, Menard R, et al: Cleavage of AL amyloid proteins and AL amyloid deposits by cathepsins B, K, and L. J Pathol 2004;203:528-537.
41. Teng J, Russell WJ, Gu X, et al: Different types of glomerulopathic light chains interact with mesangial cells using a common receptor but exhibit different intracellular trafficking patterns. Lab Invest 2004;84:440-451.
42. Rovin BH, Dickerson JA, Tan LC, et al: Activation of nuclear factor κβ correlates with MCP-1 expression by human mesangial cells. Kidney Int 1995;48:1263-1271.
43. Russell WJ, Cardelli J, Harris E, et al: Monoclonal light chain - mesangial cell interactions: early signaling events and subsequent pathologic effects. Lab Invest 2001;81:689-703.
44. Duque N, Gomez-Guerro C, Egido J: Interaction of IgA with Fc α receptors of human mesangial cells activates transcription factor nuclear factor-κβ and induces expression and synthesis of monocyte chemoattractant protein-1, IL-8, and IFN-inducible protein 10. J Immunol 1997;159:3474-3482.
45. Tagouri YM, Sanders PW, Zhu L, et al: Glomerulopathic monoclonal light chains potentiate mesangial cell apoptosis in vitro (abstract). Lab Invest, Mod Pathol 1995;8:161A.
46. Herrera GA, Shultz JJ, Soong SJ, et al: Growth factors in monoclonal light-chain-related renal diseases. Hum Pathol 1994;25:883-892.
47. Sugiyama H, Kashihara N, Makino H, et al: Apoptosis in glomerular sclerosis. Kidney Int 1996;49:103-111.
48. Teng J, Zhang PL, Russell WJ, et al: Insights into mechanisms responsible for mesangial alterations associated with fibrogenic glomerulopathic light chains. Nephron Physiol 2003;94:28-38.
49. Zhu L, Herrera GA, Murphy-Ullrich JE, et al: Pathogenesis of glomerulosclerosis in light chain deposition disease. Role for transforming growth factor-beta. Am J Pathol 1995;147:375-385.
50. Vu TH, Werb Z: Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 2000;14:2123-2133.
51. Gaire M, Magbanua Z, McDonnell S, et al: Structure and expression of the human gene for the matrix metalloproteinase matrilysin. J Biol Chem 1994;269:2032-2040.
52. Parks WC: Matrix metalloproteinases in repair. Wound Rep Reg 1999;7:423-432.
53. Bernardo M, Fridman R: TIMP-2 (tissue inhibitor of metalloproteinases-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP. Biochem J 2003;374:739-745.
54. Pardo A, Selman M: MMP-1: the elder of the family. Int J Biochem Cell Biol 2005;37:283-288.
55. Mott JD, Werb Z: Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 2004;16:558-564.
56. Murphy G, Stanton H, Cowell S, et al: Mechanisms for pro matrix metalloproteinase activation. APMIS 1999;107:38-44.
57. Egeblad M, Werb Z: New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-174.
58. Massova I, Kotra LP, Fridman R, et al: Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 1998;12:1075-1095.
59. Nagase H, Woessner Jr JF: Matrix metalloproteinases. J Biol Chem 1999;274:21491-21494.
60. Snoek-van Beurden PAM, Von den Hoff JW: Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. Biotechniques 2005;38:73-83.
61. Van Wart HE, Birkedal-Hansen H: The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990;87:5578-5582.
62. Steffensen B, Hakkinen L, Larjava H: Proteolytic events of wound-healing-coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules. Crit Rev Oral Biol Med 2001;12:373-398.
63. Visse R, Nagase H: Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, funtion, and biochemistry. Circ Res 2003;92:827-839.
64. Harendza S, Pollack AS, Mertens PR, et al: Tissue-specific enhancer-promoter interactions regulate high level constituitive expression of matrix metalloproteinase 2 by glomerular mesangial cells. J Biol Chem 1995;270:18786-18796.
65. Mertens PR, Harendza S, Pollock AS, et al: Glomerular mesangial cell-specific transactivation of matrix metalloproteinase 2 transcription is mediated by YB-1. J Biol Chem 1997;272:22905-22912.
66. Mignatti P: Extracellular matrix remodeling by metalloproteinases and plasminogen activators. Kidney Int 1995;47:S12-S14.
67. Imai K, Kusakabeb M, Sakakurac T, et al: Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases. FEBS Lett 1994;352:216-218.
68. Keeling J, Herrera GA: Matrix composition alters matrix metalloproteinase expression in mesangial cells incubated with glomerulopathic light chains. Lab Invest 2005;85:267A.
69. Truong LD, Pindur J, Barrios R, et al: Tenascin is an important component of the glomerular extracellular matrix in normal and pathologic conditions. Kidney Int 1994;45:201-210.
70. Jones FS, Jones PL: The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev Dyn 2000;218:235-259.
71. Kuhn C, Mason RJ: Immulocalization of SPARC, tenascin and thrombospondin in pulmonary fibrosis. Am J Pathol 1995;147:1759-1769.
72. Sakamura T, Kusano I: Tenascin in tissue perturbation repair. Acta Pathol Jpn 1991;41:247-258.
73. Hernandez-Barrantes S, Bernardo M, Toth M, et al: Regulation of membrane type-matrix metalloproteinases. Cancer Biol 2002;12:131-138.
74. Sounni NE, Noel A: Membrane type-matrix metalloproteinases and tumor progression. Biochimie 2004;877:329-342.
75. Sato H, Takino T, Okada Y, et al: A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 1994;370:61-65.
76. Puente XS, Pendas AM, Llano E, et al: Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res 1996;56:944-949.
77. Kanwar YS, Ota K, Yang Q, et al: Role of membrane-type matrix metalloproteinase 1 (MT-1-MMP), MMP-2, and its inhibitor in nephrogenesis. Am J Physiol 1999;277:F934-F947.
78. Seiki M: Membrane-type matrix metalloproteinases. APMIS 1999;107:137-143.
79. Stetler-Stevenson WG: Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix. Am J Pathol 1996;148:1345-1350.
80. Bruneval P, Foidart JM, Nochy D, et al: Glomerular matrix proteins in nodular glomerulosclerosis in association with light chain deposition disease and diabetes mellitus. Hum Pathol 1985;16:477-484.
81. Martin J, Eynstone L, Davies M, et al: Induction of metalloproteinases by glomerular mesangial cells stimulated by proteins of the extracellular matrix. J Am Soc Nephrol 2001;12:88-96.
82. Saito K, Shimizu F, Sato T, et al: Modulation of human mesangial cell behaviour by extracellular matrix components-the possible role of interstitial type III collagen. Clin Exp Immunol 1993;91:510-515.