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Volumn 39, Issue 4-5, 2002, Pages 173-185

Role of Ca2+ signaling in the regulation of endothelial permeability

Author keywords

Lung microvascular permeability; Protein kinase C (PKC ); Store operated Ca2+ influx; Transient receptor potential channel (TRPC); Vascular endothelial cells

Indexed keywords

CADHERIN; CALCIUM; G PROTEIN COUPLED RECEPTOR; HISTAMINE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; MYOSIN LIGHT CHAIN; PHOSPHOLIPASE; PROTEIN KINASE C; THROMBIN; CALCIUM CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL C;

EID: 0042845703     PISSN: 15371891     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1537-1891(03)00007-7     Document Type: Review
Times cited : (265)

References (75)
  • 1
    • 0030613771 scopus 로고    scopus 로고
    • c-src in the regulation of calcium entry via store-operated calcium channels
    • c-src in the regulation of calcium entry via store-operated calcium channels. J. Biol. Chem. 272:1997;29434-29437.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29434-29437
    • Babnigg, G.1    Bowersox, S.R.2    Villereal, M.L.3
  • 2
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge M.J., Irvine R.F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature (London). 312:1987;315-321.
    • (1987) Nature (London) , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 5
    • 0030774347 scopus 로고    scopus 로고
    • Concomitant and hormonally regulated expression of trp genes in bovine aortic endothelial cells
    • Chang A.S., Chang S.M., Garcia R.L., Schiling W.P. Concomitant and hormonally regulated expression of trp genes in bovine aortic endothelial cells. FEBS Lett. 415:1997;335-340.
    • (1997) FEBS Lett. , vol.415 , pp. 335-340
    • Chang, A.S.1    Chang, S.M.2    Garcia, R.L.3    Schiling, W.P.4
  • 7
    • 0029858026 scopus 로고    scopus 로고
    • Endothelial adherens junctions: Implications in the control of vascular permeability and angiogenesis
    • Dejana E. Endothelial adherens junctions: implications in the control of vascular permeability and angiogenesis. J. Clin. Invest. 98:1996;1949-1953.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1949-1953
    • Dejana, E.1
  • 8
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek S.M., Garcia J.G.N. Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 91:2001;1487-1500.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.N.2
  • 9
    • 0344324600 scopus 로고    scopus 로고
    • Pulmonary vascular endothelium and coagulation
    • R.G. Crystal, J.B. West, E.R. Weibel, & P.J. Barnes. Philadelphia: Lippincott-Raven
    • Dull R.O., Jaffe H.A., Ge M., Ryan T.J., Malik A.B. Pulmonary vascular endothelium and coagulation. Crystal R.G., West J.B., Weibel E.R., Barnes P.J. The Lung. 1997;653-662 Lippincott-Raven, Philadelphia.
    • (1997) The Lung , pp. 653-662
    • Dull, R.O.1    Jaffe, H.A.2    Ge, M.3    Ryan, T.J.4    Malik, A.B.5
  • 11
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon C.T. Molecular events that control the protein C anticoagulant pathway. Thromb. Haemost. 70:1993;29-35.
    • (1993) Thromb. Haemost. , vol.70 , pp. 29-35
    • Esmon, C.T.1
  • 14
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott R.F., Zawadzki J.V. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature. 288:1980;687-692.
    • (1980) Nature , vol.288 , pp. 687-692
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 16
    • 0029012398 scopus 로고
    • Regulation of endothelial gap formation and barrier dysfunction: Role of myosin light chain phosphorylation
    • Garcia J.G.N., Davis H.W., Patterson C.E. Regulation of endothelial gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J. Cell. Physiol. 163:1995;510-522.
    • (1995) J. Cell. Physiol. , vol.163 , pp. 510-522
    • Garcia, J.G.N.1    Davis, H.W.2    Patterson, C.E.3
  • 18
    • 0035854829 scopus 로고    scopus 로고
    • Ga Minigenes expressing C-terminal peptides serve as specific inhibitors of thrombin-mediated endothelial activation
    • Gilchrist A., Vanhauwe J.F., Li A., Thomas T.O., Voyno-Yasnetskaya T., Hamm H.E. Ga Minigenes expressing C-terminal peptides serve as specific inhibitors of thrombin-mediated endothelial activation. J. Biol. Chem. 276:2001;25672-25679.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25672-25679
    • Gilchrist, A.1    Vanhauwe, J.F.2    Li, A.3    Thomas, T.O.4    Voyno-Yasnetskaya, T.5    Hamm, H.E.6
  • 19
    • 0029119895 scopus 로고
    • Myosin light chain kinase-regulated endothelial cell contraction: The relationship between isometric tension, actin polymerization, and myosin phosphorylation
    • Goeckeler Z.M., Wysolmerski R.B. Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130:1995;613-627.
    • (1995) J. Cell Biol. , vol.130 , pp. 613-627
    • Goeckeler, Z.M.1    Wysolmerski, R.B.2
  • 20
    • 0030032791 scopus 로고    scopus 로고
    • Cellular consequences of thrombin-receptor activation
    • Grand R.J.A., Turnell A.S., Grabham P.W. Cellular consequences of thrombin-receptor activation. Biochem. J. 313:1996;353-368.
    • (1996) Biochem. J. , vol.313 , pp. 353-368
    • Grand, R.J.A.1    Turnell, A.S.2    Grabham, P.W.3
  • 23
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells
    • Hofmann T., Schaefer M., Schultz G., Gudermann T. Subunit composition of mammalian transient receptor potential channels in living cells. Proc. Natl. Acad. Sci. U. S. A. 99:2002;7461-7466.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7461-7466
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 28
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular cadherin (VE-cadherin)
    • Lampugnani M.G., Corada M., Caveda L., Breviario F., Ayalon O., Geiger B., Dejana E. The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular cadherin (VE-cadherin). J. Cell Biol. 129:1995;203-217.
    • (1995) J. Cell Biol. , vol.129 , pp. 203-217
    • Lampugnani, M.G.1    Corada, M.2    Caveda, L.3    Breviario, F.4    Ayalon, O.5    Geiger, B.6    Dejana, E.7
  • 31
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains
    • Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S., Ambudkar I.S. Assembly of trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains. J. Biol. Chem. 275:2000;11934-11942.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 33
  • 40
    • 0035933870 scopus 로고    scopus 로고
    • Protein kinase C-a signals Rho-guanine nucleotide dissociation inhibitor phosphorylation and Rho activation and regulates the endothelial cell barrier function
    • Mehta D., Rahman A., Malik A.B. Protein kinase C-a signals Rho-guanine nucleotide dissociation inhibitor phosphorylation and Rho activation and regulates the endothelial cell barrier function. J. Biol. Chem. 276:2001;22614-22620.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22614-22620
    • Mehta, D.1    Rahman, A.2    Malik, A.B.3
  • 41
    • 0036192011 scopus 로고    scopus 로고
    • Vesicle formation and trafficking in endothelial cells and regulation of endothelial barrier function
    • Minshall R.D., Tiruppathi C., Vogel S.M., Malik A.B. Vesicle formation and trafficking in endothelial cells and regulation of endothelial barrier function. Histochem. Cell Biol. 117:2002;105-112.
    • (2002) Histochem. Cell Biol. , vol.117 , pp. 105-112
    • Minshall, R.D.1    Tiruppathi, C.2    Vogel, S.M.3    Malik, A.B.4
  • 42
    • 0018045665 scopus 로고
    • Pharmacology and endogenous roles of prostaglandin endoperoxidases, thromboxane A2 and prostacyclin
    • Moncada S., Vane J.R. Pharmacology and endogenous roles of prostaglandin endoperoxidases, thromboxane A2 and prostacyclin. Pharmacol. Rev. 30:1979;293-331.
    • (1979) Pharmacol. Rev. , vol.30 , pp. 293-331
    • Moncada, S.1    Vane, J.R.2
  • 43
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • Moncada S., Palmer R.M.J., Higgs E.A. Nitric oxide: physiology, pathophysiology and pharmacology. Pharmacol. Rev. 43:1991;109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 44
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkable functional family
    • Montell C., Birnbaumer L., Flockerzi V. The TRP channels, a remarkable functional family. Cell. 108:2002;595-598.
    • (2002) Cell , vol.108 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 45
    • 0031867637 scopus 로고    scopus 로고
    • Signal transduction and regulation of lung endothelial cell permeability. Interaction between calcium and cAMP
    • Moore T.M., Chetham P.M., Kelly J.J., Stevens T. Signal transduction and regulation of lung endothelial cell permeability. Interaction between calcium and cAMP. Am. J. Physiol. Lung Cell. Mol. Physiol. 275:1998;L203-L222.
    • (1998) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.275
    • Moore, T.M.1    Chetham, P.M.2    Kelly, J.J.3    Stevens, T.4
  • 49
    • 0034789020 scopus 로고    scopus 로고
    • Ion channels and their role in vascular endothelium
    • Nilius B., Droogmans G. Ion channels and their role in vascular endothelium. Physiol. Rev. 81:2001;1415-1459.
    • (2001) Physiol. Rev. , vol.81 , pp. 1415-1459
    • Nilius, B.1    Droogmans, G.2
  • 52
    • 0033105984 scopus 로고    scopus 로고
    • Molecular properties of inositol 1,4,5-trisphosphate receptors
    • Patel S., Joseph S.K., Thomas A.P. Molecular properties of inositol 1,4,5-trisphosphate receptors. Cell Calcium. 25:1999;247-264.
    • (1999) Cell Calcium , vol.25 , pp. 247-264
    • Patel, S.1    Joseph, S.K.2    Thomas, A.P.3
  • 53
    • 0024210145 scopus 로고
    • Anti-coagulant potential of endothelial cell membrane components
    • Preissner K.T. Anti-coagulant potential of endothelial cell membrane components. Haemostasis. 18:1988;271-306.
    • (1988) Haemostasis , vol.18 , pp. 271-306
    • Preissner, K.T.1
  • 54
    • 0033592903 scopus 로고    scopus 로고
    • TRP, inositol 1, 4, 5-trisphosphate receptors, and capacitative calcium entry
    • Putney J.W. Jr. TRP, inositol 1, 4, 5-trisphosphate receptors, and capacitative calcium entry. Proc. Natl. Acad. Sci. U. S. A. 96:1999;14669-14671.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14669-14671
    • Putney Jr., J.W.1
  • 56
    • 0023446425 scopus 로고
    • The anti-aggregating properties of vascular endothelium interactions between prostacyclin and nitric oxide
    • Radomski M.W., Palmer P.M.J., Moncada S. The anti-aggregating properties of vascular endothelium interactions between prostacyclin and nitric oxide. Br. J. Pharmacol. 92:1987;639-646.
    • (1987) Br. J. Pharmacol. , vol.92 , pp. 639-646
    • Radomski, M.W.1    Palmer, P.M.J.2    Moncada, S.3
  • 57
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., Pentyala S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80:2000;1291-1335.
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 58
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee S.G. Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 70:2001;281-312.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 59
    • 0000344653 scopus 로고
    • The heparin-antithrombin system: A natural anticoagulant mechanism
    • R.W. Coleman, J. Hirsch, V.J. Marder, & E.W. Salmon. Philadelphia, PA: Lippincott
    • Rosenberg R.D., Bauer K.A. The heparin-antithrombin system: a natural anticoagulant mechanism. Coleman R.W., Hirsch J., Marder V.J., Salmon E.W. Hemostasis and Thrombosis. 1994;837-860 Lippincott, Philadelphia, PA.
    • (1994) Hemostasis and Thrombosis , pp. 837-860
    • Rosenberg, R.D.1    Bauer, K.A.2
  • 64
    • 0037154789 scopus 로고    scopus 로고
    • Loss sex discrimination and male-male aggression in mice deficient for TRP2
    • Stowers L., Holy T.E., Meister M., Dulac C., Koentges G. Loss sex discrimination and male-male aggression in mice deficient for TRP2. Science. 295:2002;1493-1500.
    • (2002) Science , vol.295 , pp. 1493-1500
    • Stowers, L.1    Holy, T.E.2    Meister, M.3    Dulac, C.4    Koentges, G.5
  • 65
    • 0026738687 scopus 로고
    • Electrical method for detection of endothelial cell shape change in real time: Assessment of endothelial barrier function
    • Tiruppathi C., Malik A.B., Del Vecchio P.J., Keese C.R., Giaever I. Electrical method for detection of endothelial cell shape change in real time: assessment of endothelial barrier function. Proc. Natl. Acad. Sci. U. S. A. 89:1992;7919-7923.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7919-7923
    • Tiruppathi, C.1    Malik, A.B.2    Del Vecchio, P.J.3    Keese, C.R.4    Giaever, I.5
  • 70
    • 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., van Hinsbergh V.W.M. Transient and prolonged increase in endothelial permeability induced by histamine and thrombin: role of protein kinases, calcium, and RhoA. Circ. Res. 83:1998;1115-1123.
    • (1998) Circ. Res. , vol.83 , pp. 1115-1123
    • Van Nieuw Amerongen, G.P.1    Draijer, R.2    Vermeer, M.A.3    Van Hinsbergh, V.W.M.4
  • 71
    • 0034682993 scopus 로고    scopus 로고
    • Activation of RhoA by thrombin in endothelial hyperpermeability. Role of rho kinase and protein tyrosine kinases
    • van Nieuw Amerongen G.P., Delft S.V., Vermeer M.A., Collard J.G., van Hinsbergh V.W.M. Activation of RhoA by thrombin in endothelial hyperpermeability. Role of rho kinase and protein tyrosine kinases. Circ. Res. 87:2000;335-340.
    • (2000) Circ. Res. , vol.87 , pp. 335-340
    • Van Nieuw Amerongen, G.P.1    Delft, S.V.2    Vermeer, M.A.3    Collard, J.G.4    Van Hinsbergh, V.W.M.5
  • 73
    • 0031717365 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton by thrombin in human endothelial cells: Role of Rho proteins in endothelial barrier function
    • Vouret-Craviari V., Boquet P., Pouyssegur J., Obberghen-Schilling E.V. Regulation of the actin cytoskeleton by thrombin in human endothelial cells: role of Rho proteins in endothelial barrier function. Mol. Biol. Cell. 9:1998;2639-2653.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2639-2653
    • Vouret-Craviari, V.1    Boquet, P.2    Pouyssegur, J.3    Obberghen-Schilling, E.V.4
  • 75
    • 0025186832 scopus 로고
    • Involvement of myosin light chain kinase in endothelial cell retraction
    • Wysolmerski R.B., Lagunoff D. Involvement of myosin light chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. U.S.A. 87:1990;16-20.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 16-20
    • Wysolmerski, R.B.1    Lagunoff, D.2


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