메뉴 건너뛰기




Volumn 84, Issue 2, 2004, Pages 579-621

Protease-Activated Receptors: Contribution to Physiology and Disease

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND; PROTEINASE ACTIVATED RECEPTOR; SERINE PROTEINASE;

EID: 1642279517     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.00028.2003     Document Type: Review
Times cited : (959)

References (319)
  • 3
    • 0028825940 scopus 로고
    • Detection of functional receptors for the proteinase-activated-receptor-2-activating polypeptide, SLIGRL-NH2, in rat vascular and gastric smooth muscle
    • Al-Ani B, Saifeddine M, and Hollenberg MD. Detection of functional receptors for the proteinase-activated-receptor-2-activating polypeptide, SLIGRL-NH2, in rat vascular and gastric smooth muscle. Can J Phys Pharmacol 73: 1203-1207, 1995.
    • (1995) Can J Phys Pharmacol , vol.73 , pp. 1203-1207
    • Al-Ani, B.1    Saifeddine, M.2    Hollenberg, M.D.3
  • 4
    • 0032712580 scopus 로고    scopus 로고
    • Proteinase activated receptor 2: Role of extracellular loop 2 for ligand-mediated activation
    • Al-Ani B, Saifeddine M, Kawabata A, and Hollenberg MD. Proteinase activated receptor 2: role of extracellular loop 2 for ligand-mediated activation. Br J Pharmacol 128: 1105-1113, 1999.
    • (1999) Br J Pharmacol , vol.128 , pp. 1105-1113
    • Al-Ani, B.1    Saifeddine, M.2    Kawabata, A.3    Hollenberg, M.D.4
  • 5
  • 7
    • 0033613269 scopus 로고    scopus 로고
    • Protease-activated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity
    • Andersen H, Greenberg DL, Fujikawa K, Xu W, Chung DW, and Davie EW. Protease-activated receptor 1 is the primary mediator of thrombin-stimulated platelet procoagulant activity. Proc Natl Acad Sci USA 96: 11189-11193, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11189-11193
    • Andersen, H.1    Greenberg, D.L.2    Fujikawa, K.3    Xu, W.4    Chung, D.W.5    Davie, E.W.6
  • 11
    • 0036193921 scopus 로고    scopus 로고
    • Proteinase-activated receptor-1 agonists attenuate nociception in response to noxious stimuli
    • Asfaha S, Brussee V, Chapman K, Zochodne DW, and Vergnolle N. Proteinase-activated receptor-1 agonists attenuate nociception in response to noxious stimuli. Br J Pharmacol 135: 1101-1106, 2002.
    • (2002) Br J Pharmacol , vol.135 , pp. 1101-1106
    • Asfaha, S.1    Brussee, V.2    Chapman, K.3    Zochodne, D.W.4    Vergnolle, N.5
  • 13
    • 0028237885 scopus 로고
    • G protein coupling to the thrombin receptor in Chinese hamster lung fibroblasts
    • Baffy G, Yang L, Raj S, Manning DR, and Williamson JR. G protein coupling to the thrombin receptor in Chinese hamster lung fibroblasts. J Biol Chem 269: 8483-8487, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 8483-8487
    • Baffy, G.1    Yang, L.2    Raj, S.3    Manning, D.R.4    Williamson, J.R.5
  • 14
    • 0028085095 scopus 로고
    • Thrombin receptor peptides induce shape change in neonatal murine astrocytes in culture
    • Beecher KL, Andersen TT, Fenton JWN, and Festoff BW. Thrombin receptor peptides induce shape change in neonatal murine astrocytes in culture. J Neurosci Res 37: 108-115, 1994.
    • (1994) J Neurosci Res , vol.37 , pp. 108-115
    • Beecher, K.L.1    Andersen, T.T.2    Fenton, J.W.N.3    Festoff, B.W.4
  • 15
    • 0030470167 scopus 로고    scopus 로고
    • Trypsin stimulates proteinase-activated receptor-2-dependent and -independent activation of mitogen-activated protein kinases
    • Belham CM, Tate RJ, Scott PH, Pemberton AD, Miller HR, Wadsworth RM, Gould GW, and Plevin R. Trypsin stimulates proteinase-activated receptor-2-dependent and -independent activation of mitogen-activated protein kinases. Biochem J 320: 939-946, 1996.
    • (1996) Biochem J , vol.320 , pp. 939-946
    • Belham, C.M.1    Tate, R.J.2    Scott, P.H.3    Pemberton, A.D.4    Miller, H.R.5    Wadsworth, R.M.6    Gould, G.W.7    Plevin, R.8
  • 22
    • 0031059468 scopus 로고    scopus 로고
    • Regulatory mechanisms that modulate signalling by G-protein-coupled receptors
    • Bohm SK, Grady EF, and Bunnett NW. Regulatory mechanisms that modulate signalling by G-protein-coupled receptors. Biochem J 322: 1-18, 1997.
    • (1997) Biochem J , vol.322 , pp. 1-18
    • Bohm, S.K.1    Grady, E.F.2    Bunnett, N.W.3
  • 23
    • 0029786481 scopus 로고    scopus 로고
    • Mechanisms of desensitization and resensitization of proteinase-activated receptor-2
    • Bohm SK, Khitin LM, Grady EF, Aponte G, Payan DG, and Bunnett NW. Mechanisms of desensitization and resensitization of proteinase-activated receptor-2. J Biol Chem 271: 22003-22016, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 22003-22016
    • Bohm, S.K.1    Khitin, L.M.2    Grady, E.F.3    Aponte, G.4    Payan, D.G.5    Bunnett, N.W.6
  • 25
    • 0028797819 scopus 로고
    • Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system
    • Bouton MC, Jandrot-Perrus M, Moog S, Cazenave JP, Guillin MC, and Lanza F. Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system. Biochem J 305: 635-641, 1995.
    • (1995) Biochem J , vol.305 , pp. 635-641
    • Bouton, M.C.1    Jandrot-Perrus, M.2    Moog, S.3    Cazenave, J.P.4    Guillin, M.C.5    Lanza, F.6
  • 26
    • 0028111114 scopus 로고
    • Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling
    • Brass LF, Pizarro S, Ahuja M, Belmonte E, Blanchard N, Stadel JM, and Hoxie JA. Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling. J Biol Chem 269: 2943-2952, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 2943-2952
    • Brass, L.F.1    Pizarro, S.2    Ahuja, M.3    Belmonte, E.4    Blanchard, N.5    Stadel, J.M.6    Hoxie, J.A.7
  • 27
    • 0035066614 scopus 로고    scopus 로고
    • Evidence for functionally active protease-activated receptor-4 (PAR-4) in human vascular smooth muscle cells
    • Bretschneider E, Kaufmann R, Braun M, Nowak G, Glusa E, and Schror K. Evidence for functionally active protease-activated receptor-4 (PAR-4) in human vascular smooth muscle cells. Br J Pharmacol 132: 1441-1446, 2001.
    • (2001) Br J Pharmacol , vol.132 , pp. 1441-1446
    • Bretschneider, E.1    Kaufmann, R.2    Braun, M.3    Nowak, G.4    Glusa, E.5    Schror, K.6
  • 28
    • 0032955959 scopus 로고    scopus 로고
    • Evidence for proteinase-activated receptor-2 (PAR-2)-mediated mitogenesis in coronary artery smooth muscle cells
    • Bretschneider E, Kaufmann R, Braun M, Wittpoth M, Glusa E, Nowak G, and Schror K. Evidence for proteinase-activated receptor-2 (PAR-2)-mediated mitogenesis in coronary artery smooth muscle cells. Br J Pharmacol 126: 1735-1740, 1999.
    • (1999) Br J Pharmacol , vol.126 , pp. 1735-1740
    • Bretschneider, E.1    Kaufmann, R.2    Braun, M.3    Wittpoth, M.4    Glusa, E.5    Nowak, G.6    Schror, K.7
  • 29
    • 0000666315 scopus 로고
    • Tryptase, the dominant secretory granular protein in human mast cells, is a potent mitogen for cultured dog tracheal smooth muscle cells
    • Brown JK, Tyler CL, Jones CA, Ruoss SJ, Hartmann T, and Caughey GH. Tryptase, the dominant secretory granular protein in human mast cells, is a potent mitogen for cultured dog tracheal smooth muscle cells. J Clin Invest 88: 493-499, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 493-499
    • Brown, J.K.1    Tyler, C.L.2    Jones, C.A.3    Ruoss, S.J.4    Hartmann, T.5    Caughey, G.H.6
  • 30
    • 0036793557 scopus 로고    scopus 로고
    • Activation of proteinase-activated receptor 1 stimulates epithelial chloride secretion through a unique MAP kinase- and cyclo-oxygenase-dependent pathway
    • Buresi MC, Buret AG, Hollenberg MD, and MacNaughton WK. Activation of proteinase-activated receptor 1 stimulates epithelial chloride secretion through a unique MAP kinase- and cyclo-oxygenase-dependent pathway. FASEB J 16: 1515-1525, 2002.
    • (2002) FASEB J , vol.16 , pp. 1515-1525
    • Buresi, M.C.1    Buret, A.G.2    Hollenberg, M.D.3    MacNaughton, W.K.4
  • 33
    • 0030032558 scopus 로고    scopus 로고
    • Mast cell tryptase is a mitogen for epithelial cells. Stimulation of IL-8 production and intercellular adhesion molecule-1 expression
    • Cairns JA and Walls AF. Mast cell tryptase is a mitogen for epithelial cells. Stimulation of IL-8 production and intercellular adhesion molecule-1 expression. J Immunol 156: 275-283, 1996.
    • (1996) J Immunol , vol.156 , pp. 275-283
    • Cairns, J.A.1    Walls, A.F.2
  • 34
    • 0034624973 scopus 로고    scopus 로고
    • Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa
    • Camerer E, Huang W, and Coughlin SR. Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa. Proc Natl Acad Sci USA 97: 5255-5260, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5255-5260
    • Camerer, E.1    Huang, W.2    Coughlin, S.R.3
  • 35
    • 0037013268 scopus 로고    scopus 로고
    • Genetic evidence that protease-activated receptors mediate factor Xa signaling in endothelial cells
    • Camerer E, Kataoka H, Kahn M, Lease K, and Coughlin SR. Genetic evidence that protease-activated receptors mediate factor Xa signaling in endothelial cells. J Biol Chem 277: 16081-16087, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 16081-16087
    • Camerer, E.1    Kataoka, H.2    Kahn, M.3    Lease, K.4    Coughlin, S.R.5
  • 38
    • 0002079441 scopus 로고
    • Mast cell chymases and tryptases: Phylogeny, family relations, and biogenesis
    • edited by Caughey GH. New York: Dekker
    • Caughey GH. Mast cell chymases and tryptases: phylogeny, family relations, and biogenesis. In: Mast Cell Proteases in Immunology and Biology, edited by Caughey GH. New York: Dekker, 1995, p. 305-329.
    • (1995) Mast Cell Proteases in Immunology and Biology , pp. 305-329
    • Caughey, G.H.1
  • 39
    • 0025255579 scopus 로고
    • Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1
    • Cavanaugh KP, Gurwitz D, Cunningham DD, and Bradshaw RA. Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1. J Neurochem 54: 1735-1743, 1990.
    • (1990) J Neurochem , vol.54 , pp. 1735-1743
    • Cavanaugh, K.P.1    Gurwitz, D.2    Cunningham, D.D.3    Bradshaw, R.A.4
  • 41
    • 0037446646 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-induced colonic inflammation in mice: Possible involvement of afferent neurons, nitric oxide, and paracellular permeability
    • Cenac N, Garcia-Villar R, Ferrier L, Larauche M, Vergnolle N, Bunnett NW, Coelho AM, Fioramonti J, and Bueno L. Proteinase-activated receptor-2-induced colonic inflammation in mice: possible involvement of afferent neurons, nitric oxide, and paracellular permeability. J Immunol 170: 4296-4300, 2003.
    • (2003) J Immunol , vol.170 , pp. 4296-4300
    • Cenac, N.1    Garcia-Villar, R.2    Ferrier, L.3    Larauche, M.4    Vergnolle, N.5    Bunnett, N.W.6    Coelho, A.M.7    Fioramonti, J.8    Bueno, L.9
  • 42
    • 0034634622 scopus 로고    scopus 로고
    • Thrombin is a potent inducer of connective tissue growth factor production via proteolytic activation of protease-activated receptor-1
    • Chambers RC, Leoni P, Blanc-Brude OP, Wembridge DE, and Laurent GJ. Thrombin is a potent inducer of connective tissue growth factor production via proteolytic activation of protease-activated receptor-1. J Biol Chem 275: 35584-35591, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35584-35591
    • Chambers, R.C.1    Leoni, P.2    Blanc-Brude, O.P.3    Wembridge, D.E.4    Laurent, G.J.5
  • 43
    • 0028364862 scopus 로고
    • Thrombin receptor activation. Confirmation of the intramolecular tethered liganding hypothesis and discovery of an alternative intermolecular liganding mode
    • Chen J, Ishii M, Wang L, Ishii K, and Coughlin SR. Thrombin receptor activation. Confirmation of the intramolecular tethered liganding hypothesis and discovery of an alternative intermolecular liganding mode. J Biol Chem 269: 16041-16045, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 16041-16045
    • Chen, J.1    Ishii, M.2    Wang, L.3    Ishii, K.4    Coughlin, S.R.5
  • 44
    • 0029915662 scopus 로고    scopus 로고
    • Functional expression of a human thrombin receptor in Sf9 insect cells: Evidence for an active tethered ligand
    • Chen X, Earley K, Luo W, Lin SH, and Schilling WP. Functional expression of a human thrombin receptor in Sf9 insect cells: evidence for an active tethered ligand. Biochem J 314: 603-611, 1996.
    • (1996) Biochem J , vol.314 , pp. 603-611
    • Chen, X.1    Earley, K.2    Luo, W.3    Lin, S.H.4    Schilling, W.P.5
  • 45
    • 0027999621 scopus 로고
    • Activation of Src family kinase activity by the G protein-coupled thrombin receptor in growth-responsive fibroblasts
    • Chen YH, Pouyssegur J, Courtneidge SA, and Van Obberghen-Schilling E. Activation of Src family kinase activity by the G protein-coupled thrombin receptor in growth-responsive fibroblasts. J Biol Chem 269: 27372-27377, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 27372-27377
    • Chen, Y.H.1    Pouyssegur, J.2    Courtneidge, S.A.3    Van Obberghen-Schilling, E.4
  • 47
    • 0031919771 scopus 로고    scopus 로고
    • Receptor-activating peptides distinguish thrombin receptor (PAR-1) and protease activated receptor 2 (PAR-2) mediated hemodynamic responses in vivo
    • Cheung WM, Andrade-Gordon P, Derian CK, and Damiano BP. Receptor-activating peptides distinguish thrombin receptor (PAR-1) and protease activated receptor 2 (PAR-2) mediated hemodynamic responses in vivo. Can J Physiol Pharmacol 76: 16-25, 1998.
    • (1998) Can J Physiol Pharmacol , vol.76 , pp. 16-25
    • Cheung, W.M.1    Andrade-Gordon, P.2    Derian, C.K.3    Damiano, B.P.4
  • 49
    • 0034528452 scopus 로고    scopus 로고
    • Effect of protease-activated receptor (PAR)-1, -2 and -4-activating peptides, thrombin and trypsin in rat isolated airways
    • Chow JM, Moffatt JD, and Cocks TM. Effect of protease-activated receptor (PAR)-1, -2 and -4-activating peptides, thrombin and trypsin in rat isolated airways. Br J Pharmacol 131: 1584-1591, 2000.
    • (2000) Br J Pharmacol , vol.131 , pp. 1584-1591
    • Chow, J.M.1    Moffatt, J.D.2    Cocks, T.M.3
  • 50
    • 0036152709 scopus 로고    scopus 로고
    • Protease activated receptor 2 and the cardiovascular system
    • Cicala C. Protease activated receptor 2 and the cardiovascular system. Br J Pharmacol 135: 14-20, 2002.
    • (2002) Br J Pharmacol , vol.135 , pp. 14-20
    • Cicala, C.1
  • 51
    • 0032910499 scopus 로고    scopus 로고
    • Bronchoconstrictor effect of thrombin and thrombin receptor activating peptide in guinea-pigs in vivo
    • Cicala C, Bucci M, De Dominicis G, Harriot P, Sorrentino L, and Cirino G. Bronchoconstrictor effect of thrombin and thrombin receptor activating peptide in guinea-pigs in vivo. Br J Pharmacol 126: 478-484, 1999.
    • (1999) Br J Pharmacol , vol.126 , pp. 478-484
    • Cicala, C.1    Bucci, M.2    De Dominicis, G.3    Harriot, P.4    Sorrentino, L.5    Cirino, G.6
  • 52
    • 0035378213 scopus 로고    scopus 로고
    • Pharmacological dissection of vascular effects caused by activation of protease-activated receptors 1 and 2 in anesthetized rats
    • Cicala C, Morello S, Santagada V, Caliendo G, Sorrentino L, and Cirino G. Pharmacological dissection of vascular effects caused by activation of protease-activated receptors 1 and 2 in anesthetized rats. FASEB J 15: 1433-1435, 2001.
    • (2001) FASEB J , vol.15 , pp. 1433-1435
    • Cicala, C.1    Morello, S.2    Santagada, V.3    Caliendo, G.4    Sorrentino, L.5    Cirino, G.6
  • 54
    • 0034194405 scopus 로고    scopus 로고
    • Inflammation-coagulation network: Are serine protease receptors the knot?
    • Cirino G, Bucci M, Cicala C, and Napoli C. Inflammation-coagulation network: are serine protease receptors the knot? Trends Pharmacol Sci 21: 170-172, 2000.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 170-172
    • Cirino, G.1    Bucci, M.2    Cicala, C.3    Napoli, C.4
  • 57
    • 0034161592 scopus 로고    scopus 로고
    • Protease-activated receptors: Sentries for inflammation?
    • Cocks TM and Moffatt JD. Protease-activated receptors: sentries for inflammation? Trends Pharmacol Sci 21: 103-108, 2000.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 103-108
    • Cocks, T.M.1    Moffatt, J.D.2
  • 58
    • 0034938379 scopus 로고    scopus 로고
    • Protease-activated receptor-2 (PAR2) in the airways
    • Cocks TM and Moffatt JD. Protease-activated receptor-2 (PAR2) in the airways. Pulm Pharmacol Ther 14: 183-191, 2001.
    • (2001) Pulm Pharmacol Ther , vol.14 , pp. 183-191
    • Cocks, T.M.1    Moffatt, J.D.2
  • 59
    • 0032971765 scopus 로고    scopus 로고
    • Protease-activated receptors mediate apamin-sensitive relaxation of mouse and guinea pig gastrointestinal smooth muscle
    • Cocks TM, Sozzi V, Moffatt JD, and Selemidis S. Protease-activated receptors mediate apamin-sensitive relaxation of mouse and guinea pig gastrointestinal smooth muscle. Gastroenterology 116: 586-592, 1999.
    • (1999) Gastroenterology , vol.116 , pp. 586-592
    • Cocks, T.M.1    Sozzi, V.2    Moffatt, J.D.3    Selemidis, S.4
  • 60
    • 0036207250 scopus 로고    scopus 로고
    • Proteinases and proteinase-activated receptor 2: A possible role to promote visceral hyperalgesia in rats
    • Coelho AM, Vergnolle N, Guiard B, Fioramonti J, and Bueno L. Proteinases and proteinase-activated receptor 2: a possible role to promote visceral hyperalgesia in rats. Gastroenterology 122: 1035-1047, 2002.
    • (2002) Gastroenterology , vol.122 , pp. 1035-1047
    • Coelho, A.M.1    Vergnolle, N.2    Guiard, B.3    Fioramonti, J.4    Bueno, L.5
  • 61
    • 0034671716 scopus 로고    scopus 로고
    • A polymorphic protease-activated receptor 2 (PAR2) displaying reduced sensitivity to trypsin and differential responses to PAR agonists
    • Compton SJ, Cairns JA, Palmer KJ, Al-Ani B, Hollenberg MD, and Walls AF. A polymorphic protease-activated receptor 2 (PAR2) displaying reduced sensitivity to trypsin and differential responses to PAR agonists. J Biol Chem 275: 39207-39212, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 39207-39212
    • Compton, S.J.1    Cairns, J.A.2    Palmer, K.J.3    Al-Ani, B.4    Hollenberg, M.D.5    Walls, A.F.6
  • 62
    • 0034748449 scopus 로고    scopus 로고
    • Glycosylation and the activation of proteinase-activated receptor 2 [PAR(2)] by human mast cell tryptase
    • Compton SJ, Renaux B, Wijesuriya SJ, and Hollenberg MD. Glycosylation and the activation of proteinase-activated receptor 2 [PAR(2)] by human mast cell tryptase. Br J Pharmacol 134: 705-718, 2001.
    • (2001) Br J Pharmacol , vol.134 , pp. 705-718
    • Compton, S.J.1    Renaux, B.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 63
    • 0036905071 scopus 로고    scopus 로고
    • Glycosylation of human proteinase-activated receptor-2 (hPAR2): Role in cell surface expression and signalling
    • Compton SJ, Sandhu S, Wijesuriya SJ, and Hollenberg MD. Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling. Biochem J 368: 495-505, 2002.
    • (2002) Biochem J , vol.368 , pp. 495-505
    • Compton, S.J.1    Sandhu, S.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 64
    • 0030008312 scopus 로고    scopus 로고
    • Role of the thrombin receptor in development and evidence for a second receptor
    • Connolly AJ, Ishihara H, Kahn ML, Farese RV Jr, and Coughlin SR. Role of the thrombin receptor in development and evidence for a second receptor. Nature 381: 516-519, 1996.
    • (1996) Nature , vol.381 , pp. 516-519
    • Connolly, A.J.1    Ishihara, H.2    Kahn, M.L.3    Farese Jr., R.V.4    Coughlin, S.R.5
  • 65
    • 0030703602 scopus 로고    scopus 로고
    • Mice lacking the thrombin receptor, PAR1 , have normal skin wound healing
    • Connolly AJ, Suh DY, Hunt TK, and Coughlin SR. Mice lacking the thrombin receptor, PAR1 , have normal skin wound healing. Am J Pathol 151: 1199-1204, 1997.
    • (1997) Am J Pathol , vol.151 , pp. 1199-1204
    • Connolly, A.J.1    Suh, D.Y.2    Hunt, T.K.3    Coughlin, S.R.4
  • 68
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin SR. Thrombin signalling and protease-activated receptors. Nature 407: 258-264, 2000.
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 69
    • 0037253347 scopus 로고    scopus 로고
    • PARticipation in inflammation
    • Coughlin SR and Camerer E. PARticipation in inflammation. J Clin Invest 111: 25-27, 2003.
    • (2003) J Clin Invest , vol.111 , pp. 25-27
    • Coughlin, S.R.1    Camerer, E.2
  • 70
    • 0034625055 scopus 로고    scopus 로고
    • Biphasic kinetics of activation and signaling for PAR1 and PAR4 thrombin receptors in platelets
    • Covic L, Gresser AL, and Kuliopulos A. Biphasic kinetics of activation and signaling for PAR1 and PAR4 thrombin receptors in platelets. Biochemistry 39: 5458-5467, 2000.
    • (2000) Biochemistry , vol.39 , pp. 5458-5467
    • Covic, L.1    Gresser, A.L.2    Kuliopulos, A.3
  • 71
    • 0037154270 scopus 로고    scopus 로고
    • Activation and inhibition of G protein-coupled receptors by cell-penetrating membrane-tethered peptides
    • Covic L, Gresser AL, Talavera J, Swift S, and Kuliopulos A. Activation and inhibition of G protein-coupled receptors by cell-penetrating membrane-tethered peptides. Proc Natl Acad Sci USA 99: 643-648, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 643-648
    • Covic, L.1    Gresser, A.L.2    Talavera, J.3    Swift, S.4    Kuliopulos, A.5
  • 72
    • 0036797590 scopus 로고    scopus 로고
    • Pepducin-based intervention of thrombin-receptor signaling and systemic platelet activation
    • Covic L, Misra M, Badar J, Singh C, and Kuliopulos A. Pepducin-based intervention of thrombin-receptor signaling and systemic platelet activation. Nat Med 8: 1161-1165, 2002.
    • (2002) Nat Med , vol.8 , pp. 1161-1165
    • Covic, L.1    Misra, M.2    Badar, J.3    Singh, C.4    Kuliopulos, A.5
  • 74
    • 0034745133 scopus 로고    scopus 로고
    • Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets
    • Cumashi A, Ansuini H, Celli N, De Blasi A, O'Brien PJ, Brass LF, and Molino M. Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets. Thromb Haemostasis 85: 533-538, 2001.
    • (2001) Thromb Haemostasis , vol.85 , pp. 533-538
    • Cumashi, A.1    Ansuini, H.2    Celli, N.3    De Blasi, A.4    O'Brien, P.J.5    Brass, L.F.6    Molino, M.7
  • 75
    • 0034614895 scopus 로고    scopus 로고
    • Protease-activated receptor 1 mediates thrombin-dependent cell-mediated renal inflammation in crescentic glomerulonephritis
    • Cunningham MA, Rondeau E, Chen X, Coughlin SR, Holdsworth SR, and Tipping PG. Protease-activated receptor 1 mediates thrombin-dependent, cell-mediated renal inflammation in crescentic glomerulonephritis. J Exp Med 191: 455-462, 2000.
    • (2000) J Exp Med , vol.191 , pp. 455-462
    • Cunningham, M.A.1    Rondeau, E.2    Chen, X.3    Coughlin, S.R.4    Holdsworth, S.R.5    Tipping, P.G.6
  • 76
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka Y, Luttrell LM, Ahn S, Della Rocca GJ, Ferguson SS, Caron MG, and Lefkowitz RJ. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J Biol Chem 273: 685-688, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3    Della Rocca, G.J.4    Ferguson, S.S.5    Caron, M.G.6    Lefkowitz, R.J.7
  • 78
    • 0034979246 scopus 로고    scopus 로고
    • Protease-activated receptor-2-mediated inhibition of ion transport in human bronchial epithelial cells
    • Danahay H, Withey L, Poll CT, van de Graaf SF, and Bridges RJ. Protease-activated receptor-2-mediated inhibition of ion transport in human bronchial epithelial cells. Am J Physiol Cell Physiol 280: C1455-C1464, 2001.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Danahay, H.1    Withey, L.2    Poll, C.T.3    Van De Graaf, S.F.4    Bridges, R.J.5
  • 80
    • 0034969753 scopus 로고    scopus 로고
    • Differential expression of protease-activated receptors-1 and -2 in stromal fibroblasts of normal, benign, and malignant human tissues
    • D'Andrea MR, Derian CK, Santulli RJ, and Andrade-Gordon P. Differential expression of protease-activated receptors-1 and -2 in stromal fibroblasts of normal, benign, and malignant human tissues. Am J Pathol 158: 2031-2041, 2001.
    • (2001) Am J Pathol , vol.158 , pp. 2031-2041
    • D'Andrea, M.R.1    Derian, C.K.2    Santulli, R.J.3    Andrade-Gordon, P.4
  • 81
    • 0037406817 scopus 로고    scopus 로고
    • Aberrant expression and activation of the thrombin receptor protease-activated receptor-1 induces cell proliferation and motility in human colon cancer cells
    • Darmoul D, Gratio V, Devaud H, Lehy T, and Laburthe M. Aberrant expression and activation of the thrombin receptor protease-activated receptor-1 induces cell proliferation and motility in human colon cancer cells. Am J Pathol 162: 1503-1513, 2003.
    • (2003) Am J Pathol , vol.162 , pp. 1503-1513
    • Darmoul, D.1    Gratio, V.2    Devaud, H.3    Lehy, T.4    Laburthe, M.5
  • 82
    • 0035444796 scopus 로고    scopus 로고
    • Initiation of human colon cancer cell proliferation by trypsin acting at protease-activated receptor-2
    • Darmoul D, Marie JC, Devaud H, Gratio V, and Laburthe M. Initiation of human colon cancer cell proliferation by trypsin acting at protease-activated receptor-2. Br J Cancer 85: 772-779, 2001.
    • (2001) Br J Cancer , vol.85 , pp. 772-779
    • Darmoul, D.1    Marie, J.C.2    Devaud, H.3    Gratio, V.4    Laburthe, M.5
  • 84
    • 0035895962 scopus 로고    scopus 로고
    • Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets
    • De Candia E, Hall SW, Rutella S, Landolfi R, Andrews RK, and De Cristofaro R. Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets. J Biol Chem 276: 4692-4698, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4692-4698
    • De Candia, E.1    Hall, S.W.2    Rutella, S.3    Landolfi, R.4    Andrews, R.K.5    De Cristofaro, R.6
  • 85
    • 0033850541 scopus 로고    scopus 로고
    • Mechanisms of initiation and termination of signalling by neuropeptide receptors: A comparison with the proteinase-activated receptors
    • Defea K, Schmidlin F, Dery O, Grady EF, and Bunnett NW. Mechanisms of initiation and termination of signalling by neuropeptide receptors: a comparison with the proteinase-activated receptors. Biochem Soc Trans 28: 419-426, 2000.
    • (2000) Biochem Soc Trans , vol.28 , pp. 419-426
    • Defea, K.1    Schmidlin, F.2    Dery, O.3    Grady, E.F.4    Bunnett, N.W.5
  • 86
    • 0034689003 scopus 로고    scopus 로고
    • Beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea KA, Zalevsky J, Thoma MS, Dery O, Mullins RD, and Bunnett NW. Beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J Cell Biol 148: 1267-1281, 2000.
    • (2000) J Cell Biol , vol.148 , pp. 1267-1281
    • DeFea, K.A.1    Zalevsky, J.2    Thoma, M.S.3    Dery, O.4    Mullins, R.D.5    Bunnett, N.W.6
  • 88
  • 89
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery O, Corvera CU, Steinhoff M, and Bunnett NW. Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. Am J Physiol Cell Physiol 274: C1429-C1452, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.274
    • Dery, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 90
    • 0039843091 scopus 로고    scopus 로고
    • Trafficking of proteinase-activated receptor-2 and beta-arrestin-1 tagged with green fluorescent protein. Beta-arrestin-dependent endocytosis of a proteinase receptor
    • Dery O, Thoma MS, Wong H, Grady EF, and Bunnett NW. Trafficking of proteinase-activated receptor-2 and beta-arrestin-1 tagged with green fluorescent protein. beta-Arrestin-dependent endocytosis of a proteinase receptor. J Biol Chem 274: 18524-18535, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 18524-18535
    • Dery, O.1    Thoma, M.S.2    Wong, H.3    Grady, E.F.4    Bunnett, N.W.5
  • 91
  • 92
    • 0032557654 scopus 로고    scopus 로고
    • Signaling pathways involved in thrombin-induced cell protection
    • Donovan FM and Cunningham DD. Signaling pathways involved in thrombin-induced cell protection. J Biol Chem 273: 12746-12752, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12746-12752
    • Donovan, F.M.1    Cunningham, D.D.2
  • 93
    • 16944366731 scopus 로고    scopus 로고
    • Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities
    • Donovan FM, Pike CJ, Cotman CW, and Cunningham DD. Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities. J Neurosci 17: 5316-5326, 1997.
    • (1997) J Neurosci , vol.17 , pp. 5316-5326
    • Donovan, F.M.1    Pike, C.J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 94
    • 0037040042 scopus 로고    scopus 로고
    • Trypsin is produced by and activates protease-activated receptor-2 in human cancer colon cells: Evidence for new autocrine loop
    • Ducroc R, Bontemps C, Marazova K, Devaud H, Darmoul D, and Laburthe M. Trypsin is produced by and activates protease-activated receptor-2 in human cancer colon cells: evidence for new autocrine loop. Life Sci 70: 1359-1367, 2002.
    • (2002) Life Sci , vol.70 , pp. 1359-1367
    • Ducroc, R.1    Bontemps, C.2    Marazova, K.3    Devaud, H.4    Darmoul, D.5    Laburthe, M.6
  • 95
    • 0037372534 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2 and human lung epithelial cells: Disarming by neutrophil serine proteinases
    • Dulon S, Cande C, Bunnett NW, Hollenberg MD, Chignard M, and Pidard D. Proteinase-activated receptor-2 and human lung epithelial cells: disarming by neutrophil serine proteinases. Am J Respir Cell Mol Biol 28: 339-346, 2003.
    • (2003) Am J Respir Cell Mol Biol , vol.28 , pp. 339-346
    • Dulon, S.1    Cande, C.2    Bunnett, N.W.3    Hollenberg, M.D.4    Chignard, M.5    Pidard, D.6
  • 96
    • 0034128648 scopus 로고    scopus 로고
    • Stratum corneum tryptic enzyme in normal epidermis: A missing link in the desquamation process?
    • Ekholm IE, Brattsand M, and Egelrud T. Stratum corneum tryptic enzyme in normal epidermis: a missing link in the desquamation process? J Invest Dermatol 114: 56-63, 2000.
    • (2000) J Invest Dermatol , vol.114 , pp. 56-63
    • Ekholm, I.E.1    Brattsand, M.2    Egelrud, T.3
  • 98
    • 0034733558 scopus 로고    scopus 로고
    • Structure-function analysis of protease-activated receptor 4 tethered ligand peptides. Determinants of specificity and utility in assays of receptor function
    • Faruqi TR, Weiss EJ, Shapiro MJ, Huang W, and Coughlin SR. Structure-function analysis of protease-activated receptor 4 tethered ligand peptides. Determinants of specificity and utility in assays of receptor function. J Biol Chem 275: 19728-19734, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 19728-19734
    • Faruqi, T.R.1    Weiss, E.J.2    Shapiro, M.J.3    Huang, W.4    Coughlin, S.R.5
  • 99
    • 0028068960 scopus 로고
    • A Chinese hamster fibroblast mutant defective in thrombin-induced signaling has a low level of phospholipase C-beta 1
    • Fee JA, Monsey JD, Handler RJ, Leonis MA, Mullaney SR, Hope HM, and Silbert DF. A Chinese hamster fibroblast mutant defective in thrombin-induced signaling has a low level of phospholipase C-beta 1. J Biol Chem 269: 21699-21708, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 21699-21708
    • Fee, J.A.1    Monsey, J.D.2    Handler, R.J.3    Leonis, M.A.4    Mullaney, S.R.5    Hope, H.M.6    Silbert, D.F.7
  • 102
    • 0030007646 scopus 로고    scopus 로고
    • Thrombin, its receptor and protease nexin I, its potent serpin, in the nervous system
    • Festoff BW, Smirnova IV, Ma J, and Citron BA. Thrombin, its receptor and protease nexin I, its potent serpin, in the nervous system. Semin Thromb Hemost 22: 267-271, 1996.
    • (1996) Semin Thromb Hemost , vol.22 , pp. 267-271
    • Festoff, B.W.1    Smirnova, I.V.2    Ma, J.3    Citron, B.A.4
  • 104
    • 0036828264 scopus 로고    scopus 로고
    • Serine proteases excite myenteric neurons through protease-activated receptors in guinea pig small intestine
    • Gao C, Liu S, Hu HZ, Gao N, Kim GY, Xia Y, and Wood JD. Serine proteases excite myenteric neurons through protease-activated receptors in guinea pig small intestine. Gastroenterology 123: 1554-1564, 2002.
    • (2002) Gastroenterology , vol.123 , pp. 1554-1564
    • Gao, C.1    Liu, S.2    Hu, H.Z.3    Gao, N.4    Kim, G.Y.5    Xia, Y.6    Wood, J.D.7
  • 106
    • 0032578046 scopus 로고    scopus 로고
    • Thrombin induced inhibition of neurite outgrowth from dorsal root ganglion neurons
    • Gill JS, Pitts K, Rusnak FM, Owen WG, and Windebank AJ. Thrombin induced inhibition of neurite outgrowth from dorsal root ganglion neurons. Brain Res 797: 321-327, 1998.
    • (1998) Brain Res , vol.797 , pp. 321-327
    • Gill, J.S.1    Pitts, K.2    Rusnak, F.M.3    Owen, W.G.4    Windebank, A.J.5
  • 107
    • 0034660448 scopus 로고    scopus 로고
    • Potentiation of NMDA receptor function by the serine protease thrombin
    • Gingrich MB, Junge CE, Lyuboslavsky P, and Traynelis SF. Potentiation of NMDA receptor function by the serine protease thrombin. J Neurosci 20: 4582-4595, 2000.
    • (2000) J Neurosci , vol.20 , pp. 4582-4595
    • Gingrich, M.B.1    Junge, C.E.2    Lyuboslavsky, P.3    Traynelis, S.F.4
  • 108
    • 0030032791 scopus 로고    scopus 로고
    • Cellular consequences of thrombin-receptor activation
    • Grand RJ, Turnell AS, and Grabham PW. Cellular consequences of thrombin-receptor activation. Biochem J 313: 353-368, 1996.
    • (1996) Biochem J , vol.313 , pp. 353-368
    • Grand, R.J.1    Turnell, A.S.2    Grabham, P.W.3
  • 109
    • 0033798625 scopus 로고    scopus 로고
    • Intestinal type 2 proteinase-activated receptors: Expression in opioid-sensitive secretomotor neural circuits that mediate epithelial ion transport
    • Green BT, Bunnett NW, Kulkarni-Narla A, Steinhoff M, and Brown DR. Intestinal type 2 proteinase-activated receptors: expression in opioid-sensitive secretomotor neural circuits that mediate epithelial ion transport. J Pharmacol Exp Ther 295: 410-416, 2000.
    • (2000) J Pharmacol Exp Ther , vol.295 , pp. 410-416
    • Green, B.T.1    Bunnett, N.W.2    Kulkarni-Narla, A.3    Steinhoff, M.4    Brown, D.R.5
  • 110
    • 0035979691 scopus 로고    scopus 로고
    • A role for thrombin receptor signaling in endothelial cells during embryonic development
    • Griffin CT, Srinivasan Y, Zheng YW, Huang W, and Coughlin SR. A role for thrombin receptor signaling in endothelial cells during embryonic development. Science 293: 1666-1670, 2001.
    • (2001) Science , vol.293 , pp. 1666-1670
    • Griffin, C.T.1    Srinivasan, Y.2    Zheng, Y.W.3    Huang, W.4    Coughlin, S.R.5
  • 111
    • 0035992710 scopus 로고    scopus 로고
    • Activated protein C: Potential therapy for severe sepsis, thrombosis, and stroke
    • Griffin JH, Zlokovic B, and Fernandez JA. Activated protein C: potential therapy for severe sepsis, thrombosis, and stroke. Semin Hematol 39: 197-205, 2002.
    • (2002) Semin Hematol , vol.39 , pp. 197-205
    • Griffin, J.H.1    Zlokovic, B.2    Fernandez, J.A.3
  • 112
    • 0011811083 scopus 로고
    • Thrombin modulates and reverses neuroblastoma neurite outgrowth
    • Gurwitz D and Cunningham DD. Thrombin modulates and reverses neuroblastoma neurite outgrowth. Proc Natl Acad Sci USA 85: 3440-3444, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3440-3444
    • Gurwitz, D.1    Cunningham, D.D.2
  • 113
    • 0032993174 scopus 로고    scopus 로고
    • Protease-activated receptor-2 turnover stimulated independently of receptor activation in porcine coronary endothelial cells
    • Hamilton JR, Chow JM, and Cocks TM. Protease-activated receptor-2 turnover stimulated independently of receptor activation in porcine coronary endothelial cells. Br J Pharmacol 127: 617-622, 1999.
    • (1999) Br J Pharmacol , vol.127 , pp. 617-622
    • Hamilton, J.R.1    Chow, J.M.2    Cocks, T.M.3
  • 114
    • 0034019115 scopus 로고    scopus 로고
    • Heterogeneous mechanisms of endothelium-dependent relaxation for thrombin and peptide activators of protease-activated receptor-1 in porcine isolated coronary artery
    • Hamilton JR and Cocks TM. Heterogeneous mechanisms of endothelium-dependent relaxation for thrombin and peptide activators of protease-activated receptor-1 in porcine isolated coronary artery. Br J Pharmacol 130: 181-188, 2000.
    • (2000) Br J Pharmacol , vol.130 , pp. 181-188
    • Hamilton, J.R.1    Cocks, T.M.2
  • 115
    • 0035816730 scopus 로고    scopus 로고
    • Increased expression of protease-activated receptor-2 (par2) and par4 in human coronary artery by inflammatory stimuli unveils endothelium-dependent relaxations to par2 and par4 agonists
    • Hamilton JR, Frauman AG, and Cocks TM. Increased expression of protease-activated receptor-2 (par2) and par4 in human coronary artery by inflammatory stimuli unveils endothelium-dependent relaxations to par2 and par4 agonists. Circ Res 89: 92-98, 2001.
    • (2001) Circ Res , vol.89 , pp. 92-98
    • Hamilton, J.R.1    Frauman, A.G.2    Cocks, T.M.3
  • 116
    • 0034936715 scopus 로고    scopus 로고
    • Protease-activated receptor (PAR) 1 but not PAR2 or PAR4 mediates endothelium-dependent relaxation to thrombin and trypsin in human pulmonary arteries
    • Hamilton JR, Moffatt JD, Frauman AG, and Cocks TM. Protease-activated receptor (PAR) 1 but not PAR2 or PAR4 mediates endothelium-dependent relaxation to thrombin and trypsin in human pulmonary arteries. J Cardiovasc Pharmacol 38: 108-119, 2001.
    • (2001) J Cardiovasc Pharmacol , vol.38 , pp. 108-119
    • Hamilton, J.R.1    Moffatt, J.D.2    Frauman, A.G.3    Cocks, T.M.4
  • 117
    • 0035984932 scopus 로고    scopus 로고
    • Enzymatic activation of endothelial protease-activated receptors is dependent on artery diameter in human and porcine isolated coronary arteries
    • Hamilton JR, Moffatt JD, Tatoulis J, and Cocks TM. Enzymatic activation of endothelial protease-activated receptors is dependent on artery diameter in human and porcine isolated coronary arteries. Br J Pharmacol 136: 492-501, 2002.
    • (2002) Br J Pharmacol , vol.136 , pp. 492-501
    • Hamilton, J.R.1    Moffatt, J.D.2    Tatoulis, J.3    Cocks, T.M.4
  • 118
    • 0033534612 scopus 로고    scopus 로고
    • The platelet high affinity binding site for thrombin mimics hirudin, modulates thrombin-induced platelet activation, and is distinct from the glycoprotein Ib-IX-V complex
    • Hayes KL and Tracy PB. The platelet high affinity binding site for thrombin mimics hirudin, modulates thrombin-induced platelet activation, and is distinct from the glycoprotein Ib-IX-V complex. J Biol Chem 274: 972-980, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 972-980
    • Hayes, K.L.1    Tracy, P.B.2
  • 119
    • 0031573586 scopus 로고    scopus 로고
    • Potent induction of a neutrophil and eosinophil-rich infiltrate in vivo by human mast cell tryptase: Selective enhancement of eosinophil recruitment by histamine
    • He S, Peng Q, and Walls AF. Potent induction of a neutrophil and eosinophil-rich infiltrate in vivo by human mast cell tryptase: selective enhancement of eosinophil recruitment by histamine. J Immunol 159: 6216-6225, 1997.
    • (1997) J Immunol , vol.159 , pp. 6216-6225
    • He, S.1    Peng, Q.2    Walls, A.F.3
  • 120
    • 0030940777 scopus 로고    scopus 로고
    • Human mast cell tryptase: A stimulus of microvascular leakage and mast cell activation
    • He S and Walls AF. Human mast cell tryptase: a stimulus of microvascular leakage and mast cell activation. Eur J Pharmacol 328: 89-97, 1997.
    • (1997) Eur J Pharmacol , vol.328 , pp. 89-97
    • He, S.1    Walls, A.F.2
  • 121
    • 0028053488 scopus 로고
    • Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor
    • Hein L, Ishii K, Coughlin SR, and Kobilka BK. Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor. J Biol Chem 269: 27719-27726, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 27719-27726
    • Hein, L.1    Ishii, K.2    Coughlin, S.R.3    Kobilka, B.K.4
  • 123
    • 0030823980 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Structural requirements for activity, receptor cross-reactivity, and receptor selectivity of receptor-activating peptides
    • Hollenberg MD, Saifeddine M, al-Ani B, and Kawabata A. Proteinase-activated receptors: structural requirements for activity, receptor cross-reactivity, and receptor selectivity of receptor-activating peptides. Can J Physiol Pharmacol 75: 832-841, 1997.
    • (1997) Can J Physiol Pharmacol , vol.75 , pp. 832-841
    • Hollenberg, M.D.1    Saifeddine, M.2    Al-Ani, B.3    Kawabata, A.4
  • 125
    • 0028959546 scopus 로고
    • The functional thrombin receptor is associated with the plasmalemma and a large endosomal network in cultured human umbilical vein endothelial cells
    • Horvat R and Palade GE. The functional thrombin receptor is associated with the plasmalemma and a large endosomal network in cultured human umbilical vein endothelial cells. J Cell Sci 108: 1155-1164, 1995.
    • (1995) J Cell Sci , vol.108 , pp. 1155-1164
    • Horvat, R.1    Palade, G.E.2
  • 126
    • 0031855366 scopus 로고    scopus 로고
    • Immunolocalization of protease-activated receptor-2 in skin: Receptor activation stimulates interleukin-8 secretion by keratinocytes in vitro
    • Hou L, Kapas S, Cruchley AT, Macey MG, Harriott P, Chinni C, Stone SR, and Howells GL. Immunolocalization of protease-activated receptor-2 in skin: receptor activation stimulates interleukin-8 secretion by keratinocytes in vitro. Immunology 94: 356-362, 1998.
    • (1998) Immunology , vol.94 , pp. 356-362
    • Hou, L.1    Kapas, S.2    Cruchley, A.T.3    Macey, M.G.4    Harriott, P.5    Chinni, C.6    Stone, S.R.7    Howells, G.L.8
  • 127
    • 0036549805 scopus 로고    scopus 로고
    • Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis
    • Howell DC, Laurent GJ, and Chambers RC. Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis. Biochem Soc Trans 30: 211-216, 2002.
    • (2002) Biochem Soc Trans , vol.30 , pp. 211-216
    • Howell, D.C.1    Laurent, G.J.2    Chambers, R.C.3
  • 130
    • 0035854794 scopus 로고    scopus 로고
    • Evaluation of the substrate specificity of human mast cell tryptase beta I and demonstration of its importance in bacterial infections of the lung
    • Huang C, De Sanctis GT, O'Brien PJ, Mizgerd JP, Friend DS, Drazen JM, Brass LF, and Stevens RL. Evaluation of the substrate specificity of human mast cell tryptase beta I and demonstration of its importance in bacterial infections of the lung. J Biol Chem 276: 26276-26284, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 26276-26284
    • Huang, C.1    De Sanctis, G.T.2    O'Brien, P.J.3    Mizgerd, J.P.4    Friend, D.S.5    Drazen, J.M.6    Brass, L.F.7    Stevens, R.L.8
  • 131
    • 0026504693 scopus 로고
    • Thrombin-induced events in non-platelet cells are mediated by the unique proteolytic mechanism established for the cloned platelet thrombin receptor
    • Hung DT, Vu TH, Nelken NA, and Coughlin SR. Thrombin-induced events in non-platelet cells are mediated by the unique proteolytic mechanism established for the cloned platelet thrombin receptor. J Cell Biol 116: 827-832, 1992.
    • (1992) J Cell Biol , vol.116 , pp. 827-832
    • Hung, D.T.1    Vu, T.H.2    Nelken, N.A.3    Coughlin, S.R.4
  • 132
    • 0026782001 scopus 로고
    • The cloned platelet thrombin receptor couples to at least two distinct effectors to stimulate phosphoinositide hydrolysis and inhibit adenylyl cyclase
    • Hung DT, Wong YH, Vu TK, and Coughlin SR. The cloned platelet thrombin receptor couples to at least two distinct effectors to stimulate phosphoinositide hydrolysis and inhibit adenylyl cyclase. J Biol Chem 267: 20831-20834, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 20831-20834
    • Hung, D.T.1    Wong, Y.H.2    Vu, T.K.3    Coughlin, S.R.4
  • 136
    • 0028009801 scopus 로고
    • Inhibition of thrombin receptor signaling by a G-protein coupled receptor kinase. Functional specificity among G-protein coupled receptor kinases
    • Ishii K, Chen J, Ishii M, Koch WJ, Freedman NJ, Lefkowitz RJ, and Coughlin SR. Inhibition of thrombin receptor signaling by a G-protein coupled receptor kinase. Functional specificity among G-protein coupled receptor kinases. J Biol Chem 269: 1125-1130, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1125-1130
    • Ishii, K.1    Chen, J.2    Ishii, M.3    Koch, W.J.4    Freedman, N.J.5    Lefkowitz, R.J.6    Coughlin, S.R.7
  • 137
    • 0027309290 scopus 로고
    • Kinetics of thrombin receptor cleavage on intact cells. Relation to signaling
    • Ishii K, Hein L, Kobilka B, and Coughlin SR. Kinetics of thrombin receptor cleavage on intact cells. Relation to signaling. J Biol Chem 268: 9780-9786, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 9780-9786
    • Ishii, K.1    Hein, L.2    Kobilka, B.3    Coughlin, S.R.4
  • 138
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink K, van Corven EJ, Hengeveld T, Morii N, Narumiya S, and Moolenaar WH. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J Cell Biol 126: 801-810, 1994.
    • (1994) J Cell Biol , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 139
    • 0025913012 scopus 로고
    • Elevated bronchoalveolar lavage fluid histamine levels in allergic asthmatics are associated with increased airway obstruction
    • Jarjour NN, Calhoun WJ, Schwartz LB, and Busse WW. Elevated bronchoalveolar lavage fluid histamine levels in allergic asthmatics are associated with increased airway obstruction. Am Rev Respir Dis 144: 83-87, 1991.
    • (1991) Am Rev Respir Dis , vol.144 , pp. 83-87
    • Jarjour, N.N.1    Calhoun, W.J.2    Schwartz, L.B.3    Busse, W.W.4
  • 140
    • 0037303494 scopus 로고    scopus 로고
    • Protease-activated receptor (PAR)-1 and PAR-2 participate in the cell growth of alveolar capillary endothelium in primary lung adenocarcinomas
    • Jin E, Fujiwara M, Pan X, Ghazizadeh M, Arai S, Ohaki Y, Kajiwara K, Takemura T, and Kawanami O. Protease-activated receptor (PAR)-1 and PAR-2 participate in the cell growth of alveolar capillary endothelium in primary lung adenocarcinomas. Cancer 97: 703-713, 2003.
    • (2003) Cancer , vol.97 , pp. 703-713
    • Jin, E.1    Fujiwara, M.2    Pan, X.3    Ghazizadeh, M.4    Arai, S.5    Ohaki, Y.6    Kajiwara, K.7    Takemura, T.8    Kawanami, O.9
  • 141
    • 0035855860 scopus 로고    scopus 로고
    • Molecular mechanisms of nociception
    • Julius D and Basbaum AI. Molecular mechanisms of nociception. Nature 413: 203-210, 2001.
    • (2001) Nature , vol.413 , pp. 203-210
    • Julius, D.1    Basbaum, A.I.2
  • 142
  • 144
    • 0035421226 scopus 로고    scopus 로고
    • Signaling from protease-activated receptor-1 inhibits migration and invasion of breast cancer cells
    • Kamath L, Meydani A, Foss F, and Kuliopulos A. Signaling from protease-activated receptor-1 inhibits migration and invasion of breast cancer cells. Cancer Res 61: 5933-5940, 2001.
    • (2001) Cancer Res , vol.61 , pp. 5933-5940
    • Kamath, L.1    Meydani, A.2    Foss, F.3    Kuliopulos, A.4
  • 145
    • 1642340462 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory kappa B kinases in NCTC 2544 keratinocytes
    • Kanke T, Macfarlane SR, Seatter MJ, Davenport E, Paul A, McKenzie R, and Plevin R. Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory kappa B kinases in NCTC 2544 keratinocytes. J Biol Chem 18: 18, 2001.
    • (2001) J Biol Chem , vol.18 , pp. 18
    • Kanke, T.1    Macfarlane, S.R.2    Seatter, M.J.3    Davenport, E.4    Paul, A.5    McKenzie, R.6    Plevin, R.7
  • 146
    • 0036304291 scopus 로고    scopus 로고
    • Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
    • Katona G, Berglund GI, Hajdu J, Graf L, and Szilagyi L. Crystal structure reveals basis for the inhibitor resistance of human brain trypsin. J Mol Biol 315: 1209-1218, 2002.
    • (2002) J Mol Biol , vol.315 , pp. 1209-1218
    • Katona, G.1    Berglund, G.I.2    Hajdu, J.3    Graf, L.4    Szilagyi, L.5
  • 147
    • 0033933005 scopus 로고    scopus 로고
    • Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production
    • Kauffman HF, Tomee JF, van de Riet MA, Timmerman AJ, and Borger P. Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production. J Allergy Clin Immunol 105: 1185-1193, 2000.
    • (2000) J Allergy Clin Immunol , vol.105 , pp. 1185-1193
    • Kauffman, H.F.1    Tomee, J.F.2    Van De Riet, M.A.3    Timmerman, A.J.4    Borger, P.5
  • 149
    • 0037171067 scopus 로고    scopus 로고
    • Specific expression of spinal Fos after PAR-2 stimulation in most cell-depleted rats
    • Kawabata A, Kawao N, Kuroda R, Itoh H, and Nishikawa H. Specific expression of spinal Fos after PAR-2 stimulation in most cell-depleted rats. Neuroreport 13: 511-514, 2002.
    • (2002) Neuroreport , vol.13 , pp. 511-514
    • Kawabata, A.1    Kawao, N.2    Kuroda, R.3    Itoh, H.4    Nishikawa, H.5
  • 150
    • 0035953151 scopus 로고    scopus 로고
    • Peripheral PAR-2 triggers thermal hyperalgesia and nociceptive responses in rats
    • Kawabata A, Kawao N, Kuroda R, Tanaka A, Itoh H, and Nishikawa H. Peripheral PAR-2 triggers thermal hyperalgesia and nociceptive responses in rats. Neuroreport 12: 715-719, 2001.
    • (2001) Neuroreport , vol.12 , pp. 715-719
    • Kawabata, A.1    Kawao, N.2    Kuroda, R.3    Tanaka, A.4    Itoh, H.5    Nishikawa, H.6
  • 151
    • 0035996861 scopus 로고    scopus 로고
    • The PAR-1-activating peptide attenuates carrageenan-induced hyperalgesia in rats
    • Kawabata A, Kawao N, Kuroda R, Tanaka A, and Shimada C. The PAR-1-activating peptide attenuates carrageenan-induced hyperalgesia in rats. Peptides 23: 1181-1183, 2002.
    • (2002) Peptides , vol.23 , pp. 1181-1183
    • Kawabata, A.1    Kawao, N.2    Kuroda, R.3    Tanaka, A.4    Shimada, C.5
  • 152
    • 0036122072 scopus 로고    scopus 로고
    • Capsazepine partially inhibits neurally mediated gastric mucus secretion following activation of protease-activated receptor 2
    • Kawabata A, Kinoshita M, Kuroda R, and Kakehi K. Capsazepine partially inhibits neurally mediated gastric mucus secretion following activation of protease-activated receptor 2. Clin Exp Pharmacol Physiol 29: 360-361, 2002.
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , pp. 360-361
    • Kawabata, A.1    Kinoshita, M.2    Kuroda, R.3    Kakehi, K.4
  • 154
    • 0033771536 scopus 로고    scopus 로고
    • Dual modulation by thrombin of the motility of rat oesophageal muscularis mucosae via two distinct protease-activated receptors (PARs): A novel role for PAR-4 as opposed to PAR-1
    • Kawabata A, Kuroda R, Kuroki N, Nishikawa H, and Kawai K. Dual modulation by thrombin of the motility of rat oesophageal muscularis mucosae via two distinct protease-activated receptors (PARs): a novel role for PAR-4 as opposed to PAR-1. Br J Pharmacol 131: 578-584, 2000.
    • (2000) Br J Pharmacol , vol.131 , pp. 578-584
    • Kawabata, A.1    Kuroda, R.2    Kuroki, N.3    Nishikawa, H.4    Kawai, K.5
  • 155
    • 0034872420 scopus 로고    scopus 로고
    • In vivo evidence that protease-activated receptors 1 and 2 modulate gastrointestinal transit in the mouse
    • Kawabata A, Kuroda R, Nagata N, Kawao N, Masuko T, Nishikawa H, and Kawai K. In vivo evidence that protease-activated receptors 1 and 2 modulate gastrointestinal transit in the mouse. Br J Pharmacol 133: 1213-1218, 2001.
    • (2001) Br J Pharmacol , vol.133 , pp. 1213-1218
    • Kawabata, A.1    Kuroda, R.2    Nagata, N.3    Kawao, N.4    Masuko, T.5    Nishikawa, H.6    Kawai, K.7
  • 156
    • 0037019916 scopus 로고    scopus 로고
    • Protease-activated receptor-2 (PAR-2) in the pancreas and parotid gland: Immunolocalization and involvement of nitric oxide in the evoked amylase secretion
    • Kawabata A, Kuroda R, Nishida M, Nagata N, Sakaguchi Y, Kawao N, Nishikawa H, Arizono N, and Kawai K. Protease-activated receptor-2 (PAR-2) in the pancreas and parotid gland: immunolocalization and involvement of nitric oxide in the evoked amylase secretion. Life Sci 71: 2435-2446, 2002.
    • (2002) Life Sci , vol.71 , pp. 2435-2446
    • Kawabata, A.1    Kuroda, R.2    Nishida, M.3    Nagata, N.4    Sakaguchi, Y.5    Kawao, N.6    Nishikawa, H.7    Arizono, N.8    Kawai, K.9
  • 157
    • 0034595060 scopus 로고    scopus 로고
    • Activation of protease-activated receptor-2 (PAR-2) triggers mucin secretion in the rat sublingual gland
    • Kawabata A, Morimoto N, Nishikawa H, Kuroda R, Oda Y, and Kakehi K. Activation of protease-activated receptor-2 (PAR-2) triggers mucin secretion in the rat sublingual gland. Biochem Biophys Res Commun 270: 298-302, 2000.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 298-302
    • Kawabata, A.1    Morimoto, N.2    Nishikawa, H.3    Kuroda, R.4    Oda, Y.5    Kakehi, K.6
  • 158
    • 0033997882 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2 (PAR-2): Regulation of salivary and pancreatic exocrine secretion in vivo in rats and mice
    • Kawabata A, Nishikawa H, Kuroda R, Kawai K, and Hollenberg MD. Proteinase-activated receptor-2 (PAR-2): regulation of salivary and pancreatic exocrine secretion in vivo in rats and mice. Br J Pharmacol 129: 1808-1814, 2000.
    • (2000) Br J Pharmacol , vol.129 , pp. 1808-1814
    • Kawabata, A.1    Nishikawa, H.2    Kuroda, R.3    Kawai, K.4    Hollenberg, M.D.5
  • 161
    • 0036292747 scopus 로고    scopus 로고
    • Thrombin-stimulated Pyk2 phosphorylation in human endothelium is dependent on intracellular calcium and independent of protein kinase C and Src kinases
    • Keogh RJ, Houliston RA, and Wheeler-Jones CP. Thrombin-stimulated Pyk2 phosphorylation in human endothelium is dependent on intracellular calcium and independent of protein kinase C and Src kinases. Biochem Biophys Res Commun 294: 1001-1008, 2002.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 1001-1008
    • Keogh, R.J.1    Houliston, R.A.2    Wheeler-Jones, C.P.3
  • 162
    • 0032193198 scopus 로고    scopus 로고
    • Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium
    • King C, Brennan S, Thompson PJ, and Stewart GA. Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium. J Immunol 161: 3645-3651, 1998.
    • (1998) J Immunol , vol.161 , pp. 3645-3651
    • King, C.1    Brennan, S.2    Thompson, P.J.3    Stewart, G.A.4
  • 163
    • 0033593667 scopus 로고    scopus 로고
    • Activation of G12/G13 results in shape change and Rho/ Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets
    • Klages B, Brandt U, Simon MI, Schultz G, and Offermanns S. Activation of G12/G13 results in shape change and Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets. J Cell Biol 144: 745-754, 1999.
    • (1999) J Cell Biol , vol.144 , pp. 745-754
    • Klages, B.1    Brandt, U.2    Simon, M.I.3    Schultz, G.4    Offermanns, S.5
  • 164
    • 0035184146 scopus 로고    scopus 로고
    • Protease-activated receptors in human airways: Upregulation of PAR-2 in respiratory epithelium from patients with asthma
    • Knight DA, Lim S, Scaffidi AK, Roche N, Chung KF, Stewart GA, and Thompson PJ. Protease-activated receptors in human airways: upregulation of PAR-2 in respiratory epithelium from patients with asthma. J Allergy Clin Immunol 108: 797-803, 2001.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 797-803
    • Knight, D.A.1    Lim, S.2    Scaffidi, A.K.3    Roche, N.4    Chung, K.F.5    Stewart, G.A.6    Thompson, P.J.7
  • 165
    • 0024346947 scopus 로고
    • Human ovarian tumor-associated trypsin. Its purification and characterization from mucinous cyst fluid and identification as an activator of pro-urokinase
    • Koivunen E, Huhtala ML, and Stenman UH. Human ovarian tumor-associated trypsin. Its purification and characterization from mucinous cyst fluid and identification as an activator of pro-urokinase. J Biol Chem 264: 14095-14099, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 14095-14099
    • Koivunen, E.1    Huhtala, M.L.2    Stenman, U.H.3
  • 166
    • 0026080403 scopus 로고
    • Human colonic carcinoma, fibrosarcoma and leukemia cell lines produce tumor-associated trypsinogen
    • Koivunen E, Saksela O, Itkonen O, Osman S, Huhtala ML, and Stenman UH. Human colonic carcinoma, fibrosarcoma and leukemia cell lines produce tumor-associated trypsinogen. Int J Cancer 47: 592-596, 1991.
    • (1991) Int J Cancer , vol.47 , pp. 592-596
    • Koivunen, E.1    Saksela, O.2    Itkonen, O.3    Osman, S.4    Huhtala, M.L.5    Stenman, U.H.6
  • 171
    • 0036357203 scopus 로고    scopus 로고
    • Ion transport induced by proteinase-activated receptors (PAR2) in colon and airways
    • Kunzelmann K, Schreiber R, Konig J, and Mall M. Ion transport induced by proteinase-activated receptors (PAR2) in colon and airways. Cell Biochem Biophys 36: 209-214, 2002.
    • (2002) Cell Biochem Biophys , vol.36 , pp. 209-214
    • Kunzelmann, K.1    Schreiber, R.2    Konig, J.3    Mall, M.4
  • 172
    • 0035146812 scopus 로고    scopus 로고
    • Role of PGE(2) in protease-activated receptor-1, -2 and -4 mediated relaxation in the mouse isolated trachea
    • Lan RS, Knight DA, Stewart GA, and Henry PJ. Role of PGE(2) in protease-activated receptor-1, -2 and -4 mediated relaxation in the mouse isolated trachea. Br J Pharmacol 132: 93-100, 2001.
    • (2001) Br J Pharmacol , vol.132 , pp. 93-100
    • Lan, R.S.1    Knight, D.A.2    Stewart, G.A.3    Henry, P.J.4
  • 173
    • 0006296520 scopus 로고    scopus 로고
    • Modulation of airway smooth muscle tone by protease activated receptor- 1,-2,-3 and -4 in trachea isolated from influenza A virus-infected mice
    • Lan RS, Stewart GA, and Henry PJ. Modulation of airway smooth muscle tone by protease activated receptor- 1,-2,-3 and -4 in trachea isolated from influenza A virus-infected mice. Br J Pharmacol 129: 63-70, 2000.
    • (2000) Br J Pharmacol , vol.129 , pp. 63-70
    • Lan, R.S.1    Stewart, G.A.2    Henry, P.J.3
  • 174
    • 0020557296 scopus 로고
    • Thrombin-induced gap formation in confluent endothelial cell monolayers in vitro
    • Laposata M, Dovnarsky DK, and Shin HS. Thrombin-induced gap formation in confluent endothelial cell monolayers in vitro. Blood 62: 549-556, 1983.
    • (1983) Blood , vol.62 , pp. 549-556
    • Laposata, M.1    Dovnarsky, D.K.2    Shin, H.S.3
  • 175
    • 0029943079 scopus 로고    scopus 로고
    • Agonist recognition by proteinase-activated receptor 2 and thrombin receptor. Importance of extracellular loop interactions for receptor function
    • Lerner DJ, Chen M, Tram T, and Coughlin SR. Agonist recognition by proteinase-activated receptor 2 and thrombin receptor. Importance of extracellular loop interactions for receptor function. J Biol Chem 271: 13943-13947, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 13943-13947
    • Lerner, D.J.1    Chen, M.2    Tram, T.3    Coughlin, S.R.4
  • 176
    • 0035941170 scopus 로고    scopus 로고
    • Agonists of proteinase-activated receptor 2 excite guinea pig ileal myenteric neurons
    • Linden DR, Manning BP, Bunnett NW, and Mawe GM. Agonists of proteinase-activated receptor 2 excite guinea pig ileal myenteric neurons. Eur J Pharmacol 431: 311-314, 2001.
    • (2001) Eur J Pharmacol , vol.431 , pp. 311-314
    • Linden, D.R.1    Manning, B.P.2    Bunnett, N.W.3    Mawe, G.M.4
  • 178
    • 0032508557 scopus 로고    scopus 로고
    • Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis
    • Lourbakos A, Chinni C, Thompson P, Potempa J, Travis J, Mackie EJ, and Pike RN. Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis. FEBS Lett 435: 45-48, 1998.
    • (1998) FEBS Lett , vol.435 , pp. 45-48
    • Lourbakos, A.1    Chinni, C.2    Thompson, P.3    Potempa, J.4    Travis, J.5    Mackie, E.J.6    Pike, R.N.7
  • 179
    • 0034923238 scopus 로고    scopus 로고
    • Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion
    • Lourbakos A, Potempa J, Travis J, D'Andrea MR, Andrade-Gordon P, Santulli R, Mackie EJ, and Pike RN. Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion. Infect Immun 69: 5121-5130, 2001.
    • (2001) Infect Immun , vol.69 , pp. 5121-5130
    • Lourbakos, A.1    Potempa, J.2    Travis, J.3    D'Andrea, M.R.4    Andrade-Gordon, P.5    Santulli, R.6    Mackie, E.J.7    Pike, R.N.8
  • 180
    • 0035877969 scopus 로고    scopus 로고
    • Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: A new trait in microbial pathogenicity
    • Lourbakos A, Yuan YP, Jenkins AL, Travis J, Andrade-Gordon P, Santulli R, Potempa J, and Pike RN. Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity. Blood 97: 3790-3797, 2001.
    • (2001) Blood , vol.97 , pp. 3790-3797
    • Lourbakos, A.1    Yuan, Y.P.2    Jenkins, A.L.3    Travis, J.4    Andrade-Gordon, P.5    Santulli, R.6    Potempa, J.7    Pike, R.N.8
  • 181
    • 0036473397 scopus 로고    scopus 로고
    • The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell LM and Lefkowitz RJ. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 115: 455-465, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 183
    • 0035378665 scopus 로고    scopus 로고
    • Thrombin regulates vascular smooth muscle cell growth and heat shock proteins via the JAK-STAT pathway
    • Madamanchi NR, Li S, Patterson C, and Runge MS. Thrombin regulates vascular smooth muscle cell growth and heat shock proteins via the JAK-STAT pathway. J Biol Chem 276: 18915-18924, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 18915-18924
    • Madamanchi, N.R.1    Li, S.2    Patterson, C.3    Runge, M.S.4
  • 184
    • 0029942335 scopus 로고    scopus 로고
    • Protease activated receptors modulate aortic vascular tone
    • Magazine HI, King JM, and Srivastava KD. Protease activated receptors modulate aortic vascular tone. Int J Cardiol 53 Suppl: S75-S80, 1996.
    • (1996) Int J Cardiol , vol.53 , Issue.SUPPL.
    • Magazine, H.I.1    King, J.M.2    Srivastava, K.D.3
  • 185
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
    • Marchese A and Benovic JL. Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J Biol Chem 276: 45509-45512, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 186
    • 0035097191 scopus 로고    scopus 로고
    • Amelioration of collagen-induced arthritis by thrombin inhibition
    • Marty I, Peclat V, Kirdaite G, Salvi R, So A, and Busso N. Amelioration of collagen-induced arthritis by thrombin inhibition. J Clin Invest 107: 631-640, 2001.
    • (2001) J Clin Invest , vol.107 , pp. 631-640
    • Marty, I.1    Peclat, V.2    Kirdaite, G.3    Salvi, R.4    So, A.5    Busso, N.6
  • 188
    • 0030602911 scopus 로고    scopus 로고
    • Guinea pig lung tryptase. Localisation to mast cells and characterisation of the partially purified enzyme
    • McEuen AR, He S, Brander ML, and Walls AF. Guinea pig lung tryptase. Localisation to mast cells and characterisation of the partially purified enzyme. Biochem Pharmacol 52: 331-340, 1996.
    • (1996) Biochem Pharmacol , vol.52 , pp. 331-340
    • McEuen, A.R.1    He, S.2    Brander, M.L.3    Walls, A.F.4
  • 189
    • 0027492461 scopus 로고
    • Thrombin stimulates proliferation of cultured rat aortic smooth muscle cells by a proteolytically activated receptor
    • McNamara CA, Sarembock IJ, Gimple LW, Fenton JW, Coughlin SR, and Owens GK. Thrombin stimulates proliferation of cultured rat aortic smooth muscle cells by a proteolytically activated receptor. J Clin Invest 91: 94-98, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 94-98
    • McNamara, C.A.1    Sarembock, I.J.2    Gimple, L.W.3    Fenton, J.W.4    Coughlin, S.R.5    Owens, G.K.6
  • 191
    • 0037163104 scopus 로고    scopus 로고
    • Protease-activated receptor-2 stimulates angiogenesis and accelerates hemodynamic recovery in a mouse model of hindlimb ischemia
    • Milia AF, Salis MB, Stacca T, Pinna A, Madeddu P, Trevisani M, Geppetti P, and Emanueli C. Protease-activated receptor-2 stimulates angiogenesis and accelerates hemodynamic recovery in a mouse model of hindlimb ischemia. Circ Res 91: 346-352, 2002.
    • (2002) Circ Res , vol.91 , pp. 346-352
    • Milia, A.F.1    Salis, M.B.2    Stacca, T.3    Pinna, A.4    Madeddu, P.5    Trevisani, M.6    Geppetti, P.7    Emanueli, C.8
  • 193
    • 0030783689 scopus 로고    scopus 로고
    • Mitogenic responses mediated through the proteinase-activated receptor-2 are induced by expressed forms of mast cell alpha- or beta-tryptases
    • Mirza H, Schmidt VA, Derian CK, Jesty J, and Bahou WF. Mitogenic responses mediated through the proteinase-activated receptor-2 are induced by expressed forms of mast cell alpha- or beta-tryptases. Blood 90: 3914-3922, 1997.
    • (1997) Blood , vol.90 , pp. 3914-3922
    • Mirza, H.1    Schmidt, V.A.2    Derian, C.K.3    Jesty, J.4    Bahou, W.F.5
  • 194
    • 0030003829 scopus 로고    scopus 로고
    • The proteinase activated receptor-2 (PAR-2) mediates mitogenic responses in human vascular endothelial cells
    • Mirza H, Yatsula V, and Bahou WF. The proteinase activated receptor-2 (PAR-2) mediates mitogenic responses in human vascular endothelial cells. J Clin Invest 97: 1705-1714, 1996.
    • (1996) J Clin Invest , vol.97 , pp. 1705-1714
    • Mirza, H.1    Yatsula, V.2    Bahou, W.F.3
  • 195
    • 0036014824 scopus 로고    scopus 로고
    • Protease-activated receptor-2 activating peptide SLIGRL inhibits bacterial lipopolysaccharide-induced recruitment of polymorphonuclear leukocytes into the airways of mice
    • Moffatt JD, Jeffrey KL, and Cocks TM. Protease-activated receptor-2 activating peptide SLIGRL inhibits bacterial lipopolysaccharide-induced recruitment of polymorphonuclear leukocytes into the airways of mice. Am J Respir Cell Mol Biol 26: 680-684, 2002.
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 680-684
    • Moffatt, J.D.1    Jeffrey, K.L.2    Cocks, T.M.3
  • 198
    • 0036016106 scopus 로고    scopus 로고
    • Dual effect mediated by protease-activated receptors on the mechanical activity of rat colon
    • Mule F, Baffi MC, and Cerra MC. Dual effect mediated by protease-activated receptors on the mechanical activity of rat colon. Br J Pharmacol 136: 367-374, 2002.
    • (2002) Br J Pharmacol , vol.136 , pp. 367-374
    • Mule, F.1    Baffi, M.C.2    Cerra, M.C.3
  • 201
    • 0029143923 scopus 로고
    • Mechanisms of thrombin receptor agonist specificity. Chimeric receptors and complementary mutations identify an agonist recognition site
    • Nanevicz T, Ishii M, Wang L, Chen M, Chen J, Turck CW, Cohen FE, and Coughlin SR. Mechanisms of thrombin receptor agonist specificity. Chimeric receptors and complementary mutations identify an agonist recognition site. J Biol Chem 270: 21619-21625, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 21619-21625
    • Nanevicz, T.1    Ishii, M.2    Wang, L.3    Chen, M.4    Chen, J.5    Turck, C.W.6    Cohen, F.E.7    Coughlin, S.R.8
  • 202
    • 0030066317 scopus 로고    scopus 로고
    • Thrombin receptor activating mutations. Alteration of an extracellular agonist recognition domain causes constitutive signaling
    • Nanevicz T, Wang L, Chen M, Ishii M, and Coughlin SR. Thrombin receptor activating mutations. Alteration of an extracellular agonist recognition domain causes constitutive signaling. J Biol Chem 271: 702-706, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 702-706
    • Nanevicz, T.1    Wang, L.2    Chen, M.3    Ishii, M.4    Coughlin, S.R.5
  • 205
    • 0032896792 scopus 로고    scopus 로고
    • Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2
    • Nguyen TD, Moody MW, Steinhoff M, Okolo C, Koh DS, and Bunnett NW. Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2. J Clin Invest 103: 261-269, 1999.
    • (1999) J Clin Invest , vol.103 , pp. 261-269
    • Nguyen, T.D.1    Moody, M.W.2    Steinhoff, M.3    Okolo, C.4    Koh, D.S.5    Bunnett, N.W.6
  • 207
    • 0031844717 scopus 로고    scopus 로고
    • Changes in the expression of protease-activated receptor 1 and protease nexin-1 mRNA during rat nervous system development and after nerve lesion
    • Niclou SP, Suidan HS, Pavlik A, Vejsada R, and Monard D. Changes in the expression of protease-activated receptor 1 and protease nexin-1 mRNA during rat nervous system development and after nerve lesion. Eur J Neurosci 10: 1590-1607, 1998.
    • (1998) Eur J Neurosci , vol.10 , pp. 1590-1607
    • Niclou, S.P.1    Suidan, H.S.2    Pavlik, A.3    Vejsada, R.4    Monard, D.5
  • 208
    • 0030071886 scopus 로고    scopus 로고
    • Presence of the seven transmembrane thrombin receptor on human tumour cells: Effect of activation on tumour adhesion to platelets and tumor tyrosine phosphorylation
    • Nierodzik ML, Bain RM, Liu LX, Shivji M, Takeshita K, and Karpatkin S. Presence of the seven transmembrane thrombin receptor on human tumour cells: effect of activation on tumour adhesion to platelets and tumor tyrosine phosphorylation. Br J Haematol 92: 452-457, 1996.
    • (1996) Br J Haematol , vol.92 , pp. 452-457
    • Nierodzik, M.L.1    Bain, R.M.2    Liu, L.X.3    Shivji, M.4    Takeshita, K.5    Karpatkin, S.6
  • 210
    • 0026684801 scopus 로고
    • Effect of thrombin treatment of tumor cells on adhesion of tumor cells to platelets in vitro and tumor metastasis in vivo
    • Nierodzik ML, Kajumo F, and Karpatkin S. Effect of thrombin treatment of tumor cells on adhesion of tumor cells to platelets in vitro and tumor metastasis in vivo. Cancer Res 52: 3267-3272, 1992.
    • (1992) Cancer Res , vol.52 , pp. 3267-3272
    • Nierodzik, M.L.1    Kajumo, F.2    Karpatkin, S.3
  • 212
    • 0027488033 scopus 로고
    • Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: Evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment
    • Norton KJ, Scarborough RM, Kutok JL, Escobedo MA, Nannizzi L, and Coller BS. Immunologic analysis of the cloned platelet thrombin receptor activation mechanism: evidence supporting receptor cleavage, release of the N-terminal peptide, and insertion of the tethered ligand into a protected environment. Blood 82: 2125-2136, 1993.
    • (1993) Blood , vol.82 , pp. 2125-2136
    • Norton, K.J.1    Scarborough, R.M.2    Kutok, J.L.3    Escobedo, M.A.4    Nannizzi, L.5    Coller, B.S.6
  • 213
    • 0029113121 scopus 로고
    • Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2
    • Nystedt S, Emilsson K, Larsson AK, Strombeck B, and Sundelin J. Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2. Eur J Biochem. 232: 84-89, 1995.
    • (1995) Eur J Biochem , vol.232 , pp. 84-89
    • Nystedt, S.1    Emilsson, K.2    Larsson, A.K.3    Strombeck, B.4    Sundelin, J.5
  • 215
    • 0028934047 scopus 로고
    • The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression
    • Nystedt S, Larsson AK, Aberg H, and Sundelin J. The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression. J Biol Chem 270: 5950-5955, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 5950-5955
    • Nystedt, S.1    Larsson, A.K.2    Aberg, H.3    Sundelin, J.4
  • 216
    • 15844401726 scopus 로고    scopus 로고
    • The proteinase-activated receptor 2 is induced by inflammatory mediators in human endothelial cells. Comparison with the thrombin receptor
    • Nystedt S, Ramakrishnan V, and Sundelin J. The proteinase-activated receptor 2 is induced by inflammatory mediators in human endothelial cells. Comparison with the thrombin receptor. J Biol Chem 271: 14910-14915, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 14910-14915
    • Nystedt, S.1    Ramakrishnan, V.2    Sundelin, J.3
  • 217
    • 0035952643 scopus 로고    scopus 로고
    • Protease activated receptors: Theme and variations
    • O'Brien PJ, Molino M, Kahn M, and Brass LF. Protease activated receptors: theme and variations. Oncogene 20: 1570-1581, 2001.
    • (2001) Oncogene , vol.20 , pp. 1570-1581
    • O'Brien, P.J.1    Molino, M.2    Kahn, M.3    Brass, L.F.4
  • 218
    • 0034608013 scopus 로고    scopus 로고
    • Thrombin responses in human endothelial cells. Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1
    • O'Brien PJ, Prevost N, Molino M, Hollinger MK, Woolkalis MJ, Woulfe DS, and Brass LF. Thrombin responses in human endothelial cells. Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1. J Biol Chem 275: 13502-13509, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 13502-13509
    • O'Brien, P.J.1    Prevost, N.2    Molino, M.3    Hollinger, M.K.4    Woolkalis, M.J.5    Woulfe, D.S.6    Brass, L.F.7
  • 219
    • 0035952734 scopus 로고    scopus 로고
    • In vivo functions of heterotrimeric G-proteins: Studies in Galpha-deficient mice
    • Offermanns S. In vivo functions of heterotrimeric G-proteins: studies in Galpha-deficient mice. Oncogene 20: 1635-1642, 2001.
    • (2001) Oncogene , vol.20 , pp. 1635-1642
    • Offermanns, S.1
  • 222
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in G alpha(q)-deficient mice
    • Offermanns S, Toombs CF, Hu YH, and Simon MI. Defective platelet activation in G alpha(q)-deficient mice. Nature 389: 183-186, 1997.
    • (1997) Nature , vol.389 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.H.3    Simon, M.I.4
  • 223
    • 0032374055 scopus 로고    scopus 로고
    • A trypsin-like platelet protease propagates protease-activated receptor-1 cleavage and platelet activation
    • Ofosu FA, Freedman J, Dewar L, Song Y, and Fenton JW II. A trypsin-like platelet protease propagates protease-activated receptor-1 cleavage and platelet activation. Biochem J 336: 283-285, 1998.
    • (1998) Biochem J , vol.336 , pp. 283-285
    • Ofosu, F.A.1    Freedman, J.2    Dewar, L.3    Song, Y.4    Fenton II, J.W.5
  • 224
    • 0035046316 scopus 로고    scopus 로고
    • An alternative approach to depigmentation by soybean extracts via inhibition of the PAR-2 pathway
    • Paine C, Sharlow E, Liebel F, Eisinger M, Shapiro S, and Seiberg M. An alternative approach to depigmentation by soybean extracts via inhibition of the PAR-2 pathway. J Invest Dermatol 116: 587-595, 2001.
    • (2001) J Invest Dermatol , vol.116 , pp. 587-595
    • Paine, C.1    Sharlow, E.2    Liebel, F.3    Eisinger, M.4    Shapiro, S.5    Seiberg, M.6
  • 225
    • 0037059795 scopus 로고    scopus 로고
    • Beta-arrestins regulate protease-activated receptor-1 desensitization but not internalization or down-regulation
    • Paing MM, Stutts AB, Kohout TA, Lefkowitz RJ, and Trejo J. beta-Arrestins regulate protease-activated receptor-1 desensitization but not internalization or down-regulation. J Biol Chem 277: 1292-1300, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 1292-1300
    • Paing, M.M.1    Stutts, A.B.2    Kohout, T.A.3    Lefkowitz, R.J.4    Trejo, J.5
  • 226
    • 0035947756 scopus 로고    scopus 로고
    • New tricks for old dogs: Nonthrombotic effects of thrombin in vessel wall biology
    • Patterson C, Stouffer GA, Madamanchi N, and Runge MS. New tricks for old dogs: nonthrombotic effects of thrombin in vessel wall biology. Circ Res 88: 987-997, 2001.
    • (2001) Circ Res , vol.88 , pp. 987-997
    • Patterson, C.1    Stouffer, G.A.2    Madamanchi, N.3    Runge, M.S.4
  • 227
    • 0036739950 scopus 로고    scopus 로고
    • Plasmin induces Cyr61 gene expression in fibroblasts via protease-activated receptor-1 and p44/42 mitogen-activated protein kinase-dependent signaling pathway
    • Pendurthi UR, Ngyuen M, Andrade-Gordon P, Petersen LC, and Rao LV. Plasmin induces Cyr61 gene expression in fibroblasts via protease-activated receptor-1 and p44/42 mitogen-activated protein kinase-dependent signaling pathway. Arterioscler Thromb Vasc Biol 22: 1421-1426, 2002.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 1421-1426
    • Pendurthi, U.R.1    Ngyuen, M.2    Andrade-Gordon, P.3    Petersen, L.C.4    Rao, L.V.5
  • 229
    • 0023517177 scopus 로고
    • Thrombin is a potent mitogen for rat astroblasts but not for oligodendroblasts and neuroblasts in primary culture
    • Perraud F, Besnard F, Sensenbrenner M, and Labourdette G. Thrombin is a potent mitogen for rat astroblasts but not for oligodendroblasts and neuroblasts in primary culture. Int J Dev Neurosci 5: 181-188, 1987.
    • (1987) Int J Dev Neurosci , vol.5 , pp. 181-188
    • Perraud, F.1    Besnard, F.2    Sensenbrenner, M.3    Labourdette, G.4
  • 230
    • 0034175489 scopus 로고    scopus 로고
    • Thrombomodulin as a new marker of lesion-induced astrogliosis: Involvement of thrombin through the G-protein-coupled protease-activated receptor-1
    • Pindon A, Berry M, and Hantai D. Thrombomodulin as a new marker of lesion-induced astrogliosis: involvement of thrombin through the G-protein-coupled protease-activated receptor-1. J Neurosci 20: 2543-2550, 2000.
    • (2000) J Neurosci , vol.20 , pp. 2543-2550
    • Pindon, A.1    Berry, M.2    Hantai, D.3
  • 231
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H, Leserer M, Abraham R, Wallasch C, and Ullrich A. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402: 884-888, 1999.
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3    Leserer, M.4    Abraham, R.5    Wallasch, C.6    Ullrich, A.7
  • 234
    • 0042819700 scopus 로고    scopus 로고
    • Role of proteinase-activated receptors in cutaneous biology and disease
    • edited by M. Hollenberg and N. Vergrolle. New York: Wiley-Liss
    • Rattenholl A and Steinhoff M. Role of proteinase-activated receptors in cutaneous biology and disease. In: Drug Development Research, edited by M. Hollenberg and N. Vergrolle. New York: Wiley-Liss, 2003, vol. 59, p. 408-417.
    • (2003) Drug Development Research , vol.59 , pp. 408-417
    • Rattenholl, A.1    Steinhoff, M.2
  • 236
    • 0030968521 scopus 로고    scopus 로고
    • Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: Evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor
    • Renesto P, Si-Tahar M, Moniatte M, Balloy V, Van Dorsselaer A, Pidard D, and Chignard M. Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor. Blood 89: 1944-1953, 1997.
    • (1997) Blood , vol.89 , pp. 1944-1953
    • Renesto, P.1    Si-Tahar, M.2    Moniatte, M.3    Balloy, V.4    Van Dorsselaer, A.5    Pidard, D.6    Chignard, M.7
  • 238
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • Riewald M, Petrovan RJ, Donner A, Mueller BM, and Ruf W. Activation of endothelial cell protease activated receptor 1 by the protein C pathway. Science 296: 1880-1882, 2002.
    • (2002) Science , vol.296 , pp. 1880-1882
    • Riewald, M.1    Petrovan, R.J.2    Donner, A.3    Mueller, B.M.4    Ruf, W.5
  • 239
    • 0034933683 scopus 로고    scopus 로고
    • Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor
    • Riewald M and Ruf W. Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor. Proc Natl Acad Sci USA 98: 7742-7747, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7742-7747
    • Riewald, M.1    Ruf, W.2
  • 240
    • 0037386434 scopus 로고    scopus 로고
    • Science review: Role of coagulation protease cascades in sepsis
    • Riewald M and Ruf W. Science review: role of coagulation protease cascades in sepsis. Crit Care 7: 123-129, 2003.
    • (2003) Crit Care , vol.7 , pp. 123-129
    • Riewald, M.1    Ruf, W.2
  • 241
    • 0037465357 scopus 로고    scopus 로고
    • Protease-activated receptor 2-mediated vasodilatation in humans in vivo: Role of nitric oxide and prostanoids
    • Robin J, Kharbanda R, McLean P, Campbell R, and Vallance P. Protease-activated receptor 2-mediated vasodilatation in humans in vivo: role of nitric oxide and prostanoids. Circulation 107: 954-959, 2003.
    • (2003) Circulation , vol.107 , pp. 954-959
    • Robin, J.1    Kharbanda, R.2    McLean, P.3    Campbell, R.4    Vallance, P.5
  • 242
    • 0037405191 scopus 로고    scopus 로고
    • Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2
    • Roosterman D, Schmidlin F, and Bunnett NW. Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2. Am J Physiol Cell Physiol 284: C1319-C1329, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Roosterman, D.1    Schmidlin, F.2    Bunnett, N.W.3
  • 243
    • 0031890089 scopus 로고    scopus 로고
    • Dual endothelium-dependent vascular activities of proteinase-activated receptor-2-activating peptides: Evidence for receptor heterogeneity
    • Roy SS, Saifeddine M, Loutzenhiser R, Triggle CR, and Hollenberg MD. Dual endothelium-dependent vascular activities of proteinase-activated receptor-2-activating peptides: evidence for receptor heterogeneity. Br J Pharmacol 123: 1434-1440, 1998.
    • (1998) Br J Pharmacol , vol.123 , pp. 1434-1440
    • Roy, S.S.1    Saifeddine, M.2    Loutzenhiser, R.3    Triggle, C.R.4    Hollenberg, M.D.5
  • 244
    • 0025864033 scopus 로고
    • Mast cell tryptase is a mitogen for cultured fibroblasts
    • Ruoss S, Hartmann T, and Caughey G. Mast cell tryptase is a mitogen for cultured fibroblasts. J Clin Invest 88: 493-499, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 493-499
    • Ruoss, S.1    Hartmann, T.2    Caughey, G.3
  • 246
    • 0037144657 scopus 로고    scopus 로고
    • Protease-activated receptor-1-mediated DNA synthesis in cardiac fibroblast is via epidermal growth factor receptor transactivation: Distinct PAR-1 signaling pathways in cardiac fibroblasts and cardiomyocytes
    • Sabri A, Short J, Guo J, and Steinberg SF. Protease-activated receptor-1-mediated DNA synthesis in cardiac fibroblast is via epidermal growth factor receptor transactivation: distinct PAR-1 signaling pathways in cardiac fibroblasts and cardiomyocytes. Circ Res 91: 532-539, 2002.
    • (2002) Circ Res , vol.91 , pp. 532-539
    • Sabri, A.1    Short, J.2    Guo, J.3    Steinberg, S.F.4
  • 247
    • 0030008482 scopus 로고    scopus 로고
    • Rat proteinase-activated receptor-2 (PAR-2): cDNA sequence and activity of receptor-derived peptides in gastric and vascular tissue
    • Saifeddine M, al-Ani B, Cheng CH, Wang L, and Hollenberg MD. Rat proteinase-activated receptor-2 (PAR-2): cDNA sequence and activity of receptor-derived peptides in gastric and vascular tissue. Br J Pharmacol 118: 521-530, 1996.
    • (1996) Br J Pharmacol , vol.118 , pp. 521-530
    • Saifeddine, M.1    Al-Ani, B.2    Cheng, C.H.3    Wang, L.4    Hollenberg, M.D.5
  • 248
    • 0031792955 scopus 로고    scopus 로고
    • Endothelium-dependent contractile actions of proteinase-activated receptor-2-activating peptides in human umbilical vein: Release of a contracting factor via a novel receptor
    • Saifeddine M, Roy SS, Al-Ani B, Triggle CR, and Hollenberg MD. Endothelium-dependent contractile actions of proteinase-activated receptor-2-activating peptides in human umbilical vein: release of a contracting factor via a novel receptor. Br J Pharmacol 125: 1445-1454, 1998.
    • (1998) Br J Pharmacol , vol.125 , pp. 1445-1454
    • Saifeddine, M.1    Roy, S.S.2    Al-Ani, B.3    Triggle, C.R.4    Hollenberg, M.D.5
  • 250
    • 0032831916 scopus 로고    scopus 로고
    • Characterisation of immune mediator release during the immediate response to segmental mucosal challenge in the jejunum of patients with food allergy
    • Santos J, Bayarri C, Saperas E, Nogueiras C, Antolin M, Mourelle M, Cadahia A, and Malagelada JR. Characterisation of immune mediator release during the immediate response to segmental mucosal challenge in the jejunum of patients with food allergy. Gut 45: 553-558, 1999.
    • (1999) Gut , vol.45 , pp. 553-558
    • Santos, J.1    Bayarri, C.2    Saperas, E.3    Nogueiras, C.4    Antolin, M.5    Mourelle, M.6    Cadahia, A.7    Malagelada, J.R.8
  • 252
    • 0034022706 scopus 로고    scopus 로고
    • Purification and characterization of a trypsin-like serine proteinase from rat brain slices that degrades laminin and type IV collagen and stimulates protease-activated receptor-2
    • Sawada K, Nishibori M, Nakaya N, Wang Z, and Saeki K. Purification and characterization of a trypsin-like serine proteinase from rat brain slices that degrades laminin and type IV collagen and stimulates protease-activated receptor-2. J Neurochem 74: 1731-1738, 2000.
    • (2000) J Neurochem , vol.74 , pp. 1731-1738
    • Sawada, K.1    Nishibori, M.2    Nakaya, N.3    Wang, Z.4    Saeki, K.5
  • 253
    • 0026629249 scopus 로고
    • Tethered ligand agonist peptides. Structural requirements for thrombin receptor activation reveal mechanism of proteolytic unmasking of agonist function
    • Scarborough RM, Naughton MA, Teng W, Hung DT, Rose J, Vu TK, Wheaton VI, Turck CW, and Coughlin SR. Tethered ligand agonist peptides. Structural requirements for thrombin receptor activation reveal mechanism of proteolytic unmasking of agonist function. J Biol Chem 267: 13146-13149, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 13146-13149
    • Scarborough, R.M.1    Naughton, M.A.2    Teng, W.3    Hung, D.T.4    Rose, J.5    Vu, T.K.6    Wheaton, V.I.7    Turck, C.W.8    Coughlin, S.R.9
  • 254
    • 0031850771 scopus 로고    scopus 로고
    • Reaction of mast cell proteases tryptase and chymase with protease activated receptors (PARs) on keratinocytes and fibroblasts
    • Schechter NM, Brass LF, Lavker RM, and Jensen PJ. Reaction of mast cell proteases tryptase and chymase with protease activated receptors (PARs) on keratinocytes and fibroblasts. J Cell Physiol 176: 365-373, 1998.
    • (1998) J Cell Physiol , vol.176 , pp. 365-373
    • Schechter, N.M.1    Brass, L.F.2    Lavker, R.M.3    Jensen, P.J.4
  • 257
    • 0035678081 scopus 로고    scopus 로고
    • Protease-activated receptor 2, a receptor involved in melanosome transfer, is upregulated in human skin by ultraviolet irradiation
    • Scott G, Deng A, Rodriguez-Burford C, Seiberg M, Han R, Babiarz L, Grizzle W, Bell W, and Pentland A. Protease-activated receptor 2, a receptor involved in melanosome transfer, is upregulated in human skin by ultraviolet irradiation. J Invest Dermatol 117: 1412-1420, 2001.
    • (2001) J Invest Dermatol , vol.117 , pp. 1412-1420
    • Scott, G.1    Deng, A.2    Rodriguez-Burford, C.3    Seiberg, M.4    Han, R.5    Babiarz, L.6    Grizzle, W.7    Bell, W.8    Pentland, A.9
  • 258
    • 0028819780 scopus 로고
    • Release of the mucosal mast cell granule chymase, rat mast cell protease-II, during anaphylaxis is associated with the rapid development of para cellular permeability to macromolecules in rat jejunum
    • Scudamore CL, Thornton EM, McMillan L, Newlands GF, and Miller HR. Release of the mucosal mast cell granule chymase, rat mast cell protease-II, during anaphylaxis is associated with the rapid development of paracellular permeability to macromolecules in rat jejunum. J Exp Med 182: 1871-1881, 1995.
    • (1995) J Exp Med , vol.182 , pp. 1871-1881
    • Scudamore, C.L.1    Thornton, E.M.2    McMillan, L.3    Newlands, G.F.4    Miller, H.R.5
  • 261
    • 0032582534 scopus 로고    scopus 로고
    • Separate signals for agonist-independent and agonist-triggered trafficking of protease-activated receptor 1
    • Shapiro MJ and Coughlin SR. Separate signals for agonist-independent and agonist-triggered trafficking of protease-activated receptor 1. J Biol Chem 273: 29009-29014, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 29009-29014
    • Shapiro, M.J.1    Coughlin, S.R.2
  • 262
    • 0030478939 scopus 로고    scopus 로고
    • Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization
    • Shapiro MJ, Trejo J, Zeng D, and Coughlin SR. Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization. J Biol Chem 271: 32874-32880, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 32874-32880
    • Shapiro, M.J.1    Trejo, J.2    Zeng, D.3    Coughlin, S.R.4
  • 263
    • 0034682810 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 are shutoff with distinct kinetics after activation by thrombin
    • Shapiro MJ, Weiss EJ, Faruqi TR, and Coughlin SR. Protease-activated receptors 1 and 4 are shutoff with distinct kinetics after activation by thrombin. J Biol Chem 275: 25216-25221, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 25216-25221
    • Shapiro, M.J.1    Weiss, E.J.2    Faruqi, T.R.3    Coughlin, S.R.4
  • 266
    • 0035827339 scopus 로고    scopus 로고
    • A genomic perspective on human proteases
    • Southan C. A genomic perspective on human proteases. FEBS Lett 498: 214-218, 2001.
    • (2001) FEBS Lett , vol.498 , pp. 214-218
    • Southan, C.1
  • 267
    • 0023332815 scopus 로고
    • Intestinal mucosal mast cells in normal and nematode-infected rat intestines are in intimate contact with peptidergic nerves
    • Stead RH, Tomioka M, Quinonez G, Simon GT, Felten SY, and Bienenstock J. Intestinal mucosal mast cells in normal and nematode-infected rat intestines are in intimate contact with peptidergic nerves. Proc Natl Acad Sci USA 84: 2975-2979, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2975-2979
    • Stead, R.H.1    Tomioka, M.2    Quinonez, G.3    Simon, G.T.4    Felten, S.Y.5    Bienenstock, J.6
  • 271
    • 0034053127 scopus 로고    scopus 로고
    • The protease thrombin is an endogenous mediator of hippocampal neuroprotection against ischemia at low concentrations but causes degeneration at high concentrations
    • Striggow F, Riek M, Breder J, Henrich-Noack P, Reymann KG, and Reiser G. The protease thrombin is an endogenous mediator of hippocampal neuroprotection against ischemia at low concentrations but causes degeneration at high concentrations. Proc Natl Acad Sci USA 97: 2264-2269, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2264-2269
    • Striggow, F.1    Riek, M.2    Breder, J.3    Henrich-Noack, P.4    Reymann, K.G.5    Reiser, G.6
  • 272
    • 0028059276 scopus 로고
    • Granzyme A released upon stimulation of cytotoxic T lymphocytes activates the thrombin receptor on neuronal cells and astrocytes
    • Suidan HS, Bouvier J, Schaerer E, Stone SR, Monard D, and Tschopp J. Granzyme A released upon stimulation of cytotoxic T lymphocytes activates the thrombin receptor on neuronal cells and astrocytes. Proc Natl Acad Sci USA 91: 8112-8116, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8112-8116
    • Suidan, H.S.1    Bouvier, J.2    Schaerer, E.3    Stone, S.R.4    Monard, D.5    Tschopp, J.6
  • 273
    • 0035879347 scopus 로고    scopus 로고
    • Interaction of mite allergens der p3 and der p9 with protease-activated receptor-2 expressed by lung epithelial cells
    • Sun G, Stacey MA, Schmidt M, Mori L, and Mattoli S. Interaction of mite allergens der p3 and der p9 with protease-activated receptor-2 expressed by lung epithelial cells. J Immunol 167: 1014-1021, 2001.
    • (2001) J Immunol , vol.167 , pp. 1014-1021
    • Sun, G.1    Stacey, M.A.2    Schmidt, M.3    Mori, L.4    Mattoli, S.5
  • 274
    • 0042904881 scopus 로고    scopus 로고
    • Persistent protease-activated receptor 4 signaling mediates thrombin-induced microglial activation
    • In press
    • Suo Z, Wu M, Citron BA, Gao C, and Festoff BW. Persistent protease-activated receptor 4 signaling mediates thrombin-induced microglial activation. J Biol Chem. In press.
    • J Biol Chem
    • Suo, Z.1    Wu, M.2    Citron, B.A.3    Gao, C.4    Festoff, B.W.5
  • 275
    • 0027303045 scopus 로고
    • Detection and characterization of endogeneous protease associated with desquamation of stratum corneum
    • Suzuki Y, Nomura J, Hori J, Koyama J, Takahashi M, and Horii I. Detection and characterization of endogeneous protease associated with desquamation of stratum corneum. Arch Dermatol Res 285: 372-377, 1993.
    • (1993) Arch Dermatol Res , vol.285 , pp. 372-377
    • Suzuki, Y.1    Nomura, J.2    Hori, J.3    Koyama, J.4    Takahashi, M.5    Horii, I.6
  • 276
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi T, Harris JL, Huang W, Yan KW, Coughlin SR, and Craik CS. Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J Biol Chem 275: 26333-26342, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 277
    • 0029047721 scopus 로고
    • Contractile actions of thrombin receptor-derived polypeptides in human umbilical and placental vasculature: Evidence for distinct receptor systems
    • Tay-Uyboco J, Poon MC, Ahmad S, and Hollenberg MD. Contractile actions of thrombin receptor-derived polypeptides in human umbilical and placental vasculature: evidence for distinct receptor systems. Br J Pharmacol 115: 569-578, 1995.
    • (1995) Br J Pharmacol , vol.115 , pp. 569-578
    • Tay-Uyboco, J.1    Poon, M.C.2    Ahmad, S.3    Hollenberg, M.D.4
  • 280
    • 0037349117 scopus 로고    scopus 로고
    • Protease-activated receptor (PAR)-independent growth and pro-inflammatory actions of thrombin on human cultured airway smooth muscle
    • Tran T and Stewart AG. Protease-activated receptor (PAR)-independent growth and pro-inflammatory actions of thrombin on human cultured airway smooth muscle. Br J Pharmacol 138: 865-875, 2003.
    • (2003) Br J Pharmacol , vol.138 , pp. 865-875
    • Tran, T.1    Stewart, A.G.2
  • 281
    • 0034613356 scopus 로고    scopus 로고
    • Protease-activated receptor-1 down-regulation: A mutant HeLa cell line suggests novel requirements for PAR1 phosphorylation and recruitment to clathrin-coated pits
    • Trejo J, Altschuler Y, Fu HW, Mostov KE, and Coughlin SR. Protease-activated receptor-1 down-regulation: a mutant HeLa cell line suggests novel requirements for PAR1 phosphorylation and recruitment to clathrin-coated pits. J Biol Chem 275: 31255-31265, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 31255-31265
    • Trejo, J.1    Altschuler, Y.2    Fu, H.W.3    Mostov, K.E.4    Coughlin, S.R.5
  • 282
    • 0033593210 scopus 로고    scopus 로고
    • The cytoplasmic tails of protease-activated receptor-1 and substance P receptor specify sorting to lysosomes versus recycling
    • Trejo J and Coughlin SR. The cytoplasmic tails of protease-activated receptor-1 and substance P receptor specify sorting to lysosomes versus recycling. J Biol Chem 274: 2216-2224, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2216-2224
    • Trejo, J.1    Coughlin, S.R.2
  • 283
    • 0032506111 scopus 로고    scopus 로고
    • Termination of signaling by protease-activated receptor-1 is linked to lysosomal sorting
    • Trejo J, Hammes SR, and Coughlin SR. Termination of signaling by protease-activated receptor-1 is linked to lysosomal sorting. Proc Natl Acad Sci USA 95: 13698-13702, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13698-13702
    • Trejo, J.1    Hammes, S.R.2    Coughlin, S.R.3
  • 285
    • 0033588371 scopus 로고    scopus 로고
    • On the mechanism of thrombin-induced angiogenesis. Potentiation of vascular endothelial growth factor activity on endothelial cells by up-regulation of its receptors
    • Tsopanoglou NE and Maragoudakis ME. On the mechanism of thrombin-induced angiogenesis. Potentiation of vascular endothelial growth factor activity on endothelial cells by up-regulation of its receptors. J Biol Chem 274: 23969-23976, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 23969-23976
    • Tsopanoglou, N.E.1    Maragoudakis, M.E.2
  • 286
    • 17344365478 scopus 로고    scopus 로고
    • Thrombin perturbs neurite outgrowth and induces apoptotic cell death in enriched chick spinal motoneuron cultures through caspase activation
    • Turgeon VL, Lloyd ED, Wang S, Festoff BW, and Houenou LJ. Thrombin perturbs neurite outgrowth and induces apoptotic cell death in enriched chick spinal motoneuron cultures through caspase activation. J Neurosci 18: 6882-6891, 1998.
    • (1998) J Neurosci , vol.18 , pp. 6882-6891
    • Turgeon, V.L.1    Lloyd, E.D.2    Wang, S.3    Festoff, B.W.4    Houenou, L.J.5
  • 287
    • 0031031775 scopus 로고    scopus 로고
    • i oscillations in rat glioma cells
    • i oscillations in rat glioma cells. Pflügers Arch 433: 312-320, 1997.
    • (1997) Pflügers Arch , vol.433 , pp. 312-320
    • Ubl, J.J.1    Reiser, G.2
  • 288
    • 0031539290 scopus 로고    scopus 로고
    • Characteristics of thrombin-induced calcium signals in rat astrocytes
    • Ubl JJ and Reiser G. Characteristics of thrombin-induced calcium signals in rat astrocytes. Glia 21: 361-369, 1997.
    • (1997) Glia , vol.21 , pp. 361-369
    • Ubl, J.J.1    Reiser, G.2
  • 289
    • 0034213673 scopus 로고    scopus 로고
    • 2+ signalling evoked by the tethered ligand
    • 2+ signalling evoked by the tethered ligand. J Physiol 525: 319-330, 2000.
    • (2000) J Physiol , vol.525 , pp. 319-330
    • Ubl, J.J.1    Sergeeva, M.2    Reiser, G.3
  • 290
    • 0032100686 scopus 로고    scopus 로고
    • i-inducing protease-activated receptors (PAR-1 and PAR-2) in rat astrocytes and C6 glioma cells
    • i-inducing protease-activated receptors (PAR-1 and PAR-2) in rat astrocytes and C6 glioma cells. Neuroscience 86: 597-609, 1998.
    • (1998) Neuroscience , vol.86 , pp. 597-609
    • Ubl, J.J.1    Vohringer, C.2    Reiser, G.3
  • 291
    • 0037797300 scopus 로고    scopus 로고
    • Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2
    • Uehara A, Muramoto K, Takada H, and Sugawara S. Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2. J Immunol 170: 5690-5696, 2003.
    • (2003) J Immunol , vol.170 , pp. 5690-5696
    • Uehara, A.1    Muramoto, K.2    Takada, H.3    Sugawara, S.4
  • 292
    • 0037108503 scopus 로고    scopus 로고
    • Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2
    • Uehara A, Sugawara S, Muramoto K, and Takada H. Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2. J Immunol 169: 4594-4603, 2002.
    • (2002) J Immunol , vol.169 , pp. 4594-4603
    • Uehara, A.1    Sugawara, S.2    Muramoto, K.3    Takada, H.4
  • 293
    • 0029012029 scopus 로고
    • Thrombin receptor activation protects neurons and astrocytes from cell death produced by environmental insults
    • Vaughan PJ, Pike CJ, Cotman CW, and Cunningham DD. Thrombin receptor activation protects neurons and astrocytes from cell death produced by environmental insults. J Neurosci 15: 5389-5401, 1995.
    • (1995) J Neurosci , vol.15 , pp. 5389-5401
    • Vaughan, P.J.1    Pike, C.J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 294
    • 0032708759 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-activating peptides induce leukocyte rolling, adhesion, and extravasation in vivo
    • Vergnolle N. Proteinase-activated receptor-2-activating peptides induce leukocyte rolling, adhesion, and extravasation in vivo. J Immunol 163: 5064-5069, 1999.
    • (1999) J Immunol , vol.163 , pp. 5064-5069
    • Vergnolle, N.1
  • 295
    • 0034055571 scopus 로고    scopus 로고
    • Review article: Proteinase-activated receptors: Novel signals for gastrointestinal pathophysiology
    • Vergnolle N. Review article: proteinase-activated receptors: novel signals for gastrointestinal pathophysiology. Aliment Pharmacol Ther 14: 257-266, 2000.
    • (2000) Aliment Pharmacol Ther , vol.14 , pp. 257-266
    • Vergnolle, N.1
  • 297
    • 0036681940 scopus 로고    scopus 로고
    • Characterization of thrombin-induced leukocyte rolling and adherence: A potential proinflammatory role for proteinase-activated receptor-4
    • Vergnolle N, Derian CK, D'Andrea MR, Steinhoff M, and Andrade-Gordon P. Characterization of thrombin-induced leukocyte rolling and adherence: a potential proinflammatory role for proteinase-activated receptor-4. J Immunol 169: 1467-1473, 2002.
    • (2002) J Immunol , vol.169 , pp. 1467-1473
    • Vergnolle, N.1    Derian, C.K.2    D'Andrea, M.R.3    Steinhoff, M.4    Andrade-Gordon, P.5
  • 298
    • 0032792955 scopus 로고    scopus 로고
    • Characterization of the inflammatory response to proteinase-activated receptor-2 (PAR2)-activating peptides in the rat paw
    • Vergnolle N, Hollenberg MD, Sharkey KA, and Wallace JL. Characterization of the inflammatory response to proteinase-activated receptor-2 (PAR2)-activating peptides in the rat paw. Br J Pharmacol 127: 1083-1090, 1999.
    • (1999) Br J Pharmacol , vol.127 , pp. 1083-1090
    • Vergnolle, N.1    Hollenberg, M.D.2    Sharkey, K.A.3    Wallace, J.L.4
  • 299
    • 0032975515 scopus 로고    scopus 로고
    • Pro- and anti-inflammatory actions of thrombin: A distinct role for proteinase-activated receptor-1 (PAR1)
    • Vergnolle N, Hollenberg MD, and Wallace JL. Pro- and anti-inflammatory actions of thrombin: a distinct role for proteinase-activated receptor-1 (PAR1). Br J Pharmacol 126: 1262-1268, 1999.
    • (1999) Br J Pharmacol , vol.126 , pp. 1262-1268
    • Vergnolle, N.1    Hollenberg, M.D.2    Wallace, J.L.3
  • 300
    • 0032560576 scopus 로고    scopus 로고
    • Proteinase-activated receptor 2 (PAR2)-activating peptides: Identification of a receptor distinct from PAR2 that regulates intestinal transport
    • Vergnolle N, MacNaughton WK, Al-Ani B, Saifeddine M, Wallace JL, and Hollenberg MD. Proteinase-activated receptor 2 (PAR2)-activating peptides: identification of a receptor distinct from PAR2 that regulates intestinal transport. Proc Natl Acad Sci USA 95: 7766-7771, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7766-7771
    • Vergnolle, N.1    MacNaughton, W.K.2    Al-Ani, B.3    Saifeddine, M.4    Wallace, J.L.5    Hollenberg, M.D.6
  • 303
    • 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, and Van Obberghen-Schilling E. Regulation of the actin cytoskeleton by thrombin in human endothelial cells: role of Rho proteins in endothelial barrier function. Mol Biol Cell 9: 2639-2653, 1998.
    • (1998) Mol Biol Cell , vol.9 , pp. 2639-2653
    • Vouret-Craviari, V.1    Boquet, P.2    Pouyssegur, J.3    Van Obberghen-Schilling, E.4
  • 305
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, and Coughlin SR. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64: 1057-1068, 1991.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 307
    • 0030893530 scopus 로고    scopus 로고
    • Thrombin and trypsin stimulate granulocyte-macrophage colony-stimulating factor and interleukin-6 gene expression in cultured normal human keratinocytes
    • Wakita H, Furukawa F, and MT. Thrombin and trypsin stimulate granulocyte-macrophage colony-stimulating factor and interleukin-6 gene expression in cultured normal human keratinocytes. Proc Assoc Am Phys 109: 190-207, 1997.
    • (1997) Proc Assoc Am Phys , vol.109 , pp. 190-207
    • Wakita, H.1    Furukawa, F.2
  • 308
    • 0037298752 scopus 로고    scopus 로고
    • Thrombin signaling in the brain: The role of protease-activated receptors
    • Wang H and Reiser G. Thrombin signaling in the brain: the role of protease-activated receptors. J Biol Chem 384: 193-202, 2003.
    • (2003) J Biol Chem , vol.384 , pp. 193-202
    • Wang, H.1    Reiser, G.2
  • 309
    • 0036006726 scopus 로고    scopus 로고
    • Four subtypes of protease-activated receptors, co-expressed in rat astrocytes, evoke different physiological signaling
    • Wang H, Ubl JJ, and Reiser G. Four subtypes of protease-activated receptors, co-expressed in rat astrocytes, evoke different physiological signaling. Glia 37: 53-63, 2002.
    • (2002) Glia , vol.37 , pp. 53-63
    • Wang, H.1    Ubl, J.J.2    Reiser, G.3
  • 310
    • 0036838021 scopus 로고    scopus 로고
    • Thrombin (PAR-1)-induced proliferation in astrocytes via MAPK involves multiple signaling pathways
    • Wang H, Ubl JJ, Stricker R, and Reiser G. Thrombin (PAR-1)-induced proliferation in astrocytes via MAPK involves multiple signaling pathways. Am J Physiol Cell Physiol 283: C1351-C1364, 2002.
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Wang, H.1    Ubl, J.J.2    Stricker, R.3    Reiser, G.4
  • 311
    • 0035985175 scopus 로고    scopus 로고
    • Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1
    • Wang Y, Zhou Y, Szabo K, Haft CR, and Trejo J. Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1. Mol Biol Cell 13: 1965-1976, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1965-1976
    • Wang, Y.1    Zhou, Y.2    Szabo, K.3    Haft, C.R.4    Trejo, J.5
  • 312
    • 0028914068 scopus 로고
    • Cellular localization of thrombin receptor mRNA in rat brain: Expression by mesencephalic dopaminergic neurons and codistribution with prothrombin mRNA
    • Weinstein JR, Gold SJ, Cunningham DD, and Gall CM. Cellular localization of thrombin receptor mRNA in rat brain: expression by mesencephalic dopaminergic neurons and codistribution with prothrombin mRNA. J Neurosci 15: 2906-2919, 1995.
    • (1995) J Neurosci , vol.15 , pp. 2906-2919
    • Weinstein, J.R.1    Gold, S.J.2    Cunningham, D.D.3    Gall, C.M.4
  • 313
    • 0036838525 scopus 로고    scopus 로고
    • Protection against thrombosis in mice lacking PAR3
    • Weiss EJ, Hamilton JR, Lease KE, and Coughlin SR. Protection against thrombosis in mice lacking PAR3. Blood 100: 3240-3244, 2002.
    • (2002) Blood , vol.100 , pp. 3240-3244
    • Weiss, E.J.1    Hamilton, J.R.2    Lease, K.E.3    Coughlin, S.R.4
  • 314
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann C, Gibson S, Jarpe MB, and Johnson GL. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol Rev 79: 143-180, 1999.
    • (1999) Physiol Rev , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 318
    • 0035132174 scopus 로고    scopus 로고
    • Mucosal pathophysiology and inflammatory changes in the late phase of the intestinal allergic reaction in the rat
    • Yang PC, Berin MC, Yu L, and Perdue MH. Mucosal pathophysiology and inflammatory changes in the late phase of the intestinal allergic reaction in the rat. Am J Pathol 158: 681-690, 2001.
    • (2001) Am J Pathol , vol.158 , pp. 681-690
    • Yang, P.C.1    Berin, M.C.2    Yu, L.3    Perdue, M.H.4
  • 319
    • 0030936370 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase SHP2 is positively linked to proteinase-activated receptor 2-mediated mitogenic pathway
    • Yu Z, Ahmad S, Schwartz JL, Banville D, and Shen SH. Protein-tyrosine phosphatase SHP2 is positively linked to proteinase-activated receptor 2-mediated mitogenic pathway. J Biol Chem 272: 7519-7524, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 7519-7524
    • Yu, Z.1    Ahmad, S.2    Schwartz, J.L.3    Banville, D.4    Shen, S.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.