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Volumn 26, Issue 1, 2010, Pages 1-10

Lovastatin inhibits the thrombin-induced loss of barrier integrity in bovine corneal endothelium

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DEXTRAN; GERANYLGERANYL PYROPHOSPHATE; MEVINOLIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN PHOSPHATASE; NOCODAZOLE; PROTEIN ZO1; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; THROMBIN;

EID: 77649300314     PISSN: 10807683     EISSN: None     Source Type: Journal    
DOI: 10.1089/jop.2009.0025     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0019857035 scopus 로고
    • Electrical properties of rabbit corneal endothelium as determined from impedance measurements
    • Lim, J.J., and Fischbarg, J. Electrical properties of rabbit corneal endothelium as determined from impedance measurements. Biophys. J. 36:677-695, 1981.
    • (1981) Biophys. J , vol.36 , pp. 677-695
    • Lim, J.J.1    Fischbarg, J.2
  • 2
    • 0028492139 scopus 로고
    • Tight junctions of the human corneal endothelium: Morphological and electrophysio-logical features
    • Noske, W., Fromm, M., Levarlet, B. et al. Tight junctions of the human corneal endothelium: morphological and electrophysio-logical features. Ger. J. Ophthalmol. 3:253-257, 1994.
    • (1994) Ger. J. Ophthalmol , vol.3 , pp. 253-257
    • Noske, W.1    Fromm, M.2    Levarlet, B.3
  • 3
    • 4544343190 scopus 로고    scopus 로고
    • Adenosine induces dephosphorylation of myosin II regulatory light chain in cultured bovine corneal endothelial cells
    • Srinivas, S.P., Satpathy, M., Gallagher, P. et al. Adenosine induces dephosphorylation of myosin II regulatory light chain in cultured bovine corneal endothelial cells. Exp. Eye Res. 79:543-551, 2004.
    • (2004) Exp. Eye Res , vol.79 , pp. 543-551
    • Srinivas, S.P.1    Satpathy, M.2    Gallagher, P.3
  • 4
    • 33744727681 scopus 로고    scopus 로고
    • The balance between corneal transparency and edema: The Proctor Lecture
    • Edelhauser, H.F. The balance between corneal transparency and edema: the Proctor Lecture. Invest. Ophthalmol. Vis. Sci. 47:1754-1767, 2006.
    • (2006) Invest. Ophthalmol. Vis. Sci , vol.47 , pp. 1754-1767
    • Edelhauser, H.F.1
  • 5
    • 0021301256 scopus 로고
    • Fluid and electrolyte transports across corneal endothelium
    • Fischbarg, J., and Lim, J.J. Fluid and electrolyte transports across corneal endothelium. Curr. Top. Eye Res. 4:201-223, 1984.
    • (1984) Curr. Top. Eye Res , vol.4 , pp. 201-223
    • Fischbarg, J.1    Lim, J.J.2
  • 6
    • 0021964106 scopus 로고
    • Pump and leak in regulation of fl uid transport in rabbit cornea
    • Riley, M. Pump and leak in regulation of fl uid transport in rabbit cornea. Curr. Eye Res. 4:371-376, 1985.
    • (1985) Curr. Eye Res , vol.4 , pp. 371-376
    • Riley, M.1
  • 7
    • 2342640996 scopus 로고    scopus 로고
    • Cytoskeletal activation and altered gene expression in endothelial barrier regulation by simvastatin
    • Jacobson, J.R., Dudek, S.M., Birukov, K.G. et al. Cytoskeletal activation and altered gene expression in endothelial barrier regulation by simvastatin. Am. J. Respir. Cell Mol. Biol. 30:662-670, 2004.
    • (2004) Am. J. Respir. Cell Mol. Biol , vol.30 , pp. 662-670
    • Jacobson, J.R.1    Dudek, S.M.2    Birukov, K.G.3
  • 8
    • 0034610474 scopus 로고    scopus 로고
    • Simvastatin improves disturbed endothelial barrier function
    • van Nieuw Amerongen, G.P., Vermeer, M.A., Nègre-Aminou, P. et al. Simvastatin improves disturbed endothelial barrier function. Circulation. 102:2803-2809, 2000.
    • (2000) Circulation , vol.102 , pp. 2803-2809
    • van Nieuw Amerongen, G.P.1    Vermeer, M.A.2    Nègre-Aminou, P.3
  • 9
    • 27744472350 scopus 로고    scopus 로고
    • HMG CoA reductase inhibition modulates VEGF-induced endothelial cell hyperperme-ability by preventing RhoA activation and myosin regulatory light chain phosphorylation
    • Zeng, L., Xu, H., Chew, T.L., et al. HMG CoA reductase inhibition modulates VEGF-induced endothelial cell hyperperme-ability by preventing RhoA activation and myosin regulatory light chain phosphorylation. FASEB J. 19:1845-1847, 2005.
    • (2005) FASEB J , vol.19 , pp. 1845-1847
    • Zeng, L.1    Xu, H.2    Chew, T.L.3
  • 10
    • 0032834070 scopus 로고    scopus 로고
    • PKC-dependent regulation of transepithelial resistance: Roles of MLC and MLC kinase
    • Turner, J.R., Angle, J.M., Black, E.D., et al. PKC-dependent regulation of transepithelial resistance: roles of MLC and MLC kinase. Am. J. Physiol. 277:C554-C562, 1999.
    • (1999) Am. J. Physiol , vol.277
    • Turner, J.R.1    Angle, J.M.2    Black, E.D.3
  • 11
    • 0141751697 scopus 로고    scopus 로고
    • Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • Somlyo, A.P., and Somlyo, A.V. Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83:1325-1358, 2003.
    • (2003) Physiol. Rev , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 12
    • 23144445052 scopus 로고    scopus 로고
    • Extracellular ATP opposes thrombin-induced myosin light chain phosphorylation and loss of barrier integrity in corneal endothelial cells
    • Satpathy, M., Gallagher, P., Jin, Y., et al. Extracellular ATP opposes thrombin-induced myosin light chain phosphorylation and loss of barrier integrity in corneal endothelial cells. Exp. Eye Res. 81:183-192, 2005.
    • (2005) Exp. Eye Res , vol.81 , pp. 183-192
    • Satpathy, M.1    Gallagher, P.2    Jin, Y.3
  • 13
    • 4544308877 scopus 로고    scopus 로고
    • Thrombin-induced phosphorylation of the regulatory light chain of myosin II in cultured bovine corneal endothelial cells
    • Satpathy, M., Gallagher, P., Lizotte-Waniewski, M., et al. Thrombin-induced phosphorylation of the regulatory light chain of myosin II in cultured bovine corneal endothelial cells. Exp. Eye Res. 79:477-486, 2004.
    • (2004) Exp. Eye Res , vol.79 , pp. 477-486
    • Satpathy, M.1    Gallagher, P.2    Lizotte-Waniewski, M.3
  • 14
    • 33749143832 scopus 로고    scopus 로고
    • Histamine-induced phosphorylation of the regulatory light chain of myosin II disrupts the barrier integrity of corneal endothelial cells
    • Srinivas, S.P., Satpathy, M., Guo, Y., et al. Histamine-induced phosphorylation of the regulatory light chain of myosin II disrupts the barrier integrity of corneal endothelial cells. Invest. Ophthalmol. Vis. Sci. 47:4011-4018, 2006.
    • (2006) Invest. Ophthalmol. Vis. Sci , vol.47 , pp. 4011-4018
    • Srinivas, S.P.1    Satpathy, M.2    Guo, Y.3
  • 15
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm, K.E., and Stull, J.T. Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276:4527-4530, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 16
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and nonmuscle myosin II
    • Somlyo, A.P., and Somlyo, A.V. Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and nonmuscle myosin II. J. Physiol. (Lond.). 522(Pt 2):177-185, 2000.
    • (2000) J. Physiol. (Lond.) , vol.522 , Issue.PART 2 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 17
    • 0032583083 scopus 로고    scopus 로고
    • Transient and prolonged increase in endothelial permeability induced by histamine and thrombin: Role of protein kinases, calcium, and RhoA
    • van Nieuw Amerongen, G.P., Draijer, R., Vermeer, M.A., et al. Transient and prolonged increase in endothelial permeability induced by histamine and thrombin: role of protein kinases, calcium, and RhoA. Circ. Res. 83:1115-1123, 1998.
    • (1998) Circ. Res , vol.83 , pp. 1115-1123
    • van Nieuw Amerongen, G.P.1    Draijer, R.2    Vermeer, M.A.3
  • 18
    • 0034682993 scopus 로고    scopus 로고
    • Activation of RhoA by thrombin in endothelial hyperperme-ability: Role of Rho kinase and protein tyrosine kinases
    • van Nieuw Amerongen, G.P., van Delft, S., Vermeer, M.A., et al. Activation of RhoA by thrombin in endothelial hyperperme-ability: role of Rho kinase and protein tyrosine kinases. Circ. Res. 87:335-340, 2000.
    • (2000) Circ. Res , vol.87 , pp. 335-340
    • van Nieuw Amerongen, G.P.1    van Delft, S.2    Vermeer, M.A.3
  • 19
    • 33644839612 scopus 로고    scopus 로고
    • Signaling mechanisms regulating endothelial permeability
    • Mehta, D., and Malik, A.B. Signaling mechanisms regulating endothelial permeability. Physiol. Rev. 86:279-367, 2006.
    • (2006) Physiol. Rev , vol.86 , pp. 279-367
    • Mehta, D.1    Malik, A.B.2
  • 21
    • 0035528772 scopus 로고    scopus 로고
    • Statins: Mechanism of action and effects
    • Stancu, C., and Sima, A. Statins: mechanism of action and effects. J. Cell. Mol. Med. 5:378-387, 2001.
    • (2001) J. Cell. Mol. Med , vol.5 , pp. 378-387
    • Stancu, C.1    Sima, A.2
  • 22
    • 0035572718 scopus 로고    scopus 로고
    • Pleiotropic effects of 3-hydroxy-3- methylglutaryl coenzyme a reductase inhibitors
    • Takemoto, M., and Liao, J.K. Pleiotropic effects of 3-hydroxy-3- methylglutaryl coenzyme a reductase inhibitors. Arterioscler. Thromb. Vasc. Biol. 21:1712-1719, 2001.
    • (2001) Arterioscler. Thromb. Vasc. Biol , vol.21 , pp. 1712-1719
    • Takemoto, M.1    Liao, J.K.2
  • 23
    • 7644242146 scopus 로고    scopus 로고
    • Effects of statins on endothelium and signaling mechanisms
    • Endres, M., and Laufs, U. Effects of statins on endothelium and signaling mechanisms. Stroke. 35:2708-2711, 2004.
    • (2004) Stroke , vol.35 , pp. 2708-2711
    • Endres, M.1    Laufs, U.2
  • 24
    • 20144370412 scopus 로고    scopus 로고
    • Thrombin-induced rapid geranylgeranylation of RhoA as an essential process for RhoA activation in endothelial cells
    • Ohkawara, H., Ishibashi, T., Sakamoto, T., et al. Thrombin-induced rapid geranylgeranylation of RhoA as an essential process for RhoA activation in endothelial cells. J. Biol. Chem. 280:10182-10188, 2005.
    • (2005) J. Biol. Chem , vol.280 , pp. 10182-10188
    • Ohkawara, H.1    Ishibashi, T.2    Sakamoto, T.3
  • 25
    • 33644946996 scopus 로고    scopus 로고
    • GEF-H1 is involved in agonist-induced human pulmonary endothelial barrier dysfunction
    • Birukova, A.A., Adyshev, D., Gorshkov, B., et al. GEF-H1 is involved in agonist-induced human pulmonary endothelial barrier dysfunction. Am. J. Physiol. Lung Cell Mol. Physiol. 290:L540-L548, 2006.
    • (2006) Am. J. Physiol. Lung Cell Mol. Physiol , vol.290
    • Birukova, A.A.1    Adyshev, D.2    Gorshkov, B.3
  • 26
    • 21844450693 scopus 로고    scopus 로고
    • Involvement of microtubules and Rho pathway in TGF-beta1-induced lung vascular barrier dysfunction
    • Birukova, A.A., Birukov, K.G., Adyshev, D., et al. Involvement of microtubules and Rho pathway in TGF-beta1-induced lung vascular barrier dysfunction. J. Cell. Physiol. 204:934-947, 2005.
    • (2005) J. Cell. Physiol , vol.204 , pp. 934-947
    • Birukova, A.A.1    Birukov, K.G.2    Adyshev, D.3
  • 27
    • 10044270843 scopus 로고    scopus 로고
    • Novel role of microtubules in thrombin-induced endothelial barrier dysfunction
    • Birukova, A.A., Birukov, K.G., Smurova, K., et al. Novel role of microtubules in thrombin-induced endothelial barrier dysfunction. FASEB J. 18:1879-1890, 2004.
    • (2004) FASEB J , vol.18 , pp. 1879-1890
    • Birukova, A.A.1    Birukov, K.G.2    Smurova, K.3
  • 28
    • 4444247919 scopus 로고    scopus 로고
    • Microtubule disassembly induces cytoskeletal remodeling and lung vascular barrier dysfunction: Role of Rho-dependent mechanisms
    • Birukova, A.A., Smurova, K., Birukov, K.G., et al. Microtubule disassembly induces cytoskeletal remodeling and lung vascular barrier dysfunction: role of Rho-dependent mechanisms. J. Cell. Physiol. 201:55-70, 2004.
    • (2004) J. Cell. Physiol , vol.201 , pp. 55-70
    • Birukova, A.A.1    Smurova, K.2    Birukov, K.G.3
  • 29
    • 0036199909 scopus 로고    scopus 로고
    • Impact of HMG CoA reductase inhibition on small GTPases in the heart
    • Laufs, U., Kilter, H., Konkol, C., et al. Impact of HMG CoA reductase inhibition on small GTPases in the heart. Cardiovasc. Res. 53:911-920, 2002.
    • (2002) Cardiovasc. Res , vol.53 , pp. 911-920
    • Laufs, U.1    Kilter, H.2    Konkol, C.3
  • 30
    • 33645957353 scopus 로고    scopus 로고
    • Signaling for contraction and relaxation in smooth muscle of the gut
    • Murthy, K.S. Signaling for contraction and relaxation in smooth muscle of the gut. Annu. Rev. Physiol. 68:345-374, 2006.
    • (2006) Annu. Rev. Physiol , vol.68 , pp. 345-374
    • Murthy, K.S.1
  • 31
    • 42449127896 scopus 로고    scopus 로고
    • (q)-dependent signalling by the lysophosphatidic acid receptor LPA(3) in gastric smooth muscle: Reciprocal regulation of MYPT1 phosphorylation by Rho kinase and cAMP-independent PKA
    • Sriwai, W., Zhou, H., and Murthy, K.S. G(q)-dependent signalling by the lysophosphatidic acid receptor LPA(3) in gastric smooth muscle: reciprocal regulation of MYPT1 phosphorylation by Rho kinase and cAMP-independent PKA. Biochem. J. 411:543-551, 2008.
    • (2008) Biochem. J , vol.411 , pp. 543-551
    • Sriwai, W.1    Zhou, H.2    Murthy, K.S.G.3
  • 32
    • 7744223152 scopus 로고    scopus 로고
    • Differential regulation of human lung epithelial and endothelial barrier function by thrombin
    • Kawkitinarong, K., Linz-McGillem, L., Birukov, K.G., et al. Differential regulation of human lung epithelial and endothelial barrier function by thrombin. Am. J. Respir. Cell Mol. Biol. 31:517-527, 2004.
    • (2004) Am. J. Respir. Cell Mol. Biol , vol.31 , pp. 517-527
    • Kawkitinarong, K.1    Linz-McGillem, L.2    Birukov, K.G.3
  • 33
    • 34347369084 scopus 로고    scopus 로고
    • Post-translational modifi cations and regulation of the RAS superfamily of GTPases as anticancer targets
    • Konstantinopoulos, P.A., Karamouzis, M.V., and Papavassiliou, A.G. Post-translational modifi cations and regulation of the RAS superfamily of GTPases as anticancer targets. Nat. Rev. Drug Discov. 6:541-555, 2007.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 541-555
    • Konstantinopoulos, P.A.1    Karamouzis, M.V.2    Papavassiliou, A.G.3
  • 34
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F.L., and Casey, P.J. 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
  • 36
    • 48249101329 scopus 로고    scopus 로고
    • Thrombin-induced endothelial barrier disruption in intact microvessels: Role of RhoA/Rho kinase-myosin phosphatase axis
    • van Nieuw Amerongen, G.P., Musters, R.J., Eringa, E.C., et al. Thrombin-induced endothelial barrier disruption in intact microvessels: role of RhoA/Rho kinase-myosin phosphatase axis. Am. J. Physiol., Cell Physiol. 294:C1234-C1241, 2008.
    • (2008) Am. J. Physiol., Cell Physiol , vol.294
    • van Nieuw Amerongen, G.P.1    Musters, R.J.2    Eringa, E.C.3
  • 37
    • 0024509437 scopus 로고
    • Nocodazole, a micro-tubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2)
    • Eilers, U., Klumperman, J., and Hauri, H.P. Nocodazole, a micro-tubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2). J. Cell Biol. 108:13-22, 1989.
    • (1989) J. Cell Biol , vol.108 , pp. 13-22
    • Eilers, U.1    Klumperman, J.2    Hauri, H.P.3
  • 38
    • 0028800221 scopus 로고
    • Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain
    • Kolodney, M.S., and Elson, E.L. Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl. Acad. Sci. USA. 92:10252-10256, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10252-10256
    • Kolodney, M.S.1    Elson, E.L.2
  • 39
    • 33747854541 scopus 로고    scopus 로고
    • Fluvastatin stabilizes the blood-brain barrier in vitro by nitric oxide-dependent dephosphorylation of myosin light chains
    • Kuhlmann, C.R., Lessmann, V., and Luhmann, H.J. Fluvastatin stabilizes the blood-brain barrier in vitro by nitric oxide-dependent dephosphorylation of myosin light chains. Neuropharmacology. 51:907-913, 2006.
    • (2006) Neuropharmacology , vol.51 , pp. 907-913
    • Kuhlmann, C.R.1    Lessmann, V.2    Luhmann, H.J.3
  • 40
    • 23244442946 scopus 로고    scopus 로고
    • Effects of cholesterol-lowering statins on the aqueous humor outflow pathway
    • Song, J., Deng, P.F., Stinnett, S.S., et al. Effects of cholesterol-lowering statins on the aqueous humor outflow pathway. Invest. Ophthalmol. Vis. Sci. 46:2424-2432, 2005.
    • (2005) Invest. Ophthalmol. Vis. Sci , vol.46 , pp. 2424-2432
    • Song, J.1    Deng, P.F.2    Stinnett, S.S.3
  • 41
    • 67651233566 scopus 로고    scopus 로고
    • Microtubule disassembly breaks down the barrier integrity of corneal endothelium
    • Jalimarada, S.S., Shivanna, M., Kini, V., et al. Microtubule disassembly breaks down the barrier integrity of corneal endothelium. Exp. Eye Res. 89:333-343, 2009.
    • (2009) Exp. Eye Res , vol.89 , pp. 333-343
    • Jalimarada, S.S.1    Shivanna, M.2    Kini, V.3
  • 42
    • 0346278773 scopus 로고    scopus 로고
    • Isoprenoid metabolism and the pleiotropic effects of statins
    • Laufs, U., and Liao, J.K. Isoprenoid metabolism and the pleiotropic effects of statins. Curr. Atheroscler. Rep. 5:372-378, 2003.
    • (2003) Curr. Atheroscler. Rep , vol.5 , pp. 372-378
    • Laufs, U.1    Liao, J.K.2
  • 43
    • 56149098127 scopus 로고    scopus 로고
    • Endothelial cell barrier protection by simvastatin: GTPase regulation and NADPH oxidase inhibition
    • Chen, W., Pendyala, S., Natarajan, V., et al. Endothelial cell barrier protection by simvastatin: GTPase regulation and NADPH oxidase inhibition. Am. J. Physiol. Lung Cell Mol. Physiol. 295:L575-L583, 2008.
    • (2008) Am. J. Physiol. Lung Cell Mol. Physiol , vol.295
    • Chen, W.1    Pendyala, S.2    Natarajan, V.3
  • 44
    • 36148972466 scopus 로고    scopus 로고
    • Does it matter whether or not a lipid-lowering agent inhibits Rho kinase?
    • Liao, J.K. Does it matter whether or not a lipid-lowering agent inhibits Rho kinase? Curr. Atheroscler. Rep. 9:384-388, 2007.
    • (2007) Curr. Atheroscler. Rep , vol.9 , pp. 384-388
    • Liao, J.K.1
  • 45
    • 2442674323 scopus 로고    scopus 로고
    • Corneal transplantation: The forgotten graft
    • George, A.J., and Larkin, D.F. Corneal transplantation: the forgotten graft. Am. J. Transplant. 4:678-685, 2004.
    • (2004) Am. J. Transplant , vol.4 , pp. 678-685
    • George, A.J.1    Larkin, D.F.2
  • 46
    • 39149083752 scopus 로고    scopus 로고
    • Immune mechanisms of corneal allograft rejection
    • Niederkorn, J.Y. Immune mechanisms of corneal allograft rejection. Curr. Eye Res. 32:1005-1016, 2007.
    • (2007) Curr. Eye Res , vol.32 , pp. 1005-1016
    • Niederkorn, J.Y.1
  • 47
    • 0037405112 scopus 로고    scopus 로고
    • The delta-isoform of protein kinase C causes inducible nitric-oxide synthase and nitric oxide up-regulation: Key mechanism for oxidant-induced carbonylation, nitration, and disassembly of the microtubule cytoskeleton and hyperpermeability of barrier of intestinal epithelia
    • Banan, A., Farhadi, A., Fields, J.Z., et al. The delta-isoform of protein kinase C causes inducible nitric-oxide synthase and nitric oxide up-regulation: key mechanism for oxidant-induced carbonylation, nitration, and disassembly of the microtubule cytoskeleton and hyperpermeability of barrier of intestinal epithelia. J. Pharmacol. Exp. Ther. 305:482-494, 2003.
    • (2003) J. Pharmacol. Exp. Ther , vol.305 , pp. 482-494
    • Banan, A.1    Farhadi, A.2    Fields, J.Z.3
  • 48
    • 0036086444 scopus 로고    scopus 로고
    • PKC-zeta is required in EGF protection of microtubules and intestinal barrier integrity against oxidant injury
    • Banan, A., Fields, J.Z., Talmage, D.A., et al. PKC-zeta is required in EGF protection of microtubules and intestinal barrier integrity against oxidant injury. Am. J. Physiol. Gastrointest. Liver Physiol. 282:G794-G808, 2002.
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol , vol.282
    • Banan, A.1    Fields, J.Z.2    Talmage, D.A.3
  • 49
    • 0038746767 scopus 로고    scopus 로고
    • The role of the micro-tubules in tumor necrosis factor-alpha-induced endothelial cell permeability
    • Petrache, I., Birukova, A., Ramirez, S.I., et al. The role of the micro-tubules in tumor necrosis factor-alpha-induced endothelial cell permeability. Am. J. Respir. Cell Mol. Biol. 28:574-581, 2003.
    • (2003) Am. J. Respir. Cell Mol. Biol , vol.28 , pp. 574-581
    • Petrache, I.1    Birukova, A.2    Ramirez, S.I.3
  • 50
    • 4143095993 scopus 로고    scopus 로고
    • Paclitaxel prevents loss of pulmonary endothelial barrier integrity during cold preservation
    • Suzuki, S., Bing, H., Sugawara, T., et al. Paclitaxel prevents loss of pulmonary endothelial barrier integrity during cold preservation. Transplantation. 78:524-529, 2004.
    • (2004) Transplantation , vol.78 , pp. 524-529
    • Suzuki, S.1    Bing, H.2    Sugawara, T.3


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