메뉴 건너뛰기




Volumn 11, Issue 6, 1996, Pages 574-582

Proliferation, migration, matrix turnover, and death of smooth muscle cells in native coronary and vein graft atherosclerosis

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; TRANSFORMING GROWTH FACTOR BETA;

EID: 0029803097     PISSN: 02684705     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001573-199611000-00004     Document Type: Review
Times cited : (88)

References (77)
  • 1
    • 85047679683 scopus 로고
    • Proposed roles for growth factors in mediating smooth muscle proliferation in vascular pathologies
    • Newby AC, George SJ: Proposed roles for growth factors in mediating smooth muscle proliferation in vascular pathologies. Cardiovasc Res 1993, 27:1173-1183.
    • (1993) Cardiovasc Res , vol.27 , pp. 1173-1183
    • Newby, A.C.1    George, S.J.2
  • 2
    • 0030052857 scopus 로고    scopus 로고
    • An essential role for platelet- Derived growth factor in neointima formation in human saphenous vein in vitro
    • George SJ, Williams A, Newby AC: An essential role for platelet- derived growth factor in neointima formation in human saphenous vein in vitro. Atherosclerosis 1996, 120:227-240. The authors detect an intimal-to-medial concentration of mRNA for PDGF α and β chains and PDGF protein in human saphenous vein organ cultures. Neointima formation is reduced by anti-PDGF antibodies without affecting VSMC proliferation, extending to humans the observations previously made in the rat.
    • (1996) Atherosclerosis , vol.120 , pp. 227-240
    • George, S.J.1    Williams, A.2    Newby, A.C.3
  • 3
    • 0028618228 scopus 로고
    • Trapidil (triazolopyrimidine), a platelet-derived growth factor antagonist reduces restenosis after percutaneous transluminal coronary angioplasty: Results of the randomized, double-blind STARC study
    • Maresta A, Balducelli M, Cantini L, Casari A, Chioin R, Fabbri M, Fontanelli A, Preti PAM, Repetto S, De Servi S, Varani E: Trapidil (triazolopyrimidine), a platelet-derived growth factor antagonist reduces restenosis after percutaneous transluminal coronary angioplasty: results of the randomized, double-blind STARC study. Circulation 1994, 90:2710-2715.
    • (1994) Circulation , vol.90 , pp. 2710-2715
    • Maresta, A.1    Balducelli, M.2    Cantini, L.3    Casari, A.4    Chioin, R.5    Fabbri, M.6    Fontanelli, A.7    Pam, P.8    Repetto, S.9    De Servi, S.10    Varani, E.11
  • 4
    • 0026639821 scopus 로고
    • Triggering signalling cascades by receptor tyrosine kinases
    • Pazin MJ, Williams LT: Triggering signalling cascades by receptor tyrosine kinases. Trends Biochem Sci 1992, 17:374-378.
    • (1992) Trends Biochem Sci , vol.17 , pp. 374-378
    • Pazin, M.J.1    Williams, L.T.2
  • 5
    • 0029948892 scopus 로고    scopus 로고
    • Depletion of mitogen activated protein kinase using an antisense oligonucleotide approach downregulates the phenylephrine-induced hypertrophic response in rat cardiac myocytes
    • Glennon PE, Kaddouri S, Sale EM, Sale GJ, Fuller FJ, Sugden PH: Depletion of mitogen activated protein kinase using an antisense oligonucleotide approach downregulates the phenylephrine-induced hypertrophic response in rat cardiac myocytes. Circ Res 1996, 78:954-961.
    • (1996) Circ Res , vol.78 , pp. 954-961
    • Glennon, P.E.1    Kaddouri, S.2    Sale, E.M.3    Sale, G.J.4    Fuller, F.J.5    Sugden, P.H.6
  • 6
    • 0028955805 scopus 로고
    • Inhibition of rabbit aortic smooth muscle cell proliferation by selective inhibitors of protein kinase C
    • Newby AC, Lim K, Evans MA, Booth RFG: Inhibition of rabbit aortic smooth muscle cell proliferation by selective inhibitors of protein kinase C. Br J Pharmacol 1995, 114:1652-1656. A highly selective protein kinase C inhibitor was shown to inhibit with equal potency basal proliferation and responses to phorbol esters, PDGF, and PDGF plus 5-hydroxytryptamine. Complete inhibition of proliferation implies an essential role for this inhibitor in both basal and stimulated proliferation.
    • (1995) Br J Pharmacol , vol.114 , pp. 1652-1656
    • Newby, A.C.1    Lim, K.2    Evans, M.A.3    Booth, R.F.G.4
  • 7
    • 0028860780 scopus 로고
    • Signalling mechanisms in the regulation of vascular cell migration
    • Abedi H, Zachary I: Signalling mechanisms in the regulation of vascular cell migration. Cardiovasc Res 1995, 30:544-556.
    • (1995) Cardiovasc Res , vol.30 , pp. 544-556
    • Abedi, H.1    Zachary, I.2
  • 8
    • 0028330152 scopus 로고
    • Insulin-like growth factor-1 and platelet-derived growth factor-BB Induce directed migration of human arterial smooth muscle cells via signaling pathways that are distinct from those of proliferation
    • Bornfeldt KE, Raines EW, Nakano T, Graves LM, Krebs EG, Ross R: Insulin-like growth factor-1 and platelet-derived growth factor-BB Induce directed migration of human arterial smooth muscle cells via signaling pathways that are distinct from those of proliferation. J Clin Invest 1994, 93:1266-1274.
    • (1994) J Clin Invest , vol.93 , pp. 1266-1274
    • Bornfeldt, K.E.1    Raines, E.W.2    Nakano, T.3    Graves, L.M.4    Krebs, E.G.5    Ross, R.6
  • 9
    • 0028919762 scopus 로고
    • The role of calcium/calmodulin-dependent protein kinase II in the regulation of vascular smooth muscle cell migration
    • Pauly RR, Bilato C, Sollott SJ, Monticone R, Kelly PT, Lakatta EG, Crow MT: The role of calcium/calmodulin-dependent protein kinase II in the regulation of vascular smooth muscle cell migration. Circulation 1995, 91:1107-1115. The authors note the migration of proliferating but not quiescent VSMCs in response to PDGF correlates with the ability to initiate rapid calcium mobilization and activation of calcium- and calmodulin-dependent protein kinase II. Inhibitors of the enzyme, but not those for protein kinase C, inhibit migration of proliferating cells. Conversely calcium ionophores or gene transfer of a mutant-activated kinase II calcium- and calmodulin-dependent protein restores migration to quiescent cells. The paper thus presents convincing evidence for the involvement of this pathway in migration responses.
    • (1995) Circulation , vol.91 , pp. 1107-1115
    • Pauly, R.R.1    Bilato, C.2    Sollott, S.J.3    Monticone, R.4    Kelly, P.T.5    Lakatta, E.G.6    Crow, M.T.7
  • 10
    • 0028810992 scopus 로고
    • Intracellular signaling pathways required for rat vascular smooth muscle cell migration: Interactions between basic fibroblast growth factor and platelet derived growth factor
    • Bilato C, Pauly RR, Melillo G, Monticone R, Gorelick-Feldman D, Gluzband YA, Sollott SJ, Ziman B, Lakatta EG, Crow MT: Intracellular signaling pathways required for rat vascular smooth muscle cell migration: interactions between basic fibroblast growth factor and platelet derived growth factor. J Clin Invest 1995, 96:1905-1915. The authors show that antibodies to bFGF block the migratory response, calcium movements, and calcium- and calmodulin-dependent protein kinase II activation after PDGF treatment. These data amplify the conclusions of Pauly et al. (Circulation 1995, 91:1107-1115) that these intracellular events mediate the migration response and furthermore show that bFGF acts as an essential costimulant in these cells.
    • (1995) J Clin Invest , vol.96 , pp. 1905-1915
    • Bilato, C.1    Pauly, R.R.2    Melillo, G.3    Monticone, R.4    Gorelick-Feldman, D.5    Gluzband, Y.A.6    Sollott, S.J.7    Ziman, B.8    Lakatta, E.G.9    Crow, M.T.10
  • 11
    • 0023214429 scopus 로고
    • The induction of smooth muscle cell proliferation in vitro using an organ culture system
    • Fingerle J, Kraft T: The induction of smooth muscle cell proliferation in vitro using an organ culture system. Int Angiol 1987, 6:65-72.
    • (1987) Int Angiol , vol.6 , pp. 65-72
    • Fingerle, J.1    Kraft, T.2
  • 12
    • 0024566201 scopus 로고
    • Endothelial stimulation of intimal cell proliferation in a porcine aortic organ culture
    • Koo EWY, Gotlieb Al: Endothelial stimulation of intimal cell proliferation in a porcine aortic organ culture. Am J Pathol 1989, 134:497-503.
    • (1989) Am J Pathol , vol.134 , pp. 497-503
    • Koo, E.W.Y.1    Al, G.2
  • 13
    • 0026114354 scopus 로고
    • Smooth muscle cell proliferation in response to injury in an organ culture of human saphenous vein
    • Angelini GD, Soyombo AA, Newby AC: Smooth muscle cell proliferation in response to injury in an organ culture of human saphenous vein. Eur J Vasc Surg 1991, 5:5-12.
    • (1991) Eur J Vasc Surg , vol.5 , pp. 5-12
    • Angelini, G.D.1    Soyombo, A.A.2    Newby, A.C.3
  • 14
    • 85047678849 scopus 로고
    • Surgical preparation induces injury and promotes smooth muscle cell proliferation in a culture of human saphenous vein
    • Soyombo AA, Angelini GD, Bryan AJ, Newby AC: Surgical preparation induces injury and promotes smooth muscle cell proliferation in a culture of human saphenous vein. Cardiovasc Res 1993, 27:1961-1967.
    • (1993) Cardiovasc Res , vol.27 , pp. 1961-1967
    • Soyombo, A.A.1    Angelini, G.D.2    Bryan, A.J.3    Newby, A.C.4
  • 15
    • 0025203810 scopus 로고
    • Intimal lesion formation in rat carotid arteries after endothelial denudation in absence of medial injury
    • Fingerle J, Tina Au YP, Clowes AW, Reidy MA: Intimal lesion formation in rat carotid arteries after endothelial denudation in absence of medial injury. Arteriosclerosis 1990,10:1082-1087.
    • (1990) Arteriosclerosis , vol.10 , pp. 1082-1087
    • Fingerle, J.1    Tina Au, Y.P.2    Clowes, A.W.3    Reidy, M.A.4
  • 16
    • 0023713505 scopus 로고
    • Diverse effects of fibronectin and laminin on phenotypic properties of cultured smooth muscle cells
    • Hedin U, Bottger BA, Forsberg E, Johansson S, Thyberg J: Diverse effects of fibronectin and laminin on phenotypic properties of cultured smooth muscle cells. J Cell Biol 1988,107:307-319.
    • (1988) J Cell Biol , vol.107 , pp. 307-319
    • Hedin, U.1    Bottger, B.A.2    Forsberg, E.3    Johansson, S.4    Thyberg, J.5
  • 17
    • 0022559203 scopus 로고
    • Endothelial cell influences on vascular smooth muscle phenotype
    • Campbell JH, Campbell GR: Endothelial cell influences on vascular smooth muscle phenotype. Ann Rev Physiol 1986,48:295-306.
    • (1986) Ann Rev Physiol , vol.48 , pp. 295-306
    • Campbell, J.H.1    Campbell, G.R.2
  • 18
    • 0026497647 scopus 로고
    • Involvement of extracellular-matrix-degrading metalloproteinases in rabbit aortic smooth-muscle cell proliferation
    • Southgate KM, Davies M, Booth RFG, Newby AC: Involvement of extracellular-matrix-degrading metalloproteinases in rabbit aortic smooth-muscle cell proliferation. Biochem J 1992, 288:93-99.
    • (1992) Biochem J , vol.288 , pp. 93-99
    • Southgate, K.M.1    Davies, M.2    Booth, R.F.G.3    Newby, A.C.4
  • 20
    • 0028137599 scopus 로고
    • Inhibition of neointimal hyperplasia by blocking avb3 integrln with a small peptide antagonist GpenGRGDSPCA*
    • Choi ET, Engel L, Callow AD, Sun S, Trachtenberg J, Santoro S, Ryan US: Inhibition of neointimal hyperplasia by blocking avb3 integrln with a small peptide antagonist GpenGRGDSPCA*. J Vasc Surg 1994, 19:125-134.
    • (1994) J Vasc Surg , vol.19 , pp. 125-134
    • Choi, E.T.1    Engel, L.2    Callow, A.D.3    Sun, S.4    Trachtenberg, J.5    Santoro, S.6    Ryan, U.S.7
  • 21
    • 0027944516 scopus 로고
    • Inhibition of integrin function by a cyclic RGD-containing peptide prevents neointima formation
    • Matsuno H, Stassen JM, Vermylen J, Deckmyn H: Inhibition of integrin function by a cyclic RGD-containing peptide prevents neointima formation. Circulation 1994, 90:2203-2206.
    • (1994) Circulation , vol.90 , pp. 2203-2206
    • Matsuno, H.1    Stassen, J.M.2    Vermylen, J.3    Deckmyn, H.4
  • 25
    • 0027454144 scopus 로고
    • Thrombospondin mediates migration and potentiates platelet-derived growth factor-dependent migration of calf pulmonary artery smooth muscle cells
    • Yabkowitz R, Mansfield PJ, Ryan US, Suchard SJ: Thrombospondin mediates migration and potentiates platelet-derived growth factor-dependent migration of calf pulmonary artery smooth muscle cells. J Cell Physiol 1993, 157:24-32.
    • (1993) J Cell Physiol , vol.157 , pp. 24-32
    • Yabkowitz, R.1    Mansfield, P.J.2    Ryan, U.S.3    Suchard, S.J.4
  • 26
    • 0028969562 scopus 로고
    • Binding of platelet-derived growth factor and low density lipoproteins to glycosaminoglycan species produced by human arterial smooth muscle cells
    • Fager G, Camejo G, Olsson U, Östergren-Lundén G, Lustig F, Bondjers G: Binding of platelet-derived growth factor and low density lipoproteins to glycosaminoglycan species produced by human arterial smooth muscle cells. J Cell Physiol 1995,163:380-392.
    • (1995) J Cell Physiol , vol.163 , pp. 380-392
    • Fager, G.1    Camejo, G.2    Olsson, U.3    Östergren-Lundén, G.4    Lustig, F.5    Bondjers, G.6
  • 27
    • 0028920533 scopus 로고
    • Neointimal fibrosis in vascular pathologies: Role of growth factors and metalloproteinases in vascular smooth muscle proliferation
    • Newby AC, Fabunmi RP, George SJ, Southgate KM, Banning AP, Thurston VJ, Williams A: Neointimal fibrosis in vascular pathologies: role of growth factors and metalloproteinases in vascular smooth muscle proliferation. Exp Nephrol 1995, 3:108-113.
    • (1995) Exp Nephrol , vol.3 , pp. 108-113
    • Newby, A.C.1    Fabunmi, R.P.2    George, S.J.3    Southgate, K.M.4    Banning, A.P.5    Thurston, V.J.6    Williams, A.7
  • 28
    • 0028792509 scopus 로고
    • Matrix metalloproteinases and cardiovascular disease
    • Dollery CM, McEwan JR, Henney AM: Matrix metalloproteinases and cardiovascular disease. Circ Res 1995, 77:863-868.
    • (1995) Circ Res , vol.77 , pp. 863-868
    • Dollery, C.M.1    McEwan, J.R.2    Henney, A.M.3
  • 29
    • 0025786614 scopus 로고
    • Production of tissue collagenase (matrix metalloproteinase 1) by human aortic smooth muscle cells in response to platelet-derived growth factor
    • Yanagi H, Sasaguri Y, Sugama K, Monmatsu M, Nagase H: Production of tissue collagenase (matrix metalloproteinase 1) by human aortic smooth muscle cells in response to platelet-derived growth factor. Atherosclerosis 1992, 91:207-216.
    • (1992) Atherosclerosis , vol.91 , pp. 207-216
    • Yanagi, H.1    Sasaguri, Y.2    Sugama, K.3    Monmatsu, M.4    Nagase, H.5
  • 30
    • 0028146228 scopus 로고
    • Smooth muscle cell migration and matrix metalloproteinase expression after arterial injury in the rat
    • Bendeck MP, Zempo N, Clowes AW, Galardy RE, Reidy MA: Smooth muscle cell migration and matrix metalloproteinase expression after arterial injury in the rat Circ Res 1994, 75:539-545.
    • (1994) Circ Res , vol.75 , pp. 539-545
    • Bendeck, M.P.1    Zempo, N.2    Clowes, A.W.3    Galardy, R.E.4    Reidy, M.A.5
  • 31
    • 0030064282 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury
    • Bendeck MP, Irvin C, Reidy MA: Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury. Circ Res 1996, 78:38-43.
    • (1996) Circ Res , vol.78 , pp. 38-43
    • Bendeck, M.P.1    Irvin, C.2    Reidy, M.A.3
  • 32
  • 33
    • 0030026574 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell migration and proliferation in vitro and injured rat arteries by a synthetic matrix metalloproteinase inhibitor
    • Zempo N, Koyama N, Kenagy RD, Lea MJ, Clowes AW: Regulation of vascular smooth muscle cell migration and proliferation in vitro and injured rat arteries by a synthetic matrix metalloproteinase inhibitor. Arterioscler Thromb Vasc Biol 1996, 16:28-33.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , pp. 28-33
    • Zempo, N.1    Koyama, N.2    Kenagy, R.D.3    Lea, M.J.4    Clowes, A.W.5
  • 34
    • 0029129597 scopus 로고
    • Microscopic localization of active proteases by in situ zymography: Detection of matrix metalloproteinase activity in vascular tissue
    • Galis ZS, Sukhova GK, Libby P: Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue. FASEB J 1995, 9:974-980.
    • (1995) FASEB J , vol.9 , pp. 974-980
    • Galis, Z.S.1    Sukhova, G.K.2    Libby, P.3
  • 35
    • 0029862599 scopus 로고    scopus 로고
    • Divergent regulation by growth factors and cytokines of 95 kDa and 72 kDa gelatinases and tissue inhibitors of metalloproteinases-1, -2 and -3 in rabbit aortic smooth muscle cells
    • Fabunmi RP, Baker AH, Murray EJ, Booth RFG, Newby AC: Divergent regulation by growth factors and cytokines of 95 kDa and 72 kDa gelatinases and tissue inhibitors of metalloproteinases-1, -2 and -3 in rabbit aortic smooth muscle cells. Biochem J 1996, 315:335-342. Stimulation of MMP-9 expression is shown to require synergistic interaction of PDGF and interleukin-1. This implies that a combination of injury, which causes PDGF production, and an inflammatory response leading to interleukin-1 production is the optimum stimulus for basement membrane degradation. By contrast, TIMP-I and -2 activity are not affected by these agents and TIMP-3 secretion is elevated by combinations of PDGF and TGF-β.
    • (1996) Biochem J , vol.315 , pp. 335-342
    • Fabunmi, R.P.1    Baker, A.H.2    Murray, E.J.3    Booth, R.F.G.4    Newby, A.C.5
  • 36
    • 0030091939 scopus 로고    scopus 로고
    • Expression of collagen, interstitial collagenase, and tissue inhibitor of metalloproteinase-1 in restenosis after carotid endarterectomy
    • Nikkari ST, Geary RL, Hatsukami T, Ferguson M, Forough R, Allpers CE, Clowes AW: Expression of collagen, interstitial collagenase, and tissue inhibitor of metalloproteinase-1 in restenosis after carotid endarterectomy. Am J Pathol 1996, 148:777-783.
    • (1996) Am J Pathol , vol.148 , pp. 777-783
    • Nikkari, S.T.1    Geary, R.L.2    Hatsukami, T.3    Ferguson, M.4    Forough, R.5    Allpers, C.E.6    Clowes, A.W.7
  • 37
    • 0028063408 scopus 로고
    • Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques
    • Galis ZS, Sukhova GK, Lark MW, Libby P: Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J Clin Invest 1994, 94:2493-2503.
    • (1994) J Clin Invest , vol.94 , pp. 2493-2503
    • Galis, Z.S.1    Sukhova, G.K.2    Lark, M.W.3    Libby, P.4
  • 39
    • 0029115532 scopus 로고
    • Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms-An elastolytic metalloproteinase expressed by aneurysm-inflltrating macrophages
    • Thompson RW, Holmes DR, Mertens RA, Liao SX, Botney MD, Mecham RP, Welgus HG, Parks WC: Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms-An elastolytic metalloproteinase expressed by aneurysm-inflltrating macrophages. J Clin Invest 1995, 96:318-326.
    • (1995) J Clin Invest , vol.96 , pp. 318-326
    • Thompson, R.W.1    Holmes, D.R.2    Mertens, R.A.3    Liao, S.X.4    Botney, M.D.5    Mecham, R.P.6    Welgus, H.G.7    Parks, W.C.8
  • 41
    • 0029080423 scopus 로고
    • In situ localisation and quantification of mRNA for 92-kD type IV collagenase and its inhibitor in aneurysmal, occlusive, and normal aorta
    • McMillan WD, Patterson BK, Keen RR, Shively VP, Cipollone M, Pearce WH: In situ localisation and quantification of mRNA for 92-kD type IV collagenase and its inhibitor in aneurysmal, occlusive, and normal aorta. Arterioscler Thromb Vasc Biol 1995, 15:1139-1144.
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 1139-1144
    • McMillan, W.D.1    Patterson, B.K.2    Keen, R.R.3    Shively, V.P.4    Cipollone, M.5    Pearce, W.H.6
  • 42
    • 0028836794 scopus 로고
    • Macrophage foam cells from experimental atheroma constitutively produce matrix degrading proteinases
    • Galis ZS, Sukhova GK, Kranzhöfer R, Clark S, Libby P: Macrophage foam cells from experimental atheroma constitutively produce matrix degrading proteinases. Proc Natl Acad Sci U S A 1995, 92:402-406. Macrophages isolated from the atherosclerotic plaques of cholesterol-fed rabbits are shown to express MMP-1, -2, -3, and -9. The results are confirmed by immunocytochemistry of arterial segments.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 402-406
    • Galis, Z.S.1    Sukhova, G.K.2    Kranzhöfer, R.3    Clark, S.4    Libby, P.5
  • 43
    • 0029084524 scopus 로고
    • Human monocyte-derived macrophages induce collagen breakdown in fibrous caps of atherosclerotic plaques: Potential role of matrix-degrading metalloproteinases and implications for plaque rupture
    • Shah PK, Falk E, Badimon JJ, Femandezortiz A, Mailhac A, Villareallevy G, Fallen JT, Regnstrom J, Fuster V: Human monocyte-derived macrophages induce collagen breakdown in fibrous caps of atherosclerotic plaques: potential role of matrix-degrading metalloproteinases and implications for plaque rupture. Circulation 1995, 92:1565-1569.
    • (1995) Circulation , vol.92 , pp. 1565-1569
    • Shah, P.K.1    Falk, E.2    Badimon, J.J.3    Femandezortiz, A.4    Mailhac, A.5    Villareallevy, G.6    Fallen, J.T.7    Regnstrom, J.8    Fuster, V.9
  • 44
    • 0025980167 scopus 로고
    • Atherosclerotic plaque caps are locally weakened when macrophage density is increased
    • Lendon CL, Davies MJ, Born GVR, Richardson PD: Atherosclerotic plaque caps are locally weakened when macrophage density is increased. Atherosclerosis 1991, 87:87-91.
    • (1991) Atherosclerosis , vol.87 , pp. 87-91
    • Lendon, C.L.1    Davies, M.J.2    Born, G.V.R.3    Richardson, P.D.4
  • 45
    • 0028906790 scopus 로고
    • Identification of 92-kD gelatinase in human coronary atherosclerotic lesions: Association of active enzyme synthesis with unstable angina
    • Brown DL, Hibbs MS, Kearney M, Loushin C, Isner JM: Identification of 92-kD gelatinase in human coronary atherosclerotic lesions: association of active enzyme synthesis with unstable angina. Circulation 1995, 91:2125-2131.
    • (1995) Circulation , vol.91 , pp. 2125-2131
    • Brown, D.L.1    Hibbs, M.S.2    Kearney, M.3    Loushin, C.4    Isner, J.M.5
  • 50
    • 85047678478 scopus 로고
    • Heparin decreases the rate of proliferation of rat vascular smooth muscle cells by releasing transforming growth factor ß-like activity from serum
    • Grainger DJ, Witchell CM, Watson JV, Metcalfe JC, Weissberg PL: Heparin decreases the rate of proliferation of rat vascular smooth muscle cells by releasing transforming growth factor ß-like activity from serum. Cardiovasc Res 1993, 27:2238-2247.
    • (1993) Cardiovasc Res , vol.27 , pp. 2238-2247
    • Grainger, D.J.1    Witchell, C.M.2    Watson, J.V.3    Metcalfe, J.C.4    Weissberg, P.L.5
  • 51
    • 0027177398 scopus 로고
    • Transforming growth factor-beta inhibits human vascular smooth muscle cell growth and migration
    • Mii S, Ware JA, Kent KC: Transforming growth factor-beta inhibits human vascular smooth muscle cell growth and migration. Surgery 1993, 114:464-470.
    • (1993) Surgery , vol.114 , pp. 464-470
    • Mii, S.1    Ware, J.A.2    Kent, K.C.3
  • 52
    • 0028859484 scopus 로고
    • Decreased type II/type I TGF-β receptor ratio in cells derived from human atherosclerotic lesions. Conversion from an antiproliferative to profibrotic response to TGF-β
    • McCaffrey TA, Consigli S, Du B, Falcone DJ, Sanborn TA, Spokojny AM, Bush HL: Decreased type II/type I TGF-β receptor ratio In cells derived from human atherosclerotic lesions. Conversion from an antiproliferative to profibrotic response to TGF-β. J Clin Invest 1995, 96:2667-2675. The VSMCs from human vascular lesions are shown to be lacking in the type II TGF-β receptor and in inhibitory growth responses to TGF-β. Gene transfer of the type II receptor into lesion cells restores inhibitory responses. The data imply that lesion VSMCs may have a paradoxically growth stimulatory response to TGF-β that leads to lesion progression.
    • (1995) J Clin Invest , vol.96 , pp. 2667-2675
    • McCaffrey, T.A.1    Consigli, S.2    Du, B.3    Falcone, D.J.4    Sanborn, T.A.5    Spokojny, A.M.6    Bush, H.L.7
  • 53
    • 0028832493 scopus 로고
    • Vascular smooth muscle cells from injured rat aortas display elevated matrix production associated with transforming growth factor-beta activity
    • Rasmussen LM, Wolf YG, Ruoslahti E: Vascular smooth muscle cells from injured rat aortas display elevated matrix production associated with transforming growth factor-beta activity. Am J Pathol 1995, 147:1041-1048.
    • (1995) Am J Pathol , vol.147 , pp. 1041-1048
    • Rasmussen, L.M.1    Wolf, Y.G.2    Ruoslahti, E.3
  • 54
    • 0026450848 scopus 로고
    • Expression of transforming growth factor-β1 is increased in human vascular restenosis lesions
    • Nikol S, Isner JM, Pickering JG, Keatney M, Leclerc G, Weir L: Expression of transforming growth factor-β1 is increased in human vascular restenosis lesions. J Clin Invest 1992, 90:1582-1592.
    • (1992) J Clin Invest , vol.90 , pp. 1582-1592
    • Nikol, S.1    Isner, J.M.2    Pickering, J.G.3    Keatney, M.4    Leclerc, G.5    Weir, L.6
  • 56
    • 0028230233 scopus 로고
    • Antibodies against transforming growth factor-β1 suppress Intimal hyperplasia in a rat model
    • Wolf YG, Rasmussen LM, Ruoslahti E: Antibodies against transforming growth factor-β1 suppress Intimal hyperplasia in a rat model. J Clin Invest 1994, 93:1172-1178.
    • (1994) J Clin Invest , vol.93 , pp. 1172-1178
    • Wolf, Y.G.1    Rasmussen, L.M.2    Ruoslahti, E.3
  • 57
  • 59
    • 0028918825 scopus 로고
    • The serum concentration of active transforming growth factor-β is severely depressed in advanced atherosclerosis
    • Grainger DJ, Kemp PR, Metcalfe JC, Liu AC, Lawn RM, Williams NR, Grace AA, Schofield PM, Chauhan A: The serum concentration of active transforming growth factor-β is severely depressed in advanced atherosclerosis. Nature Med 1995, 1:74-79. The ratio of active to total TGF-β is shown to be reduced fivefold in men with triple coronary artery disease compared with normal volunteers. The activation of TGF-β correlates inversely with PAI-1 and lipoprotein(a) levels, implying that a failure of plasmin to activate TGF-β may be a common mode of action for these atherogenic risk factors.
    • (1995) Nature Med , vol.1 , pp. 74-79
    • Grainger, D.J.1    Kemp, P.R.2    Metcalfe, J.C.3    Liu, A.C.4    Lawn, R.M.5    Williams, N.R.6    Grace, A.A.7    Schofield, P.M.8    Chauhan, A.9
  • 60
    • 0027989926 scopus 로고
    • Activation of transforming growth factor-beta is inhibited in transgenic apoliprotein(a) mice
    • Grainger DJ, Kemp PR, Liu AC, Lawn RM, Metcalfe JC: Activation of transforming growth factor-beta is inhibited in transgenic apoliprotein(a) mice. Nature 1994, 370:460-462.
    • (1994) Nature , vol.370 , pp. 460-462
    • Grainger, D.J.1    Kemp, P.R.2    Liu, A.C.3    Lawn, R.M.4    Metcalfe, J.C.5
  • 61
    • 0030039268 scopus 로고    scopus 로고
    • Serum levels of the TGF-beta receptor are increased in atherosclerosis
    • Blann AD, Wang JM, Wilson PB, Kumar S: Serum levels of the TGF-beta receptor are increased in atherosclerosis. Atherosclerosis 1996, 120:221-226.
    • (1996) Atherosclerosis , vol.120 , pp. 221-226
    • Blann, A.D.1    Wang, J.M.2    Wilson, P.B.3    Kumar, S.4
  • 62
    • 0027184395 scopus 로고
    • Tamoxifen decreases the rate of proliferation of vascular smooth muscle cells in culture by inducing production of transforming growth factor-β
    • Grainger DJ, Weissberg PL, Metcalfe JC: Tamoxifen decreases the rate of proliferation of vascular smooth muscle cells in culture by inducing production of transforming growth factor-β. Biochem J 1993, 294:109-112.
    • (1993) Biochem J , vol.294 , pp. 109-112
    • Grainger, D.J.1    Weissberg, P.L.2    Metcalfe, J.C.3
  • 63
    • 0024802762 scopus 로고
    • Morphometric analysis of the composition of atherosclerotic plaques in the four major epicardial coronary arteries in acute myocardial infarction and in sudden coronary death
    • Kragel AH, Reddy SG, Wittes JT, Roberts WC: Morphometric analysis of the composition of atherosclerotic plaques In the four major epicardial coronary arteries in acute myocardial infarction and in sudden coronary death. Circulation 1989, 80:1747-1756.
    • (1989) Circulation , vol.80 , pp. 1747-1756
    • Kragel, A.H.1    Reddy, S.G.2    Wittes, J.T.3    Roberts, W.C.4
  • 64
    • 0026454560 scopus 로고
    • Comparison of the composition of atherosclerotic plaques in saphenous veins used as aortocoronary bypass grafts with plaques in native coronary arteries in the same men
    • Mautner SL, Mautner GC, Hunsberger SA, Roberts WC: Comparison of the composition of atherosclerotic plaques In saphenous veins used as aortocoronary bypass grafts with plaques in native coronary arteries in the same men. Am J Cardiol 1992, 70:1380-1387.
    • (1992) Am J Cardiol , vol.70 , pp. 1380-1387
    • Mautner, S.L.1    Mautner, G.C.2    Hunsberger, S.A.3    Roberts, W.C.4
  • 65
    • 0028158099 scopus 로고
    • Deregulated expression of the c-myc oncogene abolishes inhibition of proliferation of rat vascular smooth muscle cells by serum reduction, interferon-γ, heparin and cyclic nucleotide analogues and induces apoptosis
    • Bennett MR, Evan GI, Newby AC: Deregulated expression of the c-myc oncogene abolishes inhibition of proliferation of rat vascular smooth muscle cells by serum reduction, interferon-γ, heparin and cyclic nucleotide analogues and induces apoptosis. Circ Res 1994, 74:525-536.
    • (1994) Circ Res , vol.74 , pp. 525-536
    • Bennett, M.R.1    Evan, G.I.2    Newby, A.C.3
  • 66
    • 0028954468 scopus 로고
    • Apoptosis (programmed cell death) in arteries of the neonatal lamb
    • Cho A, Courtman DW, Langille BL: Apoptosis (programmed cell death) In arteries of the neonatal lamb. Circ Res 1995, 76:168-175.
    • (1995) Circ Res , vol.76 , pp. 168-175
    • Cho, A.1    Courtman, D.W.2    Langille, B.L.3
  • 67
    • 0028903234 scopus 로고
    • Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques
    • Bennett MR, Evan GI, Scwartz SM: Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques. J Clin Invest 1995, 95:2266-2274. Plaque-derived VSMCs show higher rates of apoptosis than cells derived from normal tissues, especially under serum-free conditions. Addition of PFGF and IGF-1 is shown to reduce rates of apoptosis, suggesting that they act as survival cytokines in vivo. Gene transfer of the bcl-2 gene into plaque VSMCs partially restores the low rate of apoptosis in normal VSMCs. However, bcl-2 is not detectable in either normal or plaque cells, implying that other pathways may normally prevent apoptosis in these cells. Nevertheless, the possibility of gene therapy with bcl-2 is still valid.
    • (1995) J Clin Invest , vol.95 , pp. 2266-2274
    • Bennett, M.R.1    Evan, G.I.2    Scwartz, S.M.3
  • 69
    • 0029115152 scopus 로고
    • Evidence for apoptosis in advanced human atheroma. Çolocalization with interleukin-1β-converting enzyme
    • Geng Y-J, Libby P: Evidence for apoptosis in advanced human atheroma. Çolocalization with interleukin-1β-converting enzyme. Am J Pathol 1995, 147:251-266. The authors used DNA end-labelling to detect fragmentation in carotid and coronary plaques as an indicator of apoptosis. In normal media, 4% of cells stain positive compared with 30% in plaque cap VSMCs and (focally) up to 50% in foam cells abutting the lipid core. Colocalization with second marker of apoptosis, interleukin-1 converting enzyme, provides support for the idea that these very high apoptotic rates (which nevertheless remain a puzzle given plaque stability) can be measured in years.
    • (1995) Am J Pathol , vol.147 , pp. 251-266
    • Geng, Y.-J.1    Libby, P.2
  • 70
    • 0029113373 scopus 로고
    • Evidence for apoptosis in human atherogenesis and in a rat vascular injury model
    • Han DK, Haudenschild CC, Hong MK, Tinkle BT, Leon MB, Liau G: Evidence for apoptosis in human atherogenesis and in a rat vascular injury model. Am J Pathol 1995, 147:267-277.-Similar findings as as Geng and Libby (Am J Pathol 1995, 147:251-266), together with data from balloon-injured rat iliac arteries. Provocative data show very high apoptotic rates (up to 50% on day 9 following balloon injury) that appear to imply an excess of cell death over proliferation at a time when the intima is still expanding.
    • (1995) Am J Pathol , vol.147 , pp. 267-277
    • Han, D.K.1    Haudenschild, C.C.2    Hong, M.K.3    Tinkle, B.T.4    Leon, M.B.5    Liau, G.6
  • 71
    • 0030034534 scopus 로고    scopus 로고
    • Distribution of cell replication and apoptosis in atherosclerotic plaques of cholesterol-fed rabbits
    • Kockx MM, De Meyer GRY, Muhring J, Bult H, Bultinck J, Herman AG: Distribution of cell replication and apoptosis in atherosclerotic plaques of cholesterol-fed rabbits. Atherosclerosis 1996, 120:115-124. Demonstrates low but detectable rates of apoptosis in the media and intima of cholesterol-fed rabbits. Apoptosis rates are much lower than proliferation rates, implying that apoptosis has a relatively minor effect on neointima formation.
    • (1996) Atherosclerosis , vol.120 , pp. 115-124
    • Kockx, M.M.1    De Meyer, G.R.Y.2    Muhring, J.3    Bult, H.4    Bultinck, J.5    Herman, A.G.6
  • 72
    • 0028997321 scopus 로고
    • Apoptosis participates in cellularity regulation during rat aortic intimal thickening
    • Bochaton-Piallat ML, Gabbiani F, Redard M, Desmouliere A, Gabbiani G: Apoptosis participates in cellularity regulation during rat aortic intimal thickening. Am J Pathol 1995, 146:1059-1064. In situ end-labeling is used to measure apoptotic rates in a rat aortic balloon injury model. High rates are confined to the most intimal cell layers and peak at 15 days, a time when lesion area may be declining.
    • (1995) Am J Pathol , vol.146 , pp. 1059-1064
    • Bochaton-Piallat, M.L.1    Gabbiani, F.2    Redard, M.3    Desmouliere, A.4    Gabbiani, G.5
  • 73
  • 74
    • 0029998236 scopus 로고    scopus 로고
    • Biotin- Or digoxigenin-conjugated nucleotides bind to matrix vesicles in atherosclerotic plaques
    • Kockx MM, Muhring J, Bortier H, De Meyer GRY, Jacob W: Biotin- or digoxigenin-conjugated nucleotides bind to matrix vesicles in atherosclerotic plaques. Am J Pathol 1996, 148:1771-1777.
    • (1996) Am J Pathol , vol.148 , pp. 1771-1777
    • Kockx, M.M.1    Muhring, J.2    Bortier, H.3    De Meyer, G.R.Y.4    Jacob, W.5
  • 75
    • 0030048396 scopus 로고    scopus 로고
    • Apoptosis of vascular smooth muscle cells induced by in vitro stimulation with interferon-γ, tumor necrosis factor-α, and interleukin-1β
    • Geng Y-J, Wu Q, Muszynski M, Hansson GK, Libby P: Apoptosis of vascular smooth muscle cells induced by in vitro stimulation with interferon-γ, tumor necrosis factor-α, and interleukin-1β. Arteriorscler Thromb Vasc Biol 1996, 16:19-27. Combinations of interferon gamma with interleukin-1 or TNF-α stimulate apoptosis of human and rat VSMCs, in part via a nitric oxide-dependent pathway.
    • (1996) Arteriorscler Thromb Vasc Biol , vol.16 , pp. 19-27
    • Geng, Y.-J.1    Wu, Q.2    Muszynski, M.3    Hansson, G.K.4    Libby, P.5
  • 76
    • 0029081551 scopus 로고
    • Apoptosis of rat vascular smooth muscle cells is regulated by p53-dependent and -independent pathways
    • Bennett MR, Evan GI, Schwartz SM: Apoptosis of rat vascular smooth muscle cells is regulated by p53-dependent and -independent pathways. Circ Res 1995, 77:266-273.
    • (1995) Circ Res , vol.77 , pp. 266-273
    • Bennett, M.R.1    Evan, G.I.2    Schwartz, S.M.3
  • 77
    • 0028821783 scopus 로고
    • Consequences of p53 gene expression by adenovirus vector on cell cycle arrest and apoptosis in human aortic vascular smooth muscle cells
    • Katayose D, Wersto R, Cowan K, Seth P: Consequences of p53 gene expression by adenovirus vector on cell cycle arrest and apoptosis in human aortic vascular smooth muscle cells. Biochem Biophys Res Commun 1995, 215:446-451.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 446-451
    • Katayose, D.1    Wersto, R.2    Cowan, K.3    Seth, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.