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Volumn 54, Issue 7, 2005, Pages 2227-2234

Signaling pathways involved in human vascular smooth muscle cell proliferation and matrix metalloproteinase-2 expression induced by leptin: Inhibitory effect of metformin

Author keywords

[No Author keywords available]

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ALPHA TOCOPHEROL; APOCYNIN; BAY 117085; DIPHENYLIODONIUM SALT; GELATINASE A; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; METFORMIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; RECOMBINANT LEPTIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; THENOYLTRIFLUOROACETONE; UNCLASSIFIED DRUG;

EID: 21344456357     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.54.7.2227     Document Type: Article
Times cited : (182)

References (62)
  • 1
    • 0033824123 scopus 로고    scopus 로고
    • Obesity and cardiovascular disease: Pathogenic role of the metabolic syndrome and therapeutic implications
    • Abate N: Obesity and cardiovascular disease: pathogenic role of the metabolic syndrome and therapeutic implications. J Diabetes Complications 14:154-174, 2000
    • (2000) J Diabetes Complications , vol.14 , pp. 154-174
    • Abate, N.1
  • 4
    • 10744232583 scopus 로고    scopus 로고
    • Fasting plasma leptin, tumor necrosis factor-α receptor 2, and monocyte chemoattracting protein 1 concentration in a population of glucose-tolerant and glucose-intolerant women: Impact on cardiovascular mortality
    • Piemonti L, Calori G, Mercalli A, Lattuada G, Monti P, Garancini MP, Costantino F, Ruotolo G, Luzi L, Perseghin G: Fasting plasma leptin, tumor necrosis factor-α receptor 2, and monocyte chemoattracting protein 1 concentration in a population of glucose-tolerant and glucose-intolerant women: impact on cardiovascular mortality. Diabetes Care 26:2883-2889, 2003
    • (2003) Diabetes Care , vol.26 , pp. 2883-2889
    • Piemonti, L.1    Calori, G.2    Mercalli, A.3    Lattuada, G.4    Monti, P.5    Garancini, M.P.6    Costantino, F.7    Ruotolo, G.8    Luzi, L.9    Perseghin, G.10
  • 5
    • 0035816639 scopus 로고    scopus 로고
    • Leptin induces mitochondrial superoxide production and monocyte chemoattractant protein-1 expression in aortic endothelial cells by increasing fatty acid oxidation via protein kinase A
    • Yamagishi SI, Edelstein D, Du XL, Kaneda Y, Guzman M, Brownlee M: Leptin induces mitochondrial superoxide production and monocyte chemoattractant protein-1 expression in aortic endothelial cells by increasing fatty acid oxidation via protein kinase A. J Biol Chem 276:25096-25100, 2001
    • (2001) J Biol Chem , vol.276 , pp. 25096-25100
    • Yamagishi, S.I.1    Edelstein, D.2    Du, X.L.3    Kaneda, Y.4    Guzman, M.5    Brownlee, M.6
  • 6
    • 0035973147 scopus 로고    scopus 로고
    • Potential role of leptin in angiogenesis: Leptin induces endothelial cell proliferation and expression of matrix metalloproteinases in vivo and in vitro
    • Park HY, Kwon HM, Lim HJ, Hong BK, Lee JY, Park BE, Jang Y, Cho SY, Kim HS: Potential role of leptin in angiogenesis: leptin induces endothelial cell proliferation and expression of matrix metalloproteinases in vivo and in vitro. Exp Mol Med 33:95-102, 2001
    • (2001) Exp Mol Med , vol.33 , pp. 95-102
    • Park, H.Y.1    Kwon, H.M.2    Lim, H.J.3    Hong, B.K.4    Lee, J.Y.5    Park, B.E.6    Jang, Y.7    Cho, S.Y.8    Kim, H.S.9
  • 7
    • 0035206659 scopus 로고    scopus 로고
    • Leptin stimulates rat aortic smooth muscle cell proliferation and migration
    • Oda A, Taniguchi T, Yokoyama M: Leptin stimulates rat aortic smooth muscle cell proliferation and migration. Kobe J Med Sci 47:141-150, 2001
    • (2001) Kobe J Med Sci , vol.47 , pp. 141-150
    • Oda, A.1    Taniguchi, T.2    Yokoyama, M.3
  • 8
    • 0035844031 scopus 로고    scopus 로고
    • Leptin enhances the calcification of vascular cells: Artery wall as a target of leptin
    • Parhami F, Tintut Y, Ballard A, Fogelman AM, Demer LL: Leptin enhances the calcification of vascular cells: artery wall as a target of leptin. Circ Res 88:954-960, 2001
    • (2001) Circ Res , vol.88 , pp. 954-960
    • Parhami, F.1    Tintut, Y.2    Ballard, A.3    Fogelman, A.M.4    Demer, L.L.5
  • 9
    • 0032971218 scopus 로고    scopus 로고
    • Leptin promotes aggregation of human platelets via the long form of its receptor
    • Nakata M, Yada T, Soejima N, Maruyama I: Leptin promotes aggregation of human platelets via the long form of its receptor. Diabetes 48:426-429, 1999
    • (1999) Diabetes , vol.48 , pp. 426-429
    • Nakata, M.1    Yada, T.2    Soejima, N.3    Maruyama, I.4
  • 10
    • 0033602850 scopus 로고    scopus 로고
    • Human leptin stimulates proliferation and activation of human circulating monocytes
    • Santos-Alvarez J, Goberna R, Sanchez-Margalet V: Human leptin stimulates proliferation and activation of human circulating monocytes. Cell Immunol 194:6-11, 1999
    • (1999) Cell Immunol , vol.194 , pp. 6-11
    • Santos-Alvarez, J.1    Goberna, R.2    Sanchez-Margalet, V.3
  • 11
    • 0035195887 scopus 로고    scopus 로고
    • Leptin regulation of the immune response and the immunodeficiency of malnutrition
    • Faggioni R, Feingold KR, Grunfeld C: Leptin regulation of the immune response and the immunodeficiency of malnutrition. FASEB J 15:2565-2571, 2001
    • (2001) FASEB J , vol.15 , pp. 2565-2571
    • Faggioni, R.1    Feingold, K.R.2    Grunfeld, C.3
  • 12
    • 0032572722 scopus 로고    scopus 로고
    • Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression
    • Lord GM, Matarese G, Howard JK, Baker RJ, Bloom SR, Lechler RI: Leptin modulates the T-cell immune response and reverses starvation-induced immunosuppression. Nature 394:897-901, 1998
    • (1998) Nature , vol.394 , pp. 897-901
    • Lord, G.M.1    Matarese, G.2    Howard, J.K.3    Baker, R.J.4    Bloom, S.R.5    Lechler, R.I.6
  • 14
    • 0017737576 scopus 로고
    • Dissociation of obesity, hypercholesterolemia, and diabetes from atherosclerosis in ob/ob mice
    • Yen TT, Allan JA, Pearson DV, Schinitsky MR: Dissociation of obesity, hypercholesterolemia, and diabetes from atherosclerosis in ob/ob mice. Experientia 33:995-996, 1977
    • (1977) Experientia , vol.33 , pp. 995-996
    • Yen, T.T.1    Allan, J.A.2    Pearson, D.V.3    Schinitsky, M.R.4
  • 16
    • 0032511566 scopus 로고    scopus 로고
    • Effect of intensive blood glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34)
    • UK Prospective Diabetes Study (UKPDS) Group: Effect of intensive blood glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34). Lancet 352:854-865, 1998
    • (1998) Lancet , vol.352 , pp. 854-865
  • 17
    • 0032985166 scopus 로고    scopus 로고
    • A risk-benefit assessment of metformin in type 2 diabetes mellitus
    • Howlett HCS, Bailey CJ: A risk-benefit assessment of metformin in type 2 diabetes mellitus. Drug Sci 20:489-503, 1999
    • (1999) Drug Sci , vol.20 , pp. 489-503
    • Howlett, H.C.S.1    Bailey, C.J.2
  • 18
    • 0034086934 scopus 로고    scopus 로고
    • Metformin: Intrinsic vasculoprotective properties
    • Wiensperger NF: Metformin: intrinsic vasculoprotective properties. Diabetes Tech Therap 2:259-272, 2000
    • (2000) Diabetes Tech Therap , vol.2 , pp. 259-272
    • Wiensperger, N.F.1
  • 19
    • 0042878553 scopus 로고    scopus 로고
    • Metformin inhibits monocyte adhesion to endothelial cells and foam cell formation
    • Mamputu JC, Wiernsperger N, Renier G: Metformin inhibits monocyte adhesion to endothelial cells and foam cell formation. Br J Diabetes Vasc Dis 3:302-310, 2003
    • (2003) Br J Diabetes Vasc Dis , vol.3 , pp. 302-310
    • Mamputu, J.C.1    Wiernsperger, N.2    Renier, G.3
  • 20
    • 0036841861 scopus 로고    scopus 로고
    • NAD(P)H oxidase inhibition improves endothelial function in rat and human blood vessels
    • Hamilton CA, Brosnan MJ, Al-Benna S, Berg G, Dominiczak AF: NAD(P)H oxidase inhibition improves endothelial function in rat and human blood vessels. Hypertension 40:755-762, 2002
    • (2002) Hypertension , vol.40 , pp. 755-762
    • Hamilton, C.A.1    Brosnan, M.J.2    Al-Benna, S.3    Berg, G.4    Dominiczak, A.F.5
  • 21
    • 0015810429 scopus 로고
    • Mechanism of action of the hypoglycemic agent diphenyleneiodonium
    • Holland PC, Clark MG, Bloxham DP, Lardy HA: Mechanism of action of the hypoglycemic agent diphenyleneiodonium. J Biol Chem 248:6050-6056, 1973
    • (1973) J Biol Chem , vol.248 , pp. 6050-6056
    • Holland, P.C.1    Clark, M.G.2    Bloxham, D.P.3    Lardy, H.A.4
  • 22
    • 0033668399 scopus 로고    scopus 로고
    • Hypoxia-induced alterations in Ca(2+) mobilization in brain microvascular endothelial cells
    • Kimura C, Oike M, Ito Y: Hypoxia-induced alterations in Ca(2+) mobilization in brain microvascular endothelial cells. Am J Physiol Heart Circ Physiol 279:H2310-H2318, 2000
    • (2000) Am J Physiol Heart Circ Physiol , vol.279
    • Kimura, C.1    Oike, M.2    Ito, Y.3
  • 25
    • 0030772376 scopus 로고    scopus 로고
    • Novel inhibitors of cytokine-induced IkappaBalpha phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo
    • Pierce JW, Schoenleber R, Jesmok G, Best J, Moore SA, Collins T, Gerritsen ME: Novel inhibitors of cytokine-induced IkappaBalpha phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo. J Biol Chem 272:21096-21103, 1997
    • (1997) J Biol Chem , vol.272 , pp. 21096-21103
    • Pierce, J.W.1    Schoenleber, R.2    Jesmok, G.3    Best, J.4    Moore, S.A.5    Collins, T.6    Gerritsen, M.E.7
  • 26
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2- yl)-2,5-diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction
    • Berridge MV, Tan AS: Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction. Arch Biochem Biophys 303:474-482, 1993
    • (1993) Arch Biochem Biophys , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 27
    • 0027723123 scopus 로고
    • A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies
    • Fujimoto N, Mouri N, Iwata K, Ohuchi E, Okada Y, Hayakawa T: A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies. Clin Chim Acta 221:91-103, 1993
    • (1993) Clin Chim Acta , vol.221 , pp. 91-103
    • Fujimoto, N.1    Mouri, N.2    Iwata, K.3    Ohuchi, E.4    Okada, Y.5    Hayakawa, T.6
  • 28
    • 0025804191 scopus 로고
    • A monoclonal antibody to the phosphorylated form of glial fibrillary acidic protein: Application to a non-radioactive method for measuring protein kinase activities
    • Yano T, Taura C, Shibata M, Hirono Y, Ando S, Kusubata M, Takahashi T, Inagaki M: A monoclonal antibody to the phosphorylated form of glial fibrillary acidic protein: application to a non-radioactive method for measuring protein kinase activities. Biochem. Biophys Res Commun 175:1144-1151, 1991
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 1144-1151
    • Yano, T.1    Taura, C.2    Shibata, M.3    Hirono, Y.4    Ando, S.5    Kusubata, M.6    Takahashi, T.7    Inagaki, M.8
  • 29
    • 0034664960 scopus 로고    scopus 로고
    • A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element- binding protein
    • Versteeg HH, Nyhuis E, van den Brink GR, Evertzen M, Pynaert GN, van Deventer SJ, Coffer PJ, Peppelenbosch MP: A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element-binding protein. Biochem J 350:717-722, 2000
    • (2000) Biochem J , vol.350 , pp. 717-722
    • Versteeg, H.H.1    Nyhuis, E.2    Van Den Brink, G.R.3    Evertzen, M.4    Pynaert, G.N.5    Van Deventer, S.J.6    Coffer, P.J.7    Peppelenbosch, M.P.8
  • 31
    • 18144447850 scopus 로고    scopus 로고
    • Antiatherogenic properties of metformin: The experimental evidence
    • Mamputu JC, Wiernsperger NF, Renier G: Antiatherogenic properties of metformin: the experimental evidence. Diabetes Metab 29:71-76, 2003
    • (2003) Diabetes Metab , vol.29 , pp. 71-76
    • Mamputu, J.C.1    Wiernsperger, N.F.2    Renier, G.3
  • 32
    • 0020639876 scopus 로고
    • Metformin action on lipid metabolism in lesions of experimental aortic atherosclerosis of rabbits
    • Marquié G: Metformin action on lipid metabolism in lesions of experimental aortic atherosclerosis of rabbits. Atherosclerosis 47:7-17, 1983
    • (1983) Atherosclerosis , vol.47 , pp. 7-17
    • Marquié, G.1
  • 33
    • 0018739904 scopus 로고
    • Comparative effects of metformin and phenformin on the progression and regression of cholesterol induced atherosclerosis in rabbits
    • Marquié G: Comparative effects of metformin and phenformin on the progression and regression of cholesterol induced atherosclerosis in rabbits. Paroi Arterielle 5:209-218, 1973
    • (1973) Paroi Arterielle , vol.5 , pp. 209-218
    • Marquié, G.1
  • 34
    • 0343730957 scopus 로고
    • Metformin inhibits the growth of human vascular cells: A new potentially antiatherogenic drug effect
    • Bunting CE, Koschinsky T, Rütter R, Gries FA: Metformin inhibits the growth of human vascular cells: a new potentially antiatherogenic drug effect (Abstract). Diabetologia 29:523A, 1986
    • (1986) Diabetologia , vol.29
    • Bunting, C.E.1    Koschinsky, T.2    Rütter, R.3    Gries, F.A.4
  • 35
    • 21344450854 scopus 로고
    • Experimental studies on the antiatherosclerotic effect of metformin
    • Carlson LA, Paoletti R, Sirtori CR, Weber G, Eds. New York, Raven Press
    • Weber G, Catapano A, Ghiselli G, Sirtori CR: Experimental studies on the antiatherosclerotic effect of metformin. In Proceedings of the International Conference on Atherosclerosis. Carlson LA, Paoletti R, Sirtori CR, Weber G, Eds. New York, Raven Press, 1978, p. 318-325
    • (1978) Proceedings of the International Conference on Atherosclerosis , pp. 318-325
    • Weber, G.1    Catapano, A.2    Ghiselli, G.3    Sirtori, C.R.4
  • 38
    • 0042696057 scopus 로고    scopus 로고
    • Leptin decreases plasma paraoxonase 1 (PON 1) activity and induces oxidative stress: The possible novel mechanism for proatherogenic effect of chronic hyperleptinemia
    • Beltowski J, Wojccicka G, Jamroz A: Leptin decreases plasma paraoxonase 1 (PON 1) activity and induces oxidative stress: the possible novel mechanism for proatherogenic effect of chronic hyperleptinemia. Atherosclerosis 170:21-29, 2003
    • (2003) Atherosclerosis , vol.170 , pp. 21-29
    • Beltowski, J.1    Wojccicka, G.2    Jamroz, A.3
  • 39
    • 0032999682 scopus 로고    scopus 로고
    • Leptin induces oxidative stress in human endothelial cells
    • Bouloumie A, Marumo T, Lafontan M, Busse R: Leptin induces oxidative stress in human endothelial cells. FASEB J 13:1231-1238, 1999
    • (1999) FASEB J , vol.13 , pp. 1231-1238
    • Bouloumie, A.1    Marumo, T.2    Lafontan, M.3    Busse, R.4
  • 40
    • 0043268732 scopus 로고    scopus 로고
    • Leptin increases lipoprotein lipase secretion by macrophages: Involvement of oxidative stress and protein kinase C
    • Maingrette F, Renier G: Leptin increases lipoprotein lipase secretion by macrophages: involvement of oxidative stress and protein kinase C. Diabetes 52:2121-2128, 2003
    • (2003) Diabetes , vol.52 , pp. 2121-2128
    • Maingrette, F.1    Renier, G.2
  • 41
    • 0037414393 scopus 로고    scopus 로고
    • NAD(P)H oxidase participates in the signaling events in high-glucose-induced proliferation of vascular smooth muscle cells
    • Lee HS, Son SM, Kim YK, Hong KW, Kim CD: NAD(P)H oxidase participates in the signaling events in high-glucose-induced proliferation of vascular smooth muscle cells. Life Sci 72:2719-2730, 2003
    • (2003) Life Sci , vol.72 , pp. 2719-2730
    • Lee, H.S.1    Son, S.M.2    Kim, Y.K.3    Hong, K.W.4    Kim, C.D.5
  • 42
    • 0036963969 scopus 로고    scopus 로고
    • Redox signaling through NADPH oxidases: Involvement in vascular proliferation and coagulation
    • Gorlach A, Kietzmann T, Hess J: Redox signaling through NADPH oxidases: involvement in vascular proliferation and coagulation. Ann N Y Acad Sci 973:505-507, 2002
    • (2002) Ann N Y Acad Sci , vol.973 , pp. 505-507
    • Gorlach, A.1    Kietzmann, T.2    Hess, J.3
  • 43
    • 0034527379 scopus 로고    scopus 로고
    • Effect of four-week metformin treatment on plasma and erythrocyte antioxidative defense enzymes in newly diagnosed obese patients with type 2 diabetes
    • Pavlovic D, Kocic R, Kocic G, Jevtovic T, Radenkovic S, Mikic D, Stojanovic M, Djordjevic PB: Effect of four-week metformin treatment on plasma and erythrocyte antioxidative defense enzymes in newly diagnosed obese patients with type 2 diabetes. Diabetes Obes Metab 2:251-256, 2000
    • (2000) Diabetes Obes Metab , vol.2 , pp. 251-256
    • Pavlovic, D.1    Kocic, R.2    Kocic, G.3    Jevtovic, T.4    Radenkovic, S.5    Mikic, D.6    Stojanovic, M.7    Djordjevic, P.B.8
  • 44
    • 0038410183 scopus 로고    scopus 로고
    • An intracellular modulation of free radical production could contribute to the beneficial effects of metformin towards oxidative stress
    • Bonnefont-Rousselot D, Raji B, Walrand S, Gardes-Albert M, Jore D, Legrand A, Peynet J, Vasson MP: An intracellular modulation of free radical production could contribute to the beneficial effects of metformin towards oxidative stress. Metabolism 52:586-589, 2003
    • (2003) Metabolism , vol.52 , pp. 586-589
    • Bonnefont-Rousselot, D.1    Raji, B.2    Walrand, S.3    Gardes-Albert, M.4    Jore, D.5    Legrand, A.6    Peynet, J.7    Vasson, M.P.8
  • 46
    • 0033765672 scopus 로고    scopus 로고
    • High glucose level and free fatty acids stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells
    • Inoguchi T, Li P, Umeda F, Yu HY, Kakimoto M, Imamura M, Aoki T, Etoh T, Hashimoto T, Naruse M, Sano H, Utsumi H, Nawata H: High glucose level and free fatty acids stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 49:1939-1945, 2000
    • (2000) Diabetes , vol.49 , pp. 1939-1945
    • Inoguchi, T.1    Li, P.2    Umeda, F.3    Yu, H.Y.4    Kakimoto, M.5    Imamura, M.6    Aoki, T.7    Etoh, T.8    Hashimoto, T.9    Naruse, M.10    Sano, H.11    Utsumi, H.12    Nawata, H.13
  • 47
    • 0032407020 scopus 로고    scopus 로고
    • Reactive oxygen species are critical in the oleic-acid-mediated mitogenic signaling pathway in vascular smooth muscle cells
    • Lu G, Greene EL, Nagai T, Egan BM: Reactive oxygen species are critical in the oleic-acid-mediated mitogenic signaling pathway in vascular smooth muscle cells. Hypertension 32:1003-1010, 1998
    • (1998) Hypertension , vol.32 , pp. 1003-1010
    • Lu, G.1    Greene, E.L.2    Nagai, T.3    Egan, B.M.4
  • 48
    • 0034804569 scopus 로고    scopus 로고
    • Glycated serum albumin-induced vascular smooth muscle cell proliferation through activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by protein kinase C
    • Hattori Y, Kakishita H, Akimoto K, Matsumura M, Kasai K: Glycated serum albumin-induced vascular smooth muscle cell proliferation through activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by protein kinase C. Biochem Biophys Res Commun 281:891-896, 2001
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 891-896
    • Hattori, Y.1    Kakishita, H.2    Akimoto, K.3    Matsumura, M.4    Kasai, K.5
  • 49
    • 0032538875 scopus 로고    scopus 로고
    • Leptin, the product of Ob gene, promotes angiogenesis
    • Bouloumie A, Drexler HCA, Lafontan M, Busse R: Leptin, the product of Ob gene, promotes angiogenesis. Circ Res 83:1059-1066, 1998
    • (1998) Circ Res , vol.83 , pp. 1059-1066
    • Bouloumie, A.1    Drexler, H.C.A.2    Lafontan, M.3    Busse, R.4
  • 51
    • 0029417282 scopus 로고
    • d-alpha tocopherol inhibition of vascular smooth muscle cell proliferation occurs at physiological concentrations, correlates with protein kinase C inhibition, and is independent of its antioxidant properties
    • Tasinato A, Boscoboinik D, Bartoli GM, Maroni P, Azzi A: d-alpha tocopherol inhibition of vascular smooth muscle cell proliferation occurs at physiological concentrations, correlates with protein kinase C inhibition, and is independent of its antioxidant properties. Proc Natl Acad Sci U S A 92:12190-12194, 1995
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12190-12194
    • Tasinato, A.1    Boscoboinik, D.2    Bartoli, G.M.3    Maroni, P.4    Azzi, A.5
  • 54
    • 0036095269 scopus 로고    scopus 로고
    • Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: Inhibition by the AMP-activated protein kinase activation
    • Ido Y, Carling D, Ruderman N: Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation. Diabetes 51:159-167, 2002
    • (2002) Diabetes , vol.51 , pp. 159-167
    • Ido, Y.1    Carling, D.2    Ruderman, N.3
  • 55
    • 0033559856 scopus 로고    scopus 로고
    • AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: Evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
    • Muoio DM, Seefeld K, Witters LA, Coleman RA: AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target. Biochem J 338:783-791, 1999
    • (1999) Biochem J , vol.338 , pp. 783-791
    • Muoio, D.M.1    Seefeld, K.2    Witters, L.A.3    Coleman, R.A.4
  • 56
    • 0033037930 scopus 로고    scopus 로고
    • Hyperglycemia-induced activation of transcription factor κB in vascular smooth muscle cells
    • Yerneni KK, Bai W, Khan BV, Medford RM, Natarajan R: Hyperglycemia- induced activation of transcription factor κB in vascular smooth muscle cells. Diabetes 48:855-864, 1999
    • (1999) Diabetes , vol.48 , pp. 855-864
    • Yerneni, K.K.1    Bai, W.2    Khan, B.V.3    Medford, R.M.4    Natarajan, R.5
  • 57
    • 0033966202 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell proliferation by nuclear factor-κ and its inhibitor, I-κB
    • Hoshi S, Goto M, Koyama N, Nomoto K, Tanaka H: Regulation of vascular smooth muscle cell proliferation by nuclear factor-κ and its inhibitor, I-κB. J Biol Chem 275:883-889, 2000
    • (2000) J Biol Chem , vol.275 , pp. 883-889
    • Hoshi, S.1    Goto, M.2    Koyama, N.3    Nomoto, K.4    Tanaka, H.5
  • 58
    • 14344257169 scopus 로고    scopus 로고
    • AMPK inhibits fatty acid-induced increases in NF-κB transactivation in cultured human umbilical vein endothelial cells
    • Cacicedo JM, Yagihashi N, Keaney JF, Ruderman NB, Ido Y: AMPK inhibits fatty acid-induced increases in NF-κB transactivation in cultured human umbilical vein endothelial cells. Biochem Biophys Res Comm 324:1204-1209, 2004
    • (2004) Biochem Biophys Res Comm , vol.324 , pp. 1204-1209
    • Cacicedo, J.M.1    Yagihashi, N.2    Keaney, J.F.3    Ruderman, N.B.4    Ido, Y.5
  • 59
    • 0028030129 scopus 로고
    • Extracellular matrix degrading metalloproteinases in the pathogenesis of arteriosclerosis
    • Newby AC, Southgate KM, Davies M: Extracellular matrix degrading metalloproteinases in the pathogenesis of arteriosclerosis. Basic Res Cardiol 89:59-70, 1994
    • (1994) Basic Res Cardiol , vol.89 , pp. 59-70
    • Newby, A.C.1    Southgate, K.M.2    Davies, M.3
  • 61
    • 0037178897 scopus 로고    scopus 로고
    • Activation of protein kinase C zeta is essential for cytokine-induced metalloproteinase-1, -3, and -9 secretion from rabbit smooth muscle cells and inhibits proliferation
    • Hussain S, Assender JW, Bond M, Wong L-F, Murphy D, Newby AC: Activation of protein kinase C zeta is essential for cytokine-induced metalloproteinase-1, -3, and -9 secretion from rabbit smooth muscle cells and inhibits proliferation. J Biol Chem 277:27345-27352, 2002
    • (2002) J Biol Chem , vol.277 , pp. 27345-27352
    • Hussain, S.1    Assender, J.W.2    Bond, M.3    Wong, L.-F.4    Murphy, D.5    Newby, A.C.6
  • 62
    • 0032508674 scopus 로고    scopus 로고
    • Synergistic upregulation of metalloproteinase-9 by growth factors and inflammatory cytokines: An absolute requirement for transcription factor NF-kappa B
    • Bond M, Fabunmi RP, Baker AH, Newby AC: Synergistic upregulation of metalloproteinase-9 by growth factors and inflammatory cytokines: an absolute requirement for transcription factor NF-kappa B. FEBS Lett 435:29-34, 1998
    • (1998) FEBS Lett , vol.435 , pp. 29-34
    • Bond, M.1    Fabunmi, R.P.2    Baker, A.H.3    Newby, A.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.