메뉴 건너뛰기




Volumn 5, Issue 4, 1998, Pages 238-246

In vitro modulation of AL-amyloid formation by Human Mesangial Cells exposed to amyloidogenic Light Chains

Author keywords

Amyloidogenic light chain; In vitro AL amyloidosis; Mesangial cells

Indexed keywords

AMYLOID; CHLOROQUINE; IMMUNOGLOBULIN LIGHT CHAIN; THROMBOSPONDIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 0032235059     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506129809007296     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 0026585875 scopus 로고
    • Mechanisms of disease: Monoclonal im-munoglobulin deposition
    • Buxbaum J (1992). Mechanisms of disease: Monoclonal im-munoglobulin deposition. Hematol/Oncol Clin N Am 6:323-346
    • (1992) Hematol/Oncol Clin N Am , vol.6 , pp. 323-346
    • Buxbaum, J.1
  • 2
    • 0017092151 scopus 로고
    • A historical note on the iodine-sulphuric acid reaction of amyloid
    • Aterman, K (1976). A historical note on the iodine-sulphuric acid reaction of amyloid. Histochemistry 49:31-143
    • (1976) Histochemistry , vol.49 , pp. 31-143
    • Aterman, K.1
  • 3
    • 0015549030 scopus 로고
    • Fibrillar assemblage of variable segments of immunoglobulin light chains: An electron microscopic study
    • Shirahama T, Benson MD, Cohen AS, and 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
  • 4
    • 0016710364 scopus 로고
    • Immunoglobulin D myeloma and amyloidosis: Immunochemical and structural studies of Bence Jones and amyloid fibrillar protein
    • White GC, Jacobson RJ, Binder RA, and Glenner GG (1975). Immunoglobulin D myeloma and amyloidosis: Immunochemical and structural studies of Bence Jones and amyloid fibrillar protein. Blood 46:713-722
    • (1975) Blood , vol.46 , pp. 713-722
    • White, G.C.1    Jacobson, R.J.2    Binder, R.A.3    Glenner, G.G.4
  • 5
    • 0019153066 scopus 로고
    • Medical Progress. Amyloid deposits and amyloidosis. The β-fibrilloses (part 1 of 2)
    • Glenner GG (1980). Medical Progress. Amyloid deposits and amyloidosis. The β-fibrilloses (part 1 of 2). N Eng J Med 302:1283-1292
    • (1980) N Eng J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 6
    • 0015274584 scopus 로고
    • Ultrastructural observations on the first amyloid to be found in the spleen of casein treated mice
    • Kazimiercrak J (1972). Ultrastructural observations on the first amyloid to be found in the spleen of casein treated mice. Acta Pathol Microbiol Scand 80:141-150
    • (1972) Acta Pathol Microbiol Scand , vol.80 , pp. 141-150
    • Kazimiercrak, J.1
  • 7
    • 0026771089 scopus 로고
    • Amyloidosis
    • Sipe J (1992). Amyloidosis. Ann Rev Biochem 61:947-974.
    • (1992) Ann Rev Biochem , vol.61 , pp. 947-974
    • Sipe, J.1
  • 9
    • 0001632706 scopus 로고
    • Does amyloid enhancing factor(AEF) exist? Is AEF a single biological entity
    • Kisilevsky R, Gruys E and Shirahama T (1995). Does amyloid enhancing factor(AEF) exist? Is AEF a single biological entity. Amyloid. In J Clin Invest 2:128-133
    • (1995) Amyloid. In J Clin Invest , vol.2 , pp. 128-133
    • Kisilevsky, R.1    Gruys, E.2    Shirahama, T.3
  • 10
    • 0028286663 scopus 로고
    • Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-amyloidosis in mice
    • Ganowiak K, Hultman P, Engstrom U, Gustavsson A and Westermark P (1994). Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-amyloidosis in mice. Biochem Biophys Res Commun 199:306-312
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 306-312
    • Ganowiak, K.1    Hultman, P.2    Engstrom, U.3    Gustavsson, A.4    Westermark, P.5
  • 13
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)
    • Solomon A and 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
  • 15
    • 0029314729 scopus 로고
    • Transforming growth factor β: An overview
    • Lawrence DA (1995). Transforming growth factor β: An overview. Kidney Int'l 47:S19-S23
    • (1995) Kidney Int'l , vol.47
    • Lawrence, D.A.1
  • 16
    • 0002606210 scopus 로고
    • TGF-β: A cytokine mediator of glomerulosclerosis and a target for therapeutic intervention
    • Border WA, Noble NA and Ketteler M(1995). TGF-β: A cytokine mediator of glomerulosclerosis and a target for therapeutic intervention. Kidney Int'l 47:S59-S61
    • (1995) Kidney Int'l , vol.47
    • Border, W.A.1    Noble, N.A.2    Ketteler, M.3
  • 17
    • 0027930261 scopus 로고
    • Growth factors in monoclonal light-chain-related renal diseases
    • Herrera GA. Shultz JJ, Soong S-J and Sanders PW (1994). Growth factors in monoclonal light-chain-related renal diseases. Hum Pathol 25:883-892
    • (1994) Hum Pathol , vol.25 , pp. 883-892
    • Herrera, G.A.1    Shultz, J.J.2    Soong, S.-J.3    Sanders, P.W.4
  • 18
    • 0028980435 scopus 로고
    • PDGF and TGF-β mediate collagen production by mesangial cells exposed to advanced glycosylation end products
    • Throckmorton DC, Brogden AP, Min B, Rasmussen H and Kashgarian M (1995). PDGF and TGF-β mediate collagen production by mesangial cells exposed to advanced glycosylation end products. Kidney Int'l 48:111-117
    • (1995) Kidney Int'l , vol.48 , pp. 111-117
    • Throckmorton, D.C.1    Brogden, A.P.2    Min, B.3    Rasmussen, H.4    Kashgarian, M.5
  • 19
    • 0025369136 scopus 로고
    • High glucose causes an increase in extracellular matrix proteins in cultured mesangial cells
    • Ayo SH, Radnik RA, Garoni JA, Glass WF II and Kreisberg JI (1990). High glucose causes an increase in extracellular matrix proteins in cultured mesangial cells. Am J Pathol 136:1339-1348
    • (1990) Am J Pathol , vol.136 , pp. 1339-1348
    • Ayo, S.H.1    Radnik, R.A.2    Garoni, J.A.3    Glass II, W.F.4    Kreisberg, J.I.5
  • 20
    • 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 and Sanders PW (1995). Pathogenesis of glomerulosclerosis in light chain deposition disease: Role for transforming growth factor-β. Am J Pathol 147:375-385
    • (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
  • 21
    • 0023473371 scopus 로고
    • Thrombospondin secretion by cultured human glomerular mesangial cells
    • Raugi GJ and Lovett DH (1987). Thrombospondin secretion by cultured human glomerular mesangial cells. Am J Pathol 129:364-372
    • (1987) Am J Pathol , vol.129 , pp. 364-372
    • Raugi, G.J.1    Lovett, D.H.2
  • 23
    • 0027991972 scopus 로고
    • Role of thrombospondin in mesangial cell growth: Possible existence of an autocrine feedback growth circuit
    • Marinides GN, Suchard SJ and Mookerjee BK (1994). Role of thrombospondin in mesangial cell growth: Possible existence of an autocrine feedback growth circuit. Kidney Int'l 46:350-357
    • (1994) Kidney Int'l , vol.46 , pp. 350-357
    • Marinides, G.N.1    Suchard, S.J.2    Mookerjee, B.K.3
  • 24
    • 0028270932 scopus 로고
    • Thrombospondin in human glomerulopathies. A marker on inflammation and early fibrosis
    • McGregor B, Colon S, Mutin M, Chignier E, Zech P and McGregor J (1994). Thrombospondin in human glomerulopathies. A marker on inflammation and early fibrosis. Am J Pathol 144:1281-1287
    • (1994) Am J Pathol , vol.144 , pp. 1281-1287
    • McGregor, B.1    Colon, S.2    Mutin, M.3    Chignier, E.4    Zech, P.5    McGregor, J.6
  • 25
    • 0026452515 scopus 로고
    • Thrombospondins: Structure and regulation of expression
    • Bornstein P (1992). Thrombospondins: structure and regulation of expression. FASEB J 6:3290-3299
    • (1992) FASEB J , vol.6 , pp. 3290-3299
    • Bornstein, P.1
  • 26
    • 0025343641 scopus 로고
    • Physiology of thrombospondin
    • Mosher DF (1990). Physiology of thrombospondin. Ann Rev Med 41:85-97
    • (1990) Ann Rev Med , vol.41 , pp. 85-97
    • Mosher, D.F.1
  • 27
    • 0027319916 scopus 로고
    • The functions of thrombospondin and its involvement in physiology and pathophysiology
    • Lahav J (1993). The functions of thrombospondin and its involvement in physiology and pathophysiology. Biochim Byophys Acta 1182:1-14
    • (1993) Biochim Byophys Acta , vol.1182 , pp. 1-14
    • Lahav, J.1
  • 28
    • 0027739741 scopus 로고
    • Inhibitors of endocytosis, endosome fusion and lysosomal processing inhibit proteolysis of the amyloid precursor protein
    • Dash PK and Moore AN (1993). Inhibitors of endocytosis, endosome fusion and lysosomal processing inhibit proteolysis of the amyloid precursor protein. Neurosci Lett 164:183-186
    • (1993) Neurosci Lett , vol.164 , pp. 183-186
    • Dash, P.K.1    Moore, A.N.2
  • 29
    • 0018872030 scopus 로고
    • Chloroquine and ammonium ion inhibit receptor-mediated endocytosis of mannose-glycoconjugates by macrophages: Apparent inhibition of receptor recycling
    • Tietze C, Schlesinger P and Stahl P (1980). Chloroquine and ammonium ion inhibit receptor-mediated endocytosis of mannose-glycoconjugates by macrophages: Apparent inhibition of receptor recycling. Biochem Biophys Res Comm 93:1-8
    • (1980) Biochem Biophys Res Comm , vol.93 , pp. 1-8
    • Tietze, C.1    Schlesinger, P.2    Stahl, P.3
  • 30
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor cycling
    • Gonzalez-Noriega A, Grubb JH, Talkad V and Sly WS (1980). Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor cycling. J Cell Biol 85:839-852
    • (1980) J Cell Biol , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 31
    • 0019866088 scopus 로고
    • Effect of weak bases on the intralysosomal pH in mouse peritoneal macrophages
    • Poole B and Ohkuma S (1981). Effect of weak bases on the intralysosomal pH in mouse peritoneal macrophages. J Cell Biol 90:665-669
    • (1981) J Cell Biol , vol.90 , pp. 665-669
    • Poole, B.1    Ohkuma, S.2
  • 32
    • 0024978029 scopus 로고
    • Role of acidic intracellular compartments in the biosynthesis of Dictyostelium lysosomal enzymes
    • Cardelli JA, Richardson J and Miears D (1989). Role of acidic intracellular compartments in the biosynthesis of Dictyostelium lysosomal enzymes. J Biol Chem 264:3454-3463
    • (1989) J Biol Chem , vol.264 , pp. 3454-3463
    • Cardelli, J.A.1    Richardson, J.2    Miears, D.3
  • 34
    • 0016212674 scopus 로고
    • Formation of "amyloid" fibrils in vitro by action of human kidney lysosomal enzymes on Bence Jones proteins
    • Epstein WV, Tan M and Wood IS (1974). Formation of "amyloid" fibrils in vitro by action of human kidney lysosomal enzymes on Bence Jones proteins. J Lab Clin Med 84:107-110
    • (1974) J Lab Clin Med , vol.84 , pp. 107-110
    • Epstein, W.V.1    Tan, M.2    Wood, I.S.3
  • 35
    • 0018118615 scopus 로고
    • Bence Jones proteins and light chains of immunoglobulins-XVII. Unique susceptibility of certain kappa chains to proteolysis by human granulocyte-derived neutral proteases
    • Solomon A and Haverman K (1978). Bence Jones proteins and light chains of immunoglobulins-XVII. Unique susceptibility of certain kappa chains to proteolysis by human granulocyte-derived neutral proteases. Immunochemistry 15:453-458
    • (1978) Immunochemistry , vol.15 , pp. 453-458
    • Solomon, A.1    Haverman, K.2
  • 36
    • 0026607225 scopus 로고
    • Pathobiology of cast nephropathy from human Bence Jones proteins
    • Sanders PW and Booker BB (1992). Pathobiology of cast nephropathy from human Bence Jones proteins. J Clin Invest 89:630-639
    • (1992) J Clin Invest , vol.89 , pp. 630-639
    • Sanders, P.W.1    Booker, B.B.2
  • 38
    • 0027305971 scopus 로고
    • Thrombospondin causes activation of latent transforming growth factor-β secreted by endothelial cells by a novel mechanism
    • Schultz-Cherry S and Murphy-Ullrich JE (1993). Thrombospondin causes activation of latent transforming growth factor-β secreted by endothelial cells by a novel mechanism. J Cell Biol 122:923-932
    • (1993) J Cell Biol , vol.122 , pp. 923-932
    • Schultz-Cherry, S.1    Murphy-Ullrich, J.E.2
  • 39
    • 0029918182 scopus 로고    scopus 로고
    • Misfolding the way to disease
    • Taub, G (1996) Misfolding the way to disease. Science 271:1493-1495
    • (1996) Science , vol.271 , pp. 1493-1495
    • Taub, G.1
  • 40
    • 0022477623 scopus 로고
    • β-transforming growth factor is stored in human blood platelets as a latent high molecular weight complex
    • Pircher R and Jullien P (1986). β-transforming growth factor is stored in human blood platelets as a latent high molecular weight complex. Biochem Biophys Res Commun 136:30-37
    • (1986) Biochem Biophys Res Commun , vol.136 , pp. 30-37
    • Pircher, R.1    Jullien, P.2
  • 41
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T and Frangione B (1992). Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett 135:235-238
    • (1992) Neurosci Lett , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.