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Volumn 52, Issue 2, 2003, Pages 254-259

Garlic extract methylallyl thiosulfinate blocks insulin potentiation of platelet-derived growth factor-stimulated migration of vascular smooth muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; GARLIC EXTRACT; GERANYLGERANYLATED RHOA; GERANYLGERANYLTRANSFERASE I; INSULIN; PLATELET DERIVED GROWTH FACTOR; PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; THIOSULFINIC ACID METHYLALLYL ESTER; UNCLASSIFIED DRUG;

EID: 0037304135     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1053/meta.2003.50042     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • Owens GK: Regulation of differentiation of vascular smooth muscle cells. Physiol Rev 75:487-517, 1995
    • (1995) Physiol Rev , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 2
    • 0344353645 scopus 로고    scopus 로고
    • Inhibition of platelet-derived growth factor receptor tyrosine kinase inhibits vascular smooth muscle cell migration and proliferation
    • Myllarniemi M, Calderon L, Lemstrom K, et al: Inhibition of platelet-derived growth factor receptor tyrosine kinase inhibits vascular smooth muscle cell migration and proliferation. FASEB J 11:1119-1126, 1997
    • (1997) FASEB J , vol.11 , pp. 1119-1126
    • Myllarniemi, M.1    Calderon, L.2    Lemstrom, K.3
  • 3
    • 0032582808 scopus 로고    scopus 로고
    • Differentiated phenotype of smooth muscle cells depends on signaling pathway through insulin-like growth factors and PI 3-kinase
    • Hyashi K, Sapa H, Chitnori Y, et al: Differentiated phenotype of smooth muscle cells depends on signaling pathway through insulin-like growth factors and PI 3-kinase. J Biol Chem 273:28860-28867, 1998
    • (1998) J Biol Chem , vol.273 , pp. 28860-28867
    • Hyashi, K.1    Sapa, H.2    Chitnori, Y.3
  • 4
    • 14444278515 scopus 로고    scopus 로고
    • Insulin potentiates platelet-derived growth factor action in vascular smooth muscle cells
    • Goalstone ML, Natarajan R, Stanley PR, et al: Insulin potentiates platelet-derived growth factor action in vascular smooth muscle cells. Endocrinology 139:4067-4072, 1998
    • (1998) Endocrinology , vol.139 , pp. 4067-4072
    • Goalstone, M.L.1    Natarajan, R.2    Stanley, P.R.3
  • 5
    • 0034811763 scopus 로고    scopus 로고
    • Dominant negative α-subunit inhibits insulin mitogenic effects
    • Solomon CC, Goalstone ML: Dominant negative α-subunit inhibits insulin mitogenic effects. Biochem Biophys Res Commun 285:161-166, 2001
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 161-166
    • Solomon, C.C.1    Goalstone, M.L.2
  • 6
    • 0034644757 scopus 로고    scopus 로고
    • Potentiation of Rho-A mediated lysophosphatidic acid activity by hyperinsulinemia
    • Chappell J, Golovchenko I, Wall K, et al: Potentiation of Rho-A mediated lysophosphatidic acid activity by hyperinsulinemia. J Biol Chem 275:31792-31797, 2000
    • (2000) J Biol Chem , vol.275 , pp. 31792-31797
    • Chappell, J.1    Golovchenko, I.2    Wall, K.3
  • 7
    • 0030963460 scopus 로고    scopus 로고
    • Hyperinsulinemia potentiates activation of p21 Ras by growth factors
    • Leitner JW, Kline T, Carel K, et al: Hyperinsulinemia potentiates activation of p21 Ras by growth factors. Endocrinology 130:2211-2214, 1997
    • (1997) Endocrinology , vol.130 , pp. 2211-2214
    • Leitner, J.W.1    Kline, T.2    Carel, K.3
  • 8
    • 0030690195 scopus 로고    scopus 로고
    • Insulin stimulates the phosphorylation and activity of farnesyltransferase via the ras-mitogen-activated protein kinase pathway
    • Goalstone ML, Carel K, Leitner JW, et al: Insulin stimulates the phosphorylation and activity of farnesyltransferase via the ras-mitogen-activated protein kinase pathway. Endocrinology 138:5119-5124, 1997
    • (1997) Endocrinology , vol.138 , pp. 5119-5124
    • Goalstone, M.L.1    Carel, K.2    Leitner, J.W.3
  • 9
    • 0035918286 scopus 로고    scopus 로고
    • Insulin signals to prenyltransferases via the Shc branch of intracellular signaling
    • Goalstone ML, Leitner JW, Berhanu P, et al: Insulin signals to prenyltransferases via the Shc branch of intracellular signaling. J Biol Chem 276:12805-12812, 2001
    • (2001) J Biol Chem , vol.276 , pp. 12805-12812
    • Goalstone, M.L.1    Leitner, J.W.2    Berhanu, P.3
  • 10
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
    • Seabra MC, Reiss Y, Casey PJ, et al: Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit. Cell 65:429-434, 1991
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3
  • 11
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang FL, Casey PJ: Protein prenylation: Molecular mechanisms and functional consequences. Annu Rev Biochem 65:241-269, 1996
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 12
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A: Rho GTPases and the actin cytoskeleton. Science 279:509-514, 1998
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 13
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi D, Hall A: Ras and Rho GTPases: A family reunion. Cell 103:227-238, 2000
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 14
    • 0026353346 scopus 로고
    • Sequence dependence of protein isoprenylation
    • Moores SL, Schader MD, Mosser SD, et al: Sequence dependence of protein isoprenylation. J Biol Chem 266:4603-4610, 1991
    • (1991) J Biol Chem , vol.266 , pp. 4603-4610
    • Moores, S.L.1    Schader, M.D.2    Mosser, S.D.3
  • 15
    • 0031833268 scopus 로고    scopus 로고
    • Natural inhibitors for protein prenyltransferases
    • Lee S, Park S, Oh J-W, et al: Natural inhibitors for protein prenyltransferases. Planta Medica 64:303-308, 1998
    • (1998) Planta Medica , vol.64 , pp. 303-308
    • Lee, S.1    Park, S.2    Oh, J.-W.3
  • 16
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C: Rho GTPases and signaling networks. Genes Dev 11:2295-2322, 1997
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 17
    • 0025978177 scopus 로고
    • 2+ sensitization of smooth muscle contraction through myosin light chain phosphorylation
    • 2+ sensitization of smooth muscle contraction through myosin light chain phosphorylation. J Biol Chem 266:1708-1715, 1991
    • (1991) J Biol Chem , vol.266 , pp. 1708-1715
    • Kitazawa, T.1    Gaylinn, B.D.2    Denney, G.H.3
  • 18
    • 0033612371 scopus 로고    scopus 로고
    • Rho and Rho kinase mediate thrombin-stimulated vascular smooth muscle cell DNA synthesis and migration
    • Seasholtz TM, Majumdar M, Kaplan DD, et al: Rho and Rho kinase mediate thrombin-stimulated vascular smooth muscle cell DNA synthesis and migration. Circ Res 84:1186-1193, 1999
    • (1999) Circ Res , vol.84 , pp. 1186-1193
    • Seasholtz, T.M.1    Majumdar, M.2    Kaplan, D.D.3
  • 19
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling network
    • Van Aelst L, D'Sonza-Schorey C: Rho GTPases and signaling network. Genes Dev 11:2295-2322, 1997
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Sonza-Schorey, C.2
  • 20
    • 0034721925 scopus 로고    scopus 로고
    • Hyperinsulinemia enhances transcriptional activity of nuclear factor-kB induced by angiotensin II, hyperglycemia and advanced glycosylation end products in vascular smooth muscle cells
    • Golovchenko I, Goalstone ML, Watson P, et al: Hyperinsulinemia enhances transcriptional activity of nuclear factor-kB induced by angiotensin II, hyperglycemia and advanced glycosylation end products in vascular smooth muscle cells. Circ Res 87:746-752, 2000
    • (2000) Circ Res , vol.87 , pp. 746-752
    • Golovchenko, I.1    Goalstone, M.L.2    Watson, P.3
  • 21
    • 0035851206 scopus 로고    scopus 로고
    • Effect of insulin on cell cycle progression in MCF-7 breast cancer cells
    • Chappell J, Leitner JW, Solomon S, et al: Effect of insulin on cell cycle progression in MCF-7 breast cancer cells. J Biol Chem 276:38023-38028, 2001
    • (2001) J Biol Chem , vol.276 , pp. 38023-38028
    • Chappell, J.1    Leitner, J.W.2    Solomon, S.3
  • 22
    • 0032719024 scopus 로고    scopus 로고
    • Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats
    • Jiang ZY, Li Y-W, Clemont A, et al: Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats. J Clin Invest 104:447-457, 1999
    • (1999) J Clin Invest , vol.104 , pp. 447-457
    • Jiang, Z.Y.1    Li, Y.-W.2    Clemont, A.3
  • 23
    • 0033968126 scopus 로고    scopus 로고
    • Insulin resistance differentially affects the PI 3-kinase- and MAP kinase-mediated signaling in human muscle
    • Cusi K, Maezono K, Osman A, et al: Insulin resistance differentially affects the PI 3-kinase- and MAP kinase-mediated signaling in human muscle. J Clin Invest 105:311-320, 2000
    • (2000) J Clin Invest , vol.105 , pp. 311-320
    • Cusi, K.1    Maezono, K.2    Osman, A.3
  • 24
    • 18544363627 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase enhances mitogenic action in insulin in endothelial cells
    • Montagnani M, Golovchenko I, Kim I, et al: Inhibition of phosphatidylinositol 3-kinase enhances mitogenic action in insulin in endothelial cells. J Biol Chem 277:1794-1799, 2002
    • (2002) J Biol Chem , vol.277 , pp. 1794-1799
    • Montagnani, M.1    Golovchenko, I.2    Kim, I.3
  • 25
    • 0022539320 scopus 로고
    • Allium sativum (garlic) inhibits lipid synthesis by Candida albicans
    • Adetumbi M, Javor GT: Allium sativum (garlic) inhibits lipid synthesis by Candida albicans. Antimicrobial Agents Chemother 30: 499-501, 1986
    • (1986) Antimicrobial Agents Chemother , vol.30 , pp. 499-501
    • Adetumbi, M.1    Javor, G.T.2
  • 26
    • 0024428297 scopus 로고
    • A case-control study of gastric cancer and diet in Italy
    • Buiatti E, Palli D,D Decarli A, et al: A case-control study of gastric cancer and diet in Italy. Int J Cancer 44:611-616, 1989
    • (1989) Int J Cancer , vol.44 , pp. 611-616
    • Buiatti, E.1    Palli, D.2    Decarli, A.3
  • 27
    • 0030583242 scopus 로고    scopus 로고
    • Novel anti-cancerogenic activity of an organosulfide from garlic: Inhibition of H-ras oncogene transformed tumor growth in vivo by diallyl disulfide is associated with inhibition of p21 H-ras processing
    • Singh SV, Mohan RR, Agarwal R, et al: Novel anti-cancerogenic activity of an organosulfide from garlic: Inhibition of H-ras oncogene transformed tumor growth in vivo by diallyl disulfide is associated with inhibition of p21 H-ras processing. Biochem Biophys Res Commun 225:660-665, 1996
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 660-665
    • Singh, S.V.1    Mohan, R.R.2    Agarwal, R.3
  • 28
    • 0035125669 scopus 로고    scopus 로고
    • Impact of garlic organosulfides on p21H-ras processing
    • Singh S: Impact of garlic organosulfides on p21H-ras processing. J Nutr 131:1046S-1048S, 2001 (suppl 35)
    • (2001) J Nutr , vol.131 , Issue.SUPPL. 35
    • Singh, S.1
  • 29
    • 0035123580 scopus 로고    scopus 로고
    • Molecular basis by which garlic suppresses atherosclerosis
    • Campbell JH, Efendy JL, Smith NJ, et al: Molecular basis by which garlic suppresses atherosclerosis. J Nutr 131:1006S-1009S, 2001 (suppl 35)
    • (2001) J Nutr , vol.131 , Issue.SUPPL. 35
    • Campbell, J.H.1    Efendy, J.L.2    Smith, N.J.3
  • 30
    • 0023120463 scopus 로고
    • Effect of an odour-modified garlic preparation on blood lipids
    • Lau B, Lam F, Wang-Chen R: Effect of an odour-modified garlic preparation on blood lipids. Nutr Res 7:139-149, 1987
    • (1987) Nutr Res , vol.7 , pp. 139-149
    • Lau, B.1    Lam, F.2    Wang-Chen, R.3
  • 31
    • 0027322071 scopus 로고
    • Garlic supplementation and lipoprotein oxidation susceptibility
    • Phelps S, Harris W: Garlic supplementation and lipoprotein oxidation susceptibility. Lipids 28:475-477, 1993
    • (1993) Lipids , vol.28 , pp. 475-477
    • Phelps, S.1    Harris, W.2
  • 32
    • 0017740350 scopus 로고
    • Effect of essential oil of garlic on serum fibrinolytic activity in patients with coronary artery disease
    • Bordia AK, Joshi HK, Sanadhya YK, et al: Effect of essential oil of garlic on serum fibrinolytic activity in patients with coronary artery disease. Atherosclerosis 28:155-159, 1977
    • (1977) Atherosclerosis , vol.28 , pp. 155-159
    • Bordia, A.K.1    Joshi, H.K.2    Sanadhya, Y.K.3
  • 33
    • 0024245112 scopus 로고
    • Effect of dried garlic on blood coagulation fibrinolysis, platelet aggregation and serum cholesterol levels in patients with hyperlipoproteinemia
    • Harenberg J, Griese C, Zimmermann R: Effect of dried garlic on blood coagulation fibrinolysis, platelet aggregation and serum cholesterol levels in patients with hyperlipoproteinemia. Atherosclerosis 74: 247-249, 1988
    • (1988) Atherosclerosis , vol.74 , pp. 247-249
    • Harenberg, J.1    Griese, C.2    Zimmermann, R.3
  • 34
    • 0035126519 scopus 로고    scopus 로고
    • Garlic compounds minimize intracellular oxidative stress and inhibit nuclear factor-κB activation
    • Ide N, Lau BHS: Garlic compounds minimize intracellular oxidative stress and inhibit nuclear factor-κB activation. J Nutr 131: 1020S-1026S, 2001 (suppl 35)
    • (2001) J Nutr , vol.131 , Issue.SUPPL. 35
    • Ide, N.1    Lau, B.H.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.