메뉴 건너뛰기




Volumn 52, Issue 5-6, 2010, Pages 199-206

Molecular mechanisms involved in adenosine-induced endothelial cell barrier enhancement

Author keywords

Anti inflammation; Human pulmonary artery endothelial cells; Myosin light chain phosphatase; P1 receptor agonists

Indexed keywords

ADENOSINE; ADENOSINE A2A RECEPTOR; ADENOSINE A2B RECEPTOR; F ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; MYOSIN LIGHT CHAIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; SMALL INTERFERING RNA; VASCULAR ENDOTHELIAL CADHERIN;

EID: 77950917821     PISSN: 15371891     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vph.2009.12.008     Document Type: Article
Times cited : (42)

References (62)
  • 2
    • 38949112840 scopus 로고    scopus 로고
    • Adenosine promotion of cellular migration in bronchial epithelial cells is mediated by the activation of cyclic adenosine monophosphate-dependent protein kinase A
    • Allen-Gipson D.S., Spurzem K., Kolm N., Spurzem J.R., and Wyatt T.A. Adenosine promotion of cellular migration in bronchial epithelial cells is mediated by the activation of cyclic adenosine monophosphate-dependent protein kinase A. J. Investig. Med. 55 (2007) 378-385
    • (2007) J. Investig. Med. , vol.55 , pp. 378-385
    • Allen-Gipson, D.S.1    Spurzem, K.2    Kolm, N.3    Spurzem, J.R.4    Wyatt, T.A.5
  • 3
    • 0032455877 scopus 로고    scopus 로고
    • Types of purinoceptors and phospholipase A2 involved in the activation of the platelet-activating factor-dependent transacetylase activity and arachidonate release by ATP in endothelial cells
    • Balestrieri M.L., Malik K.U., Balestrieri C., and Lee T.C. Types of purinoceptors and phospholipase A2 involved in the activation of the platelet-activating factor-dependent transacetylase activity and arachidonate release by ATP in endothelial cells. Prostaglandins Other Lipid Mediat. 56 (1998) 363-375
    • (1998) Prostaglandins Other Lipid Mediat. , vol.56 , pp. 363-375
    • Balestrieri, M.L.1    Malik, K.U.2    Balestrieri, C.3    Lee, T.C.4
  • 5
    • 53649089268 scopus 로고    scopus 로고
    • Bogatcheva, N.V., Verin, A.D., 2008. The role of cytoskeleton in the regulation of vascular endothelial barrier function. Microvasc. Res. 76 (3), 202-207 (Electronic publication ahead of print, 2008 Jun 28).
    • Bogatcheva, N.V., Verin, A.D., 2008. The role of cytoskeleton in the regulation of vascular endothelial barrier function. Microvasc. Res. 76 (3), 202-207 (Electronic publication ahead of print, 2008 Jun 28).
  • 7
    • 77950916562 scopus 로고    scopus 로고
    • Potential therapeutic targets in the rapidly expanding field of purinergic signaling
    • Burnstock G. Potential therapeutic targets in the rapidly expanding field of purinergic signaling. Clin. Med. 91 (2003) 1487-1500
    • (2003) Clin. Med. , vol.91 , pp. 1487-1500
    • Burnstock, G.1
  • 8
    • 35348875514 scopus 로고    scopus 로고
    • Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family
    • Csortos, C., Kolosova, I., Verin, A.D., 2007. Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family. Am. J. Physiol. Lung Cell. Mol. Physiol. 293 (4), L843-L854.
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.293 , Issue.4
    • Csortos, C.1    Kolosova, I.2    Verin, A.D.3
  • 9
    • 0030922645 scopus 로고    scopus 로고
    • Inhibition of serine-threonine protein phosphatases decreases barrier function of rat pulmonary microvascular endothelial cells
    • Diwan A.H., Honkanen R.E., Schaeffer Jr. R.C., Strada S.J., and Thompson W.J. Inhibition of serine-threonine protein phosphatases decreases barrier function of rat pulmonary microvascular endothelial cells. J. Cell. Physiol. 171 (1997) 259-270
    • (1997) J. Cell. Physiol. , vol.171 , pp. 259-270
    • Diwan, A.H.1    Honkanen, R.E.2    Schaeffer Jr., R.C.3    Strada, S.J.4    Thompson, W.J.5
  • 10
    • 0035093023 scopus 로고    scopus 로고
    • A(2b) receptors mediate the antimitogenic effects of adenosine in cardiac fibroblasts
    • Dubey R.K., Gillespie D.G., Shue H., and Jackson E.K. A(2b) receptors mediate the antimitogenic effects of adenosine in cardiac fibroblasts. Hypertension 37 (2001) 716-721
    • (2001) Hypertension , vol.37 , pp. 716-721
    • Dubey, R.K.1    Gillespie, D.G.2    Shue, H.3    Jackson, E.K.4
  • 11
    • 0034807581 scopus 로고    scopus 로고
    • Cytoskeletal regulation of pulmonary vascular permeability
    • Dudek, S.M., Garcia, J.G., 2001. Cytoskeletal regulation of pulmonary vascular permeability. J. Appl. Physiol. 91 (4), 1487-500.
    • (2001) J. Appl. Physiol , vol.91 , Issue.4 , pp. 1487-1500
    • Dudek, S.M.1    Garcia, J.G.2
  • 14
    • 10244222236 scopus 로고    scopus 로고
    • Endogenous adenosine produced during hypoxia attenuates neutrophil accumulation: coordination by extracellular nucleotide metabolism
    • Eltzschig H.K., Thompson L.F., Karhausen J., Cotta R.J., Ibla J.C., Robson S.C., and Colgan S.P. Endogenous adenosine produced during hypoxia attenuates neutrophil accumulation: coordination by extracellular nucleotide metabolism. Blood 104 (2004) 3986-3992
    • (2004) Blood , vol.104 , pp. 3986-3992
    • Eltzschig, H.K.1    Thompson, L.F.2    Karhausen, J.3    Cotta, R.J.4    Ibla, J.C.5    Robson, S.C.6    Colgan, S.P.7
  • 15
    • 0032555506 scopus 로고    scopus 로고
    • Thrombin inactivates myosin light chain phosphatase via Rho and in target Rho kinase in human endothelial cells
    • 21867-21574
    • Essler M., Amano M., Kruse H.J., Kaibuchi K., Weber P.C., and Aepfelbacher M. Thrombin inactivates myosin light chain phosphatase via Rho and in target Rho kinase in human endothelial cells. J. Biol. Chem. 273 (1998) 21867-21574
    • (1998) J. Biol. Chem. , vol.273
    • Essler, M.1    Amano, M.2    Kruse, H.J.3    Kaibuchi, K.4    Weber, P.C.5    Aepfelbacher, M.6
  • 16
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J., and Nakano T. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274 (1999) 37385-37390
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3    Isaka, N.4    Nishikawa, M.5    Hartshorne, D.J.6    Nakano, T.7
  • 17
    • 0035865444 scopus 로고    scopus 로고
    • Comparison of the potency of adenosine as an agonist at human adenosine receptors expressed in Chinese hamster ovary cells
    • Fredholm B.B., Irenius E., Kull B., and Schulte G. Comparison of the potency of adenosine as an agonist at human adenosine receptors expressed in Chinese hamster ovary cells. Biochem. Pharmacol. 61 (2001) 443-448
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 443-448
    • Fredholm, B.B.1    Irenius, E.2    Kull, B.3    Schulte, G.4
  • 19
    • 0030037103 scopus 로고    scopus 로고
    • Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle
    • Gailly P., Wu X., Haystead T.A., Somlyo A.P., Cohen P.T., Cohen P., and Somlyo A.V. Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle. Eur. J. Biochem. 239 (1996) 326-332
    • (1996) Eur. J. Biochem. , vol.239 , pp. 326-332
    • Gailly, P.1    Wu, X.2    Haystead, T.A.3    Somlyo, A.P.4    Cohen, P.T.5    Cohen, P.6    Somlyo, A.V.7
  • 20
    • 0033604903 scopus 로고    scopus 로고
    • A2B adenosine and P2Y2 receptors stimulate mitogen-activated protein kinase in human embryonic kidney-293 cells. Cross-talk between cyclic AMP and protein kinase c pathways
    • Gao Z., Chen T., Weber M.J., and Linden J. A2B adenosine and P2Y2 receptors stimulate mitogen-activated protein kinase in human embryonic kidney-293 cells. Cross-talk between cyclic AMP and protein kinase c pathways. J. Biol. Chem. 274 (1999) 5972-5980
    • (1999) J. Biol. Chem. , vol.274 , pp. 5972-5980
    • Gao, Z.1    Chen, T.2    Weber, M.J.3    Linden, J.4
  • 21
    • 0029283128 scopus 로고
    • Regulation of endothelial cell gap formation and paracellular permeability
    • Garcia J.G.N., and Schaphorst K.L. Regulation of endothelial cell gap formation and paracellular permeability. J. Invest. Med. 43 (1995) 117-126
    • (1995) J. Invest. Med. , vol.43 , pp. 117-126
    • Garcia, J.G.N.1    Schaphorst, K.L.2
  • 22
    • 0029012398 scopus 로고
    • Regulation of endothelial cell gap formation and barrier dysfunction. Role of myosin light chain phosphorylation
    • Garcia J.G.N., Davis H.W., and Patterson C.E. Regulation of endothelial cell 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
  • 23
    • 38949213299 scopus 로고    scopus 로고
    • Adenosine A2A receptor activation and macrophage-mediated experimental glomerulonephritis
    • Garcia G.E., Truong L.D., Li P., Zhang P., Du J., Chen J.F., and Feng L. Adenosine A2A receptor activation and macrophage-mediated experimental glomerulonephritis. FASEB J. 22 (2008) 445-454
    • (2008) FASEB J. , vol.22 , pp. 445-454
    • Garcia, G.E.1    Truong, L.D.2    Li, P.3    Zhang, P.4    Du, J.5    Chen, J.F.6    Feng, L.7
  • 25
    • 34247876192 scopus 로고    scopus 로고
    • Extracellular ATP induces assembly and activation of the myosin light chain phosphatase complex in endothelial cells
    • Härtel F.V., Rodewald C.W., Aslam M., Gündüz D., Hafer L., Neumann J., Piper H.M., and Noll T. Extracellular ATP induces assembly and activation of the myosin light chain phosphatase complex in endothelial cells. Cardiovasc. Res. 74 (2007) 487-496
    • (2007) Cardiovasc. Res. , vol.74 , pp. 487-496
    • Härtel, F.V.1    Rodewald, C.W.2    Aslam, M.3    Gündüz, D.4    Hafer, L.5    Neumann, J.6    Piper, H.M.7    Noll, T.8
  • 26
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase; subunit composition, interactions and regulation
    • Hartshorne D.J., Ito M., and Erdodi F. Myosin light chain phosphatase; subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19 (1998) 325-341
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 27
    • 0027191841 scopus 로고
    • Adenosine decreases permeability of in vitro endothelial monolayers
    • Haselton, F.R., Alexander, J.S., Mueller, S.N., 1993. Adenosine decreases permeability of in vitro endothelial monolayers. J. Appl. Physiol. 74 (4), 1581-1590.
    • (1993) J. Appl. Physiol , vol.74 , Issue.4 , pp. 1581-1590
    • Haselton, F.R.1    Alexander, J.S.2    Mueller, S.N.3
  • 28
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine; an endogeneous regulator of innate immunity
    • Hasko G., and Cronstein B.N. Adenosine; an endogeneous regulator of innate immunity. Trends Immunol. 25 (2004) 33-39
    • (2004) Trends Immunol. , vol.25 , pp. 33-39
    • Hasko, G.1    Cronstein, B.N.2
  • 29
    • 43349085701 scopus 로고    scopus 로고
    • A2A receptors in inflammation and injury: lessons learned from transgenic animals
    • Haskó G., and Pacher P. A2A receptors in inflammation and injury: lessons learned from transgenic animals. J. Leukoc. Biol. 83 (2008) 447-455
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 447-455
    • Haskó, G.1    Pacher, P.2
  • 30
    • 1942538405 scopus 로고    scopus 로고
    • Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits
    • Ito M., Nakano T., Erdodi F., and Hartshorne D.J. Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits. Mol. Cell. Biochem. 259 (2004) 197-209
    • (2004) Mol. Cell. Biochem. , vol.259 , pp. 197-209
    • Ito, M.1    Nakano, T.2    Erdodi, F.3    Hartshorne, D.J.4
  • 31
    • 33745373374 scopus 로고    scopus 로고
    • Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway
    • Janiak A., Zemskov E.A., and Belkin A.M. Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway. Mol. Biol. Cell 17 (2006) 1606-1619
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1606-1619
    • Janiak, A.1    Zemskov, E.A.2    Belkin, A.M.3
  • 32
    • 0030036564 scopus 로고    scopus 로고
    • Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits
    • Johnson D.F., Moorhead G., Caudwell F.B., Cohen P., Chen Y.H., Chen M.X., and Cohen P.T. Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targetting subunits. Eur. J. Biochem. 239 (1996) 317-325
    • (1996) Eur. J. Biochem. , vol.239 , pp. 317-325
    • Johnson, D.F.1    Moorhead, G.2    Caudwell, F.B.3    Cohen, P.4    Chen, Y.H.5    Chen, M.X.6    Cohen, P.T.7
  • 36
    • 0035040532 scopus 로고    scopus 로고
    • Molecular approach to adenosine receptors: receptor-mediated mechanisms of tissue protection
    • Linden J. Molecular approach to adenosine receptors: receptor-mediated mechanisms of tissue protection. Annu. Rev. Pharmacol. Toxicol. 41 (2001) 775-787
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 775-787
    • Linden, J.1
  • 38
    • 0032772422 scopus 로고    scopus 로고
    • Microvascular permeability
    • Mickell C.C., and Curry F.E. Microvascular permeability. Physiol. Rev. 79 (1999) 703-761
    • (1999) Physiol. Rev. , vol.79 , pp. 703-761
    • Mickell, C.C.1    Curry, F.E.2
  • 39
    • 34548398926 scopus 로고    scopus 로고
    • Genetic removal of the A2A adenosine receptor enhances pulmonary inflammation, mucin production, and angiogenesis in adenosine deaminase-deficient mice
    • Mohsenin A., Mi T., Xia Y., Kellems R.E., Chen J.F., and Blackburn M.R. Genetic removal of the A2A adenosine receptor enhances pulmonary inflammation, mucin production, and angiogenesis in adenosine deaminase-deficient mice. Am. J. Physiol. Lung Cell. Mol. Physiol 293 (2007) L753-L761
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.293
    • Mohsenin, A.1    Mi, T.2    Xia, Y.3    Kellems, R.E.4    Chen, J.F.5    Blackburn, M.R.6
  • 40
    • 35349031091 scopus 로고    scopus 로고
    • Targeted deletion of A2A adenosine receptors attenuates the protective effects of myocardial postconditioning
    • Morrison R.R., Tan X.L., Ledent C., Mustafa S.J., and Hofmann P.A. Targeted deletion of A2A adenosine receptors attenuates the protective effects of myocardial postconditioning. Am. J. Physiol. Heart Circ. Physiol. 293 (2007) H2523-H2529
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293
    • Morrison, R.R.1    Tan, X.L.2    Ledent, C.3    Mustafa, S.J.4    Hofmann, P.A.5
  • 41
    • 0035924320 scopus 로고    scopus 로고
    • Role of G-protein-coupled adenosine receptors in downregulation of inflammation and protection from tissue damage
    • Ohta A., and Sitkovsky M. Role of G-protein-coupled adenosine receptors in downregulation of inflammation and protection from tissue damage. Nature 414 (2001) 916-920
    • (2001) Nature , vol.414 , pp. 916-920
    • Ohta, A.1    Sitkovsky, M.2
  • 42
    • 40349110970 scopus 로고    scopus 로고
    • Suppression of inflammatory and immune responses by the A(2A) adenosine receptor: an introduction
    • Palmer T.M., and Trevethick M.A. Suppression of inflammatory and immune responses by the A(2A) adenosine receptor: an introduction. Br. J. Pharmacol. 153 Suppl 1 (2008) S27-S34
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.SUPPL. 1
    • Palmer, T.M.1    Trevethick, M.A.2
  • 43
    • 0026587590 scopus 로고
    • Role of adenosine in platelet-mediated reduction in pulmonary vascular permeability
    • Paty, P.S., Sherman, P.F., Shepard, J.M., Malik, A.B., Kaplan, J.E., 1992. Role of adenosine in platelet-mediated reduction in pulmonary vascular permeability. Am. J. Physiol. 262 (3 Pt 2), H771-H777.
    • (1992) Am. J. Physiol , vol.262 , Issue.3 PART 2
    • Paty, P.S.1    Sherman, P.F.2    Shepard, J.M.3    Malik, A.B.4    Kaplan, J.E.5
  • 45
    • 39749100503 scopus 로고    scopus 로고
    • Physiological functions of the imprinted Gnas locus and its protein variants Galpha(s) and XLalpha(s) in human and mouse
    • Plagge A., Kelsey G., and Germain-Lee E.L. Physiological functions of the imprinted Gnas locus and its protein variants Galpha(s) and XLalpha(s) in human and mouse. J. Endocrinol. 96 (2008) 193-214
    • (2008) J. Endocrinol. , vol.96 , pp. 193-214
    • Plagge, A.1    Kelsey, G.2    Germain-Lee, E.L.3
  • 46
    • 33744810576 scopus 로고    scopus 로고
    • Adenosine receptors as promising therapeutic targets for drug development in chronic airway inflammation
    • Polosa R.T., and Holgate S.T. Adenosine receptors as promising therapeutic targets for drug development in chronic airway inflammation. Curr. Drug Targets 7 (2006) 699-706
    • (2006) Curr. Drug Targets , vol.7 , pp. 699-706
    • Polosa, R.T.1    Holgate, S.T.2
  • 47
    • 0022638420 scopus 로고
    • Simultaneous cell cycle analysis and two-color surface immunofluorescence using 7-amino-actinomycin D and single laser excitation: applications to study of cell activation and the cell cycle of murine Ly-1 B cells
    • Rabinovitch P.S., Torres R.M., and Engel D. Simultaneous cell cycle analysis and two-color surface immunofluorescence using 7-amino-actinomycin D and single laser excitation: applications to study of cell activation and the cell cycle of murine Ly-1 B cells. J. Immunol. 136 (1986) 2769-2775
    • (1986) J. Immunol. , vol.136 , pp. 2769-2775
    • Rabinovitch, P.S.1    Torres, R.M.2    Engel, D.3
  • 48
    • 59649088866 scopus 로고    scopus 로고
    • Adenosine and inflammation: CD39 and CD73 are critical mediators in LPS-induced PMN trafficking into the lungs
    • Reutershan J., Vollmer I., Stark S., Wagner R., Ngamsri K.C., and Eltzschig H.K. Adenosine and inflammation: CD39 and CD73 are critical mediators in LPS-induced PMN trafficking into the lungs. FASEB J. 23 (2009) 473-482
    • (2009) FASEB J. , vol.23 , pp. 473-482
    • Reutershan, J.1    Vollmer, I.2    Stark, S.3    Wagner, R.4    Ngamsri, K.C.5    Eltzschig, H.K.6
  • 49
    • 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., and Srinivas. Extracellular ATP opposes thrombin-induced myosin light chain phosphorylation and loss of barrier integrity in corneal endothelial cells. Exp. Eye Res. 81 (2005) 183-192
    • (2005) Exp. Eye Res. , vol.81 , pp. 183-192
    • Satpathy, M.1    Gallagher, P.2    Jin, Y.3    Srinivas4
  • 51
    • 0025642947 scopus 로고
    • Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium
    • Schnittler H.J., Wilke A., Gress T., Suttorp N., and Drenckhahn D. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J. Physiol. 431 (1990) 379-401
    • (1990) J. Physiol. , vol.431 , pp. 379-401
    • Schnittler, H.J.1    Wilke, A.2    Gress, T.3    Suttorp, N.4    Drenckhahn, D.5
  • 52
    • 19544391973 scopus 로고    scopus 로고
    • The 'danger' sensors that STOP the immune response: the A2 adenosine receptors?
    • Sitkovsky M.V., and Ohta A. The 'danger' sensors that STOP the immune response: the A2 adenosine receptors?. Trends Immunol. 26 (2005) 299-304
    • (2005) Trends Immunol. , vol.26 , pp. 299-304
    • Sitkovsky, M.V.1    Ohta, A.2
  • 53
    • 0024594707 scopus 로고
    • Role of cyclic adenosine monophosphate in the induction of endothelial barrier properties
    • Stelzner T.J., Weil J.V., and O'Brien R.F. Role of cyclic adenosine monophosphate in the induction of endothelial barrier properties. J. Cell. Physiol. 139 (1989) 157-166
    • (1989) J. Cell. Physiol. , vol.139 , pp. 157-166
    • Stelzner, T.J.1    Weil, J.V.2    O'Brien, R.F.3
  • 55
    • 16544387521 scopus 로고    scopus 로고
    • Phosphatase 2A is involved in endothelial cell microtubule remodeling and barrier regulation
    • Tar K., Birukova A.A., Csortos C., Bakó E., Garcia J.G., and Verin A.D. Phosphatase 2A is involved in endothelial cell microtubule remodeling and barrier regulation. J. Cell. Biochem 92 (2004) 534-546
    • (2004) J. Cell. Biochem , vol.92 , pp. 534-546
    • Tar, K.1    Birukova, A.A.2    Csortos, C.3    Bakó, E.4    Garcia, J.G.5    Verin, A.D.6
  • 59
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: crossing cellular barriers
    • Tuma P.L., and Hubbardm A.L. Transcytosis: crossing cellular barriers. Physiol. Rev. 83 (2003) 871-932
    • (2003) Physiol. Rev. , vol.83 , pp. 871-932
    • Tuma, P.L.1    Hubbardm, A.L.2
  • 60
    • 0029131091 scopus 로고
    • Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities
    • Verin A.D., Patterson C.E., Day M.A., and Garcia J.G. Regulation of endothelial cell gap formation and barrier function by myosin-associated phosphatase activities. Am. J. Physiol. 269 (1995) L99-L108
    • (1995) Am. J. Physiol. , vol.269
    • Verin, A.D.1    Patterson, C.E.2    Day, M.A.3    Garcia, J.G.4
  • 61
    • 0036374565 scopus 로고    scopus 로고
    • Lipopolysaccharide binds to and activates A(1) adenosine receptors on human pulmonary artery endothelial cells
    • Wilson C.N., and Batra V.K. Lipopolysaccharide binds to and activates A(1) adenosine receptors on human pulmonary artery endothelial cells. J. Endotoxin Res. 8 (2002) 263-271
    • (2002) J. Endotoxin Res. , vol.8 , pp. 263-271
    • Wilson, C.N.1    Batra, V.K.2
  • 62
    • 0033766981 scopus 로고    scopus 로고
    • Extracellular metabolism of ATP and other nucleotides
    • Zimmermann H. Extracellular metabolism of ATP and other nucleotides. Naunyn Schmiedebergs Arch. Pharmacol. 362 (2000) 299-309
    • (2000) Naunyn Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 299-309
    • Zimmermann, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.