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Volumn 7, Issue 2, 1999, Pages 167-177

Progressive renal disease: Fibroblasts, extracellular matrix, and integrins

Author keywords

Extracellular matrix; Fibrosis; Integrins; Interstitital fibroblasts

Indexed keywords

INTEGRIN;

EID: 0032956765     PISSN: 10187782     EISSN: None     Source Type: Journal    
DOI: 10.1159/000020597     Document Type: Review
Times cited : (68)

References (94)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hyres RO: Integrins: Versatility, modulation and signaling in cell adhesion. Cell 1992;69: 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hyres, R.O.1
  • 2
    • 0030224080 scopus 로고    scopus 로고
    • Integrins in cell adhesion and signaling
    • Akiyama SK: Integrins in cell adhesion and signaling. Hum Cell 1996;9:181-186.
    • (1996) Hum Cell , vol.9 , pp. 181-186
    • Akiyama, S.K.1
  • 3
    • 0028987936 scopus 로고    scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS: Integrins and signal transduction pathways: The road taken. Science 1996;268:233-239.
    • (1996) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 4
    • 0030777243 scopus 로고    scopus 로고
    • Integrin signaling: Specificity and control of cell survival and cell cycle progression
    • Giancotti FG: Integrin signaling: Specificity and control of cell survival and cell cycle progression. Curr Opin Cell Biol 1997;9:691-700.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 691-700
    • Giancotti, F.G.1
  • 6
    • 0031258760 scopus 로고    scopus 로고
    • Integrin signaling
    • Yamada KM: Integrin signaling. Matrix Biol 1997;16:137-141.
    • (1997) Matrix Biol , vol.16 , pp. 137-141
    • Yamada, K.M.1
  • 7
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano RL, Haskill S: Signal transduction from the extracellular matrix. J Cell Biol 1993;120: 577-580.
    • (1993) J Cell Biol , vol.120 , pp. 577-580
    • Juliano, R.L.1    Haskill, S.2
  • 8
    • 0030901145 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor cooperates with integrin avβ5 to promote tumor cell dissemination in vivo
    • Brooks PC, Klemke RL, Schön S, Lewis JM; Schwartz MA, Cheresh DA: Insulin-like growth factor receptor cooperates with integrin avβ5 to promote tumor cell dissemination in vivo. J Clin Invest 1997;99:1390-1398.
    • (1997) J Clin Invest , vol.99 , pp. 1390-1398
    • Brooks, P.C.1    Klemke, R.L.2    Schön, S.3    Lewis, J.M.4    Schwartz, M.A.5    Cheresh, D.A.6
  • 12
    • 0031053137 scopus 로고    scopus 로고
    • The cell adhesion molecule L1: Species- and cell-type-dependent multiple binding mechanisms
    • Kadmon G, Altevogt P: The cell adhesion molecule L1: Species- and cell-type-dependent multiple binding mechanisms. Differentiation 1997;61:143-150.
    • (1997) Differentiation , vol.61 , pp. 143-150
    • Kadmon, G.1    Altevogt, P.2
  • 14
    • 0023633741 scopus 로고
    • Cell adhesion protein receptors are targets for transforming growth factor-β
    • Ignotz RA, Massague J: Cell adhesion protein receptors are targets for transforming growth factor-β. Cell 1987;51:189-195.
    • (1987) Cell , vol.51 , pp. 189-195
    • Ignotz, R.A.1    Massague, J.2
  • 15
    • 0030994656 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 potentiates vascular smooth muscle cell migration to platelet-derived growth factor: Upregulation of integrin and disassembly of actin filaments
    • Pickering JG, Uniyal S, Ford CM, Chau T, Laurin MA, Chow LH, Ellis CG, Fish J, Chan BM: Fibroblast growth factor-2 potentiates vascular smooth muscle cell migration to platelet-derived growth factor: Upregulation of integrin and disassembly of actin filaments. Circ Res 1997;80:627-637.
    • (1997) Circ Res , vol.80 , pp. 627-637
    • Pickering, J.G.1    Uniyal, S.2    Ford, C.M.3    Chau, T.4    Laurin, M.A.5    Chow, L.H.6    Ellis, C.G.7    Fish, J.8    Chan, B.M.9
  • 16
    • 0030023905 scopus 로고    scopus 로고
    • Extracellular matrix alters pdgf regulation of fibroblast integrins
    • Xu J, Clark RAF: Extracellular matrix alters PDGF regulation of fibroblast integrins. J Cell Biol 1996;132:239-249.
    • (1996) J Cell Biol , vol.132 , pp. 239-249
    • Xu, J.1    Clark, R.A.F.2
  • 18
    • 0345031255 scopus 로고    scopus 로고
    • Integrins and repair after acute renal injury
    • Paller M: Integrins and repair after acute renal injury. Kidney Int 1997;52(suppl 61):52-55.
    • (1997) Kidney Int , vol.52 , Issue.SUPPL. 61 , pp. 52-55
    • Paller, M.1
  • 20
    • 0030765404 scopus 로고    scopus 로고
    • Two novel probes reveal tubular and vascular Arg-Gly-Asp (RGD) binding sites in the ischemic rat kidney
    • Romanov V, Noiri E, Czerwinski G, Finsinger D, Kesser H, Goligorsky MS: Two novel probes reveal tubular and vascular Arg-Gly-Asp (RGD) binding sites in the ischemic rat kidney. Kidney Int 1997;52:93-102.
    • (1997) Kidney Int , vol.52 , pp. 93-102
    • Romanov, V.1    Noiri, E.2    Czerwinski, G.3    Finsinger, D.4    Kesser, H.5    Goligorsky, M.S.6
  • 22
    • 0030842899 scopus 로고    scopus 로고
    • Importance of the tubulointerstitium in human glomerulonephritis. II. Distribution of integrin chains β1, α1 to 6 and αV
    • Roy-Chaudhury P, Hillis G, McDonald S, Simpson JG, Power DA: Importance of the tubulointerstitium in human glomerulonephritis. II. Distribution of integrin chains β1, α1 to 6 and αV. Kidney Int 1997;52:103-110.
    • (1997) Kidney Int , vol.52 , pp. 103-110
    • Roy-Chaudhury, P.1    Hillis, G.2    McDonald, S.3    Simpson, J.G.4    Power, D.A.5
  • 25
    • 0027968246 scopus 로고
    • Extracellular matrix accumulation in immune mediated tubulointerstitial injury
    • Tang WW, Feng L, Xia Y, Wilson CB: Extracellular matrix accumulation in immune mediated tubulointerstitial injury. Kidney Int 1994;45:1077-1084.
    • (1994) Kidney Int , vol.45 , pp. 1077-1084
    • Tang, W.W.1    Feng, L.2    Xia, Y.3    Wilson, C.B.4
  • 26
    • 0030419494 scopus 로고    scopus 로고
    • Molecular insights into renal interstitial fibrosis
    • Eddy A: Molecular insights into renal interstitial fibrosis. J Am Soc Nephrol 1996;7:2495-2508.
    • (1996) J Am Soc Nephrol , vol.7 , pp. 2495-2508
    • Eddy, A.1
  • 27
    • 0029963991 scopus 로고    scopus 로고
    • Morphology of interstitial cells in the healthy kidney
    • Kaissling B, Hegyi I, Loffing J, Le Hir M: Morphology of interstitial cells in the healthy kidney. Anat Embryol 1996;193:303-318.
    • (1996) Anat Embryol , vol.193 , pp. 303-318
    • Kaissling, B.1    Hegyi, I.2    Loffing, J.3    Le Hir, M.4
  • 29
    • 0030773542 scopus 로고    scopus 로고
    • The fibroblast-specific Mab AS02: A novel tool for detection and elimination of human fibroblasts
    • Saalbach A, Aust G, Haustein UF, Herrman K, Anderegg U: The fibroblast-specific Mab AS02: A novel tool for detection and elimination of human fibroblasts. Cell Tissue Res 1997;290:593-599.
    • (1997) Cell Tissue Res , vol.290 , pp. 593-599
    • Saalbach, A.1    Aust, G.2    Haustein, U.F.3    Herrman, K.4    Anderegg, U.5
  • 31
    • 0029265873 scopus 로고
    • Renal scarring: A multi-organ approach to fibrosis
    • El Nahas M: Renal scarring: A multi-organ approach to fibrosis. Exp Nephrol 1995;3:65-148.
    • (1995) Exp Nephrol , vol.3 , pp. 65-148
    • El Nahas, M.1
  • 32
    • 0028122690 scopus 로고
    • Heterogeneity of myofibroblast phenotypic features: An example of fibroblastic cell plasticity
    • Schmitt-Graff A, Desmoulière A, Gabbiani G: Heterogeneity of myofibroblast phenotypic features: An example of fibroblastic cell plasticity. Virchows Arch 1994;425:3-24.
    • (1994) Virchows Arch , vol.425 , pp. 3-24
    • Schmitt-Graff, A.1    Desmoulière, A.2    Gabbiani, G.3
  • 33
    • 0031985789 scopus 로고    scopus 로고
    • Demonstration of collagen type VI and alpha-smooth muscle actin in renal fibrotic injury in man
    • Groma V: Demonstration of collagen type VI and alpha-smooth muscle actin in renal fibrotic injury in man. Nephrol Dial Transplant 1998; 13:305-312.
    • (1998) Nephrol Dial Transplant , vol.13 , pp. 305-312
    • Groma, V.1
  • 34
    • 0039056496 scopus 로고    scopus 로고
    • Location of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidney
    • Hägg PM, Hägg PO, Peltonen S, Autio-Harmainen H, Pihlajaniemi T: Location of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidney. Am J Pathol 1997;150:2075-2086.
    • (1997) Am J Pathol , vol.150 , pp. 2075-2086
    • Hägg, P.M.1    Hägg, P.O.2    Peltonen, S.3    Autio-Harmainen, H.4    Pihlajaniemi, T.5
  • 36
    • 0031046646 scopus 로고    scopus 로고
    • Growth factors in the extracellular matrix
    • Taipale J, Keski-Oja J: Growth factors in the extracellular matrix. FASEB J 1997;11:51-59.
    • (1997) FASEB J , vol.11 , pp. 51-59
    • Taipale, J.1    Keski-Oja, J.2
  • 37
    • 0031446329 scopus 로고    scopus 로고
    • Cytokines, growth factors and renal injury: Where do we go from here?
    • Johnson RJ: Cytokines, growth factors and renal injury: Where do we go from here? Kidney Int 1997;52(suppl63):2-6.
    • (1997) Kidney Int , vol.52 , Issue.SUPPL. 36 , pp. 2-6
    • Johnson, R.J.1
  • 38
    • 0029953925 scopus 로고    scopus 로고
    • Syndecans: Signaling and cell adhesion
    • Couchman JR, Woods A: Syndecans: Signaling and cell adhesion. J Cell Biochem 1996;61: 578-584.
    • (1996) J Cell Biochem , vol.61 , pp. 578-584
    • Couchman, J.R.1    Woods, A.2
  • 39
    • 0026531659 scopus 로고
    • Biosynthetic and proliferative characteristics of tubulointerstitial fibroblasts probed with paracrine cytokines
    • Alvarez RJ, Sun MJ, Haverty TP, Iozzo RV, Mayers JC, Neilson EG: Biosynthetic and proliferative characteristics of tubulointerstitial fibroblasts probed with paracrine cytokines. Kidney Int 1992;41:14-23.
    • (1992) Kidney Int , vol.41 , pp. 14-23
    • Alvarez, R.J.1    Sun, M.J.2    Haverty, T.P.3    Iozzo, R.V.4    Mayers, J.C.5    Neilson, E.G.6
  • 40
    • 0030035008 scopus 로고    scopus 로고
    • Pexicrine effects of basement membrane components on paracrine signalling by renal tubular cells
    • Lewis M, Fine LG, Norman JT: Pexicrine effects of basement membrane components on paracrine signalling by renal tubular cells. Kidney Int 1996;49:48-58.
    • (1996) Kidney Int , vol.49 , pp. 48-58
    • Lewis, M.1    Fine, L.G.2    Norman, J.T.3
  • 41
    • 0026075951 scopus 로고
    • Fibroblasts of the rabbit kidney in culture. I. Characterization of growth properties and identification of cell-specific markers
    • Rodemann HP; Müller G, Knecht A, Norman JT, Fine LG: Fibroblasts of the rabbit kidney in culture. I. Characterization of growth properties and identification of cell-specific markers. Am J Physiol 1991;261:F283-F291.
    • (1991) Am J Physiol , vol.261
    • Rodemann, H.P.1    Müller, G.2    Knecht, A.3    Norman, J.T.4    Fine, L.G.5
  • 42
    • 0028913911 scopus 로고
    • Human renal fibroblast cell lines (tFKIF and tNKF) are new tools to investigate pathophysiologic mechanisms of renal interstitial fibrosis
    • Müller GA, Frank J, Rodemann HP, Engler-Blum G: Human renal fibroblast cell lines (tFKIF and tNKF) are new tools to investigate pathophysiologic mechanisms of renal interstitial fibrosis. Exp Nephrol 1995;3:127-133.
    • (1995) Exp Nephrol , vol.3 , pp. 127-133
    • Müller, G.A.1    Frank, J.2    Rodemann, H.P.3    Engler-Blum, G.4
  • 43
    • 0344984701 scopus 로고    scopus 로고
    • Hypoxia coordinately regulates extracellular matrix production and turnover to promote fibrogenesis in human renal fibroblasts: An oxygen-responsive system independent of autocrine mediators
    • submitted
    • Norman JT, Clark IM, Garcia PL: Hypoxia coordinately regulates extracellular matrix production and turnover to promote fibrogenesis in human renal fibroblasts: An oxygen-responsive system independent of autocrine mediators. Kidney Int, submitted 1999.
    • (1999) Kidney Int
    • Norman, J.T.1    Clark, I.M.2    Garcia, P.L.3
  • 45
    • 0027165676 scopus 로고
    • Impaired regulation of collagen proαl(I) mRNA and change in pattern of collagen binding integrins on scleroderma fibroblasts
    • Ivarsson M, McWhirter A, Black CM, Rubin C: Impaired regulation of collagen proαl(I) mRNA and change in pattern of collagen binding integrins on scleroderma fibroblasts. J Invest Dermatol 1993;101:216-221.
    • (1993) J Invest Dermatol , vol.101 , pp. 216-221
    • Ivarsson, M.1    McWhirter, A.2    Black, C.M.3    Rubin, C.4
  • 46
    • 0028854277 scopus 로고
    • Myofibroblasts from scleroderma skin synthesise elevated levels of collagen and tissue inhibitor of metalloproteinase (TIMP-1) with two forms of TIMP-1
    • Kirk TZ, Mark ME, Chua CC, Chua BH, Mayes MD: Myofibroblasts from scleroderma skin synthesise elevated levels of collagen and tissue inhibitor of metalloproteinase (TIMP-1) with two forms of TIMP-1. J Biol Chem 1995; 270:3423-3428.
    • (1995) J Biol Chem , vol.270 , pp. 3423-3428
    • Kirk, T.Z.1    Mark, M.E.2    Chua, C.C.3    Chua, B.H.4    Mayes, M.D.5
  • 47
    • 0031444087 scopus 로고    scopus 로고
    • Immunohistochemical expression and distribution of alpha2beta1, alpha6beta1, alpha5beta1 integrins and their extracellular ligands type IV collagen, laminin and fibronectin in palmar fibromatosis
    • Magor G, Fraggetta F, Travail S, Lanzafame S: Immunohistochemical expression and distribution of alpha2beta1, alpha6beta1, alpha5beta1 integrins and their extracellular ligands type IV collagen, laminin and fibronectin in palmar fibromatosis. Gen Diag Pathol 1997;143:203-208.
    • (1997) Gen Diag Pathol , vol.143 , pp. 203-208
    • Magor, G.1    Fraggetta, F.2    Travail, S.3    Lanzafame, S.4
  • 48
    • 13144249138 scopus 로고    scopus 로고
    • Relationships of cell proliferation and expression of integrin subunits and type I collagen in skin fibroblasts with renal lesions in patients with IDDM
    • Jin DK, Kim Y, Mauer M, Fioretto P, Vats A, Fish AJ: Relationships of cell proliferation and expression of integrin subunits and type I collagen in skin fibroblasts with renal lesions in patients with IDDM. Am J Kidney Dis 1998; 31:293-300.
    • (1998) Am J Kidney Dis , vol.31 , pp. 293-300
    • Jin, D.K.1    Kim, Y.2    Mauer, M.3    Fioretto, P.4    Vats, A.5    Fish, A.J.6
  • 49
    • 0345461657 scopus 로고    scopus 로고
    • Hypoxia alters integrin expression in human proximal tubular epithelial cells (PTE) and cortical interstitial fibroblasts (CF)
    • Orphanides C, Norman JT: Hypoxia alters integrin expression in human proximal tubular epithelial cells (PTE) and cortical interstitial fibroblasts (CF). J Am Soc Nephrol 1997;8: 523.
    • (1997) J Am Soc Nephrol , vol.8 , pp. 523
    • Orphanides, C.1    Norman, J.T.2
  • 50
    • 0025816170 scopus 로고
    • Characterisation of human renal fibroblasts in health and disease. II. In vitro growth, differentiation and collagen synthesis of fibroblasts from kidneys with interstitial fibrosis
    • Rodemann HP, Müller GA: Characterisation of human renal fibroblasts in health and disease. II. In vitro growth, differentiation and collagen synthesis of fibroblasts from kidneys with interstitial fibrosis. Am J Kidney Dis 1991;17:684-686.
    • (1991) Am J Kidney Dis , vol.17 , pp. 684-686
    • Rodemann, H.P.1    Müller, G.A.2
  • 51
    • 0345461658 scopus 로고    scopus 로고
    • Ligation of integrins (I) dictates the phenotype of rat kidney fibroblasts (NRK-49F)
    • Norman JT, Goligorsky M: Ligation of integrins (I) dictates the phenotype of rat kidney fibroblasts (NRK-49F). J Am Soc Nephrol 1997;8:523.
    • (1997) J Am Soc Nephrol , vol.8 , pp. 523
    • Norman, J.T.1    Goligorsky, M.2
  • 52
    • 0030947446 scopus 로고    scopus 로고
    • Extracellular matrix deposition, lysyl oxidase expression and myofibroblastic differentiation during the initial stages of cholestatic fibrosis in the rat
    • Desmoulière A, Darby I, Costa AM, Raccurt M, Tuchweber B, Sommer P, Gabbiani G: Extracellular matrix deposition, lysyl oxidase expression and myofibroblastic differentiation during the initial stages of cholestatic fibrosis in the rat. Lab Invest 1997;76:765-778.
    • (1997) Lab Invest , vol.76 , pp. 765-778
    • Desmoulière, A.1    Darby, I.2    Costa, A.M.3    Raccurt, M.4    Tuchweber, B.5    Sommer, P.6    Gabbiani, G.7
  • 53
    • 0030011880 scopus 로고    scopus 로고
    • A function for filamentous α-smooth muscle actin: Retardation of motility in fibroblasts
    • Rønnov-Jessen L, Petersen OW: A function for filamentous α-smooth muscle actin: Retardation of motility in fibroblasts. J Cell Biol 1996; 134:76-80.
    • (1996) J Cell Biol , vol.134 , pp. 76-80
    • Rønnov-Jessen, L.1    Petersen, O.W.2
  • 55
    • 0030662293 scopus 로고    scopus 로고
    • Expression of β1 integrins on activated mesangial cells in human glomerulonephritis
    • Kuhara T, Kagami S, Kuroda Y: Expression of β1 integrins on activated mesangial cells in human glomerulonephritis. J Am Soc Nephrol 1997;8:1679-1687.
    • (1997) J Am Soc Nephrol , vol.8 , pp. 1679-1687
    • Kuhara, T.1    Kagami, S.2    Kuroda, Y.3
  • 56
    • 0031939554 scopus 로고    scopus 로고
    • Hepatic fibrosis and wound repair: A progress report
    • Bissell DM: Hepatic fibrosis and wound repair: A progress report. J Gastroenterol 1998;33: 295-302.
    • (1998) J Gastroenterol , vol.33 , pp. 295-302
    • Bissell, D.M.1
  • 57
    • 0029665532 scopus 로고    scopus 로고
    • The alβ1 integrin is expressed during neointima formation in rat arteries and mediates collagen matrix reorganisation
    • Gotwals PJ, Chi-Rosso G, Lindner V, Yang J, Ling L, Fawell SE, Koteliansky VE: The alβ1 integrin is expressed during neointima formation in rat arteries and mediates collagen matrix reorganisation. J Clin Invest 1996;97: 2469-2477.
    • (1996) J Clin Invest , vol.97 , pp. 2469-2477
    • Gotwals, P.J.1    Chi-Rosso, G.2    Lindner, V.3    Yang, J.4    Ling, L.5    Fawell, S.E.6    Koteliansky, V.E.7
  • 58
    • 0031828004 scopus 로고    scopus 로고
    • The fibronectin domain ED-A is crucial for myofibroblastic phenotype induction by transforming growth factor-beta 1
    • Serini G, Bochaton-Piallat ML, Ropraz P, Geinoz A, Borsi L, Zardi L, Gabbiani G: The fibronectin domain ED-A is crucial for myofibroblastic phenotype induction by transforming growth factor-beta 1. J Cell Biol 1998;142: 873-881.
    • (1998) J Cell Biol , vol.142 , pp. 873-881
    • Serini, G.1    Bochaton-Piallat, M.L.2    Ropraz, P.3    Geinoz, A.4    Borsi, L.5    Zardi, L.6    Gabbiani, G.7
  • 59
    • 0344599613 scopus 로고
    • The role of extracellular matrix (ECM) and growth factors in the activation of renal fibroblasts
    • Norman JT, Lewis MP, Fine LG, Orphanides C: The role of extracellular matrix (ECM) and growth factors in the activation of renal fibroblasts. J Am Soc Nephrol 1995;6:905.
    • (1995) J Am Soc Nephrol , vol.6 , pp. 905
    • Norman, J.T.1    Lewis, M.P.2    Fine, L.G.3    Orphanides, C.4
  • 60
    • 0028851160 scopus 로고
    • Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar
    • Desmoulière A, Redard M, Darby I, Gabbiani G: Apoptosis mediates the decrease in cellularity during the transition between granulation tissue and scar. Am J Pathol 1995;146:56-66.
    • (1995) Am J Pathol , vol.146 , pp. 56-66
    • Desmoulière, A.1    Redard, M.2    Darby, I.3    Gabbiani, G.4
  • 61
    • 0030484702 scopus 로고    scopus 로고
    • Role of integrins in angiogenesis
    • Brooks P: Role of integrins in angiogenesis. Eur J Cancer 1996;32:2423-2429.
    • (1996) Eur J Cancer , vol.32 , pp. 2423-2429
    • Brooks, P.1
  • 62
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn HF, Poynton R: Oxygen sensing and molecular adaptation to hypoxia. Physiol Rev 1996;76:839-885.
    • (1996) Physiol Rev , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poynton, R.2
  • 63
    • 0031976812 scopus 로고    scopus 로고
    • Hypoxia and vascular endothelial growth factor stimulate angiogenic integrin expression in bovine microvascular endothelial cells
    • Suzuma K, Takagi H, Otani A, Honda Y: Hypoxia and vascular endothelial growth factor stimulate angiogenic integrin expression in bovine microvascular endothelial cells. J Invest Ophthalmol Vis Sci 1998;39:1028-1035.
    • (1998) J Invest Ophthalmol Vis Sci , vol.39 , pp. 1028-1035
    • Suzuma, K.1    Takagi, H.2    Otani, A.3    Honda, Y.4
  • 64
    • 0030835890 scopus 로고    scopus 로고
    • Functional expression of the α7 integrin receptor in differentiated smooth muscle cells
    • Yao CC, Breuss J, Pytela R, Kramer RH: Functional expression of the α7 integrin receptor in differentiated smooth muscle cells. J Cell Sci 1997;110:1477-1487.
    • (1997) J Cell Sci , vol.110 , pp. 1477-1487
    • Yao, C.C.1    Breuss, J.2    Pytela, R.3    Kramer, R.H.4
  • 65
    • 0028939758 scopus 로고
    • Sequence and tissue distribution of the human integrin alpha 8 subunit: A beta 1 associated alpha subunit expressed in smooth muscle cells
    • Schnapp LM, Breua JM, Ramos DM, Sheppard D, Pytela R: Sequence and tissue distribution of the human integrin alpha 8 subunit: A beta 1 associated alpha subunit expressed in smooth muscle cells. J Cell Sci 1995;108:537-544.
    • (1995) J Cell Sci , vol.108 , pp. 537-544
    • Schnapp, L.M.1    Breua, J.M.2    Ramos, D.M.3    Sheppard, D.4    Pytela, R.5
  • 67
    • 0031406579 scopus 로고    scopus 로고
    • Regulation of apoptosis by integrin receptors
    • Malik RK: Regulation of apoptosis by integrin receptors. J Pediatr Hematol Oncol 1997;19: 541-545.
    • (1997) J Pediatr Hematol Oncol , vol.19 , pp. 541-545
    • Malik, R.K.1
  • 68
    • 0030990594 scopus 로고    scopus 로고
    • Induction of apoptosis in human neuroblastoma cells by abrogation of integrin-mediated cell adhesion
    • Rozzo C, Chiesa V, Caridi G, Pagnan G, Ponzoni M: Induction of apoptosis in human neuroblastoma cells by abrogation of integrin-mediated cell adhesion. Int J Cancer 1997;70: 688-698.
    • (1997) Int J Cancer , vol.70 , pp. 688-698
    • Rozzo, C.1    Chiesa, V.2    Caridi, G.3    Pagnan, G.4    Ponzoni, M.5
  • 69
    • 0028670833 scopus 로고
    • Integrin avβ3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • Brooks PC, Montgomery AMP, Rosenfled M, Reisfeld RA, Hu T, Klier G, Cheresh DA: Integrin avβ3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 1994;79:1157-1164.
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.P.2    Rosenfled, M.3    Reisfeld, R.A.4    Hu, T.5    Klier, G.6    Cheresh, D.A.7
  • 72
    • 0030136756 scopus 로고    scopus 로고
    • Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix
    • Stetler-Stevenson WG: Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix. Am J Pathol 1996;148: 1345-1350.
    • (1996) Am J Pathol , vol.148 , pp. 1345-1350
    • Stetler-Stevenson, W.G.1
  • 73
    • 0027435065 scopus 로고
    • Tissue inhibitors of metalloproteinases (TIMP. aka ERP): Structure, control of expression and biological functions
    • Denhardt DT, Feng B, Edwards DR, Cocuzzi ET, Malyankar UM: Tissue inhibitors of metalloproteinases (TIMP. aka ERP): Structure, control of expression and biological functions. Pharmacol Ther 1993;59:329-341.
    • (1993) Pharmacol Ther , vol.59 , pp. 329-341
    • Denhardt, D.T.1    Feng, B.2    Edwards, D.R.3    Cocuzzi, E.T.4    Malyankar, U.M.5
  • 74
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez DE, Alonso DF, Yoshiji H, Thorgiesson UP: Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions. Eur J Cell Biol 1997;74:111-122.
    • (1997) Eur J Cell Biol , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgiesson, U.P.4
  • 75
    • 0028979348 scopus 로고
    • Integrin α1β1 is a positive regulator of collagenase (MMP-1) and collagen α1(I) gene expression
    • Riikonen T, Westermarck J, Koivisto L, Borberg A, Kähäri V-M, Heino J: Integrin α1β1 is a positive regulator of collagenase (MMP-1) and collagen α1(I) gene expression. J Biol Chem 1995;270:13548-13552.
    • (1995) J Biol Chem , vol.270 , pp. 13548-13552
    • Riikonen, T.1    Westermarck, J.2    Koivisto, L.3    Borberg, A.4    Kähäri, V.-M.5    Heino, J.6
  • 76
    • 0030916129 scopus 로고    scopus 로고
    • Urokinase plasminogen activator receptors associate with beta 1 and beta3 integrins of fibrosarcoma cells: Dependence on extracellular matrix components
    • Xue W, Mizumaki I, Rodd RF, Petty HR: Urokinase plasminogen activator receptors associate with beta 1 and beta3 integrins of fibrosarcoma cells: Dependence on extracellular matrix components. Cancer Res 1997;57:1682-1689.
    • (1997) Cancer Res , vol.57 , pp. 1682-1689
    • Xue, W.1    Mizumaki, I.2    Rodd, R.F.3    Petty, H.R.4
  • 77
    • 0030877824 scopus 로고    scopus 로고
    • Molecular cross talk between adhesion receptors and proteolytic cascades in vascular remodelling
    • Preissner KT, May AE, Wohn KD, Germer M, Kanse SM: Molecular cross talk between adhesion receptors and proteolytic cascades in vascular remodelling. Thromb Haemost 1997;78: 88-95.
    • (1997) Thromb Haemost , vol.78 , pp. 88-95
    • Preissner, K.T.1    May, A.E.2    Wohn, K.D.3    Germer, M.4    Kanse, S.M.5
  • 79
    • 0029954059 scopus 로고    scopus 로고
    • Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organisation of the cytoskeleton
    • Mercier I, Lechaire JP, Desmoulière A, Gaill F, Aumailley M: Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organisation of the cytoskeleton. Exp Cell Res 1996;225:245-266.
    • (1996) Exp Cell Res , vol.225 , pp. 245-266
    • Mercier, I.1    Lechaire, J.P.2    Desmoulière, A.3    Gaill, F.4    Aumailley, M.5
  • 80
    • 0030761314 scopus 로고    scopus 로고
    • Induction and repression of collagenase by keratinocytes is controlled by distinct components of different extracellular matrix components
    • Sudbeck BD, Parks WC, Welgus HG, Pentland AP: Induction and repression of collagenase by keratinocytes is controlled by distinct components of different extracellular matrix components. J Biol Chem 1997;272:22103-22110.
    • (1997) J Biol Chem , vol.272 , pp. 22103-22110
    • Sudbeck, B.D.1    Parks, W.C.2    Welgus, H.G.3    Pentland, A.P.4
  • 81
    • 0029585289 scopus 로고
    • Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins
    • Langholz O, Rockel D, Mauch C, Kozlowska E, Bank I, Kreig T: Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by α1β1 and α2β1 integrins. J Cell Biol 1995;131:1903-1915.
    • (1995) J Cell Biol , vol.131 , pp. 1903-1915
    • Langholz, O.1    Rockel, D.2    Mauch, C.3    Kozlowska, E.4    Bank, I.5    Kreig, T.6
  • 82
    • 0032496276 scopus 로고    scopus 로고
    • Fibronectin-mediated cell adhesion is required for induction of 92-kDa type IV collagenase/gelatinase (MMP-9) gene expression during macrophage differentiation
    • Xie B, Laouar A, Huberman E: Fibronectin-mediated cell adhesion is required for induction of 92-kDa type IV collagenase/gelatinase (MMP-9) gene expression during macrophage differentiation. J Biol Chem 1998;273:11576-11582.
    • (1998) J Biol Chem , vol.273 , pp. 11576-11582
    • Xie, B.1    Laouar, A.2    Huberman, E.3
  • 83
    • 0028987190 scopus 로고
    • Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z: Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol 1995;129:867-879.
    • (1995) J Cell Biol , vol.129 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5
  • 84
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjoller L, Kanse SM, Kirkergaard T, Rodenburg KW, Ronne E, Goodman SL, Preissner KT, Ossowski L, Andreasen PA: Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation. Exp Cell Res 1997;32: 420-429.
    • (1997) Exp Cell Res , vol.32 , pp. 420-429
    • Kjoller, L.1    Kanse, S.M.2    Kirkergaard, T.3    Rodenburg, K.W.4    Ronne, E.5    Goodman, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 86
    • 0031046237 scopus 로고    scopus 로고
    • Human fibroblast adhesion to fibrinogen
    • Farrell DH, Al-Mondhiry HA: Human fibroblast adhesion to fibrinogen. Biochemistry 1997;6:1123-1128.
    • (1997) Biochemistry , vol.6 , pp. 1123-1128
    • Farrell, D.H.1    Al-Mondhiry, H.A.2
  • 88
    • 0029901771 scopus 로고    scopus 로고
    • Expression of adhesion molecules in rat renal cortex during experimental hydronephrosis
    • Ricardo SD, Levinson ME, De Joseph MR, Diamond JR: Expression of adhesion molecules in rat renal cortex during experimental hydronephrosis. Kidney Int 1996;50:202-210.
    • (1996) Kidney Int , vol.50 , pp. 202-210
    • Ricardo, S.D.1    Levinson, M.E.2    De Joseph, M.R.3    Diamond, J.R.4
  • 90
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel W, Gish GD, Alves F, Pawson T: The discoidin domain receptor tyrosine kinases are activated by collagen. Mol Cell 1997;1:13-23.
    • (1997) Mol Cell , vol.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 92
    • 0027491025 scopus 로고
    • Integrin overexpression induced by high glucose and by human diabetes: Potential pathway to cell dysfunction in diabetic microangiopathy
    • Roth T, Podesta F, Stepp MA, Boeri D, Lorenzi M: Integrin overexpression induced by high glucose and by human diabetes: Potential pathway to cell dysfunction in diabetic microangiopathy. Proc Natl Acad Sci USA 1993;90: 9640-9644.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9640-9644
    • Roth, T.1    Podesta, F.2    Stepp, M.A.3    Boeri, D.4    Lorenzi, M.5
  • 93
    • 0030836233 scopus 로고    scopus 로고
    • Alterations in human glomerular epithelial cells interacting with nonenzymatically glycosylated matrix
    • Krishnamurti U, Rondeau E, Sraer JD, Michael AF, Tsilibary EC: Alterations in human glomerular epithelial cells interacting with nonenzymatically glycosylated matrix. J Biol Chem 1997;272:27966-27970.
    • (1997) J Biol Chem , vol.272 , pp. 27966-27970
    • Krishnamurti, U.1    Rondeau, E.2    Sraer, J.D.3    Michael, A.F.4    Tsilibary, E.C.5
  • 94
    • 0040037123 scopus 로고    scopus 로고
    • Glycation of the extracellular matrix (ECM) alters rat renal fibroblast (NRK-49F) growth, differentiation and ECM production
    • Norman J, Brought C, Romanov V, Goligorsky M: Glycation of the extracellular matrix (ECM) alters rat renal fibroblast (NRK-49F) growth, differentiation and ECM production. J Am Soc Nephrol 1998;9:638A.
    • (1998) J Am Soc Nephrol , vol.9
    • Norman, J.1    Brought, C.2    Romanov, V.3    Goligorsky, M.4


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