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Volumn 4, Issue 12, 2003, Pages 981-990

Proteinase-activated receptors in the nervous system

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; PROTEINASE ACTIVATED RECEPTOR; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 2; PROTEINASE ACTIVATED RECEPTOR 3; PROTEINASE ACTIVATED RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 0345724732     PISSN: 1471003X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrn1255     Document Type: Review
Times cited : (115)

References (117)
  • 1
    • 0023959725 scopus 로고
    • Proopiomelanocortin processing in the pituitary, central nervous system, and peripheral tissues
    • Smith, A. I. & Funder, J. W. Proopiomelanocortin processing in the pituitary, central nervous system, and peripheral tissues. Endocr. Rev. 9, 159-179 (1988).
    • (1988) Endocr. Rev. , vol.9 , pp. 159-179
    • Smith, A.I.1    Funder, J.W.2
  • 2
    • 0036262319 scopus 로고    scopus 로고
    • Proteinase-activated receptors
    • International Union of Pharmacology. XXVIII
    • Hollenberg, M. D. & Compton, S. J. International Union of Pharmacology. XXVIII. Proteinase-activated receptors. Pharmacol. Rev. 54, 203-217 (2002).
    • (2002) Pharmacol. Rev. , vol.54 , pp. 203-217
    • Hollenberg, M.D.1    Compton, S.J.2
  • 3
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T. K., Hung, D. T., Wheaton, V. I. & Coughlin, S. R. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64, 1057-1068 (1991). Cloning of the first member of the PAR family, showing its activation by thrombin and by a peptide resembling the N terminus generated by thrombin.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 4
    • 0041317074 scopus 로고    scopus 로고
    • Proteinase-activated receptor activation by coagulation proteinases
    • Riewald, M. & Ruf, W. Proteinase-activated receptor activation by coagulation proteinases. Drug Dev. Res. 59, 400-407 (2003).
    • (2003) Drug Dev. Res. , vol.59 , pp. 400-407
    • Riewald, M.1    Ruf, W.2
  • 5
    • 0030979972 scopus 로고    scopus 로고
    • Protease-activated receptor 3 is a second thrombin receptor in humans
    • Ishihara, H. et al. Protease-activated receptor 3 is a second thrombin receptor in humans. Nature 386, 502-506 (1997).
    • (1997) Nature , vol.386 , pp. 502-506
    • Ishihara, H.1
  • 6
    • 0032499696 scopus 로고    scopus 로고
    • Cloning and characterization of human protease-activated receptor 4
    • Xu, W. F. et al. Cloning and characterization of human protease-activated receptor 4. Proc. Natl Acad. Sci. USA 95, 6642-6646 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6642-6646
    • Xu, W.F.1
  • 8
    • 0028934047 scopus 로고
    • The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression
    • Nystedt, S., Larsson, A. K., Aberg, H. & 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
  • 9
    • 15444346942 scopus 로고    scopus 로고
    • Interactions of mast cell tryptase with thrombin receptors and PAR-2
    • Molino, M. et al. Interactions of mast cell tryptase with thrombin receptors and PAR-2. J. Biol. Chem. 272, 4043-4049 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4043-4049
    • Molino, M.1
  • 10
    • 0026072517 scopus 로고
    • Domains specifying thrombin-receptor interaction
    • Vu, T. K., Wheaton, V. I., Hung, D. T., Charo, I. & Coughlin, S. R. Domains specifying thrombin-receptor interaction. Nature 353, 674-677 (1991). Definition of PAR1 cleavage as the receptor-activating mechanism.
    • (1991) Nature , vol.353 , pp. 674-677
    • Vu, T.K.1    Wheaton, V.I.2    Hung, D.T.3    Charo, I.4    Coughlin, S.R.5
  • 11
    • 0028850759 scopus 로고
    • + exchange by a thrombin receptor antagonist
    • + exchange by a thrombin receptor antagonist. Biochem. Pharmacol. 49, 519-528 (1995).
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 519-528
    • Seiler, S.M.1
  • 13
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery, O., Corvera, C. U., Steinhoff, M. & Bunnett, N. W. Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. Am. J. Physiol. 274, C1429-C1452 (1998).
    • (1998) Am. J. Physiol. , vol.274
    • Dery, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 14
    • 0037491754 scopus 로고    scopus 로고
    • Protease-activated receptor subtype expression in developing eye and adult retina of the rat after optic nerve crush
    • Rohatgi, T., Sedehizade, F., Sabel, B. A. & Reiser, G. Protease-activated receptor subtype expression in developing eye and adult retina of the rat after optic nerve crush. J. Neurosci. Res. 73, 246-254 (2003).
    • (2003) J. Neurosci. Res. , vol.73 , pp. 246-254
    • Rohatgi, T.1    Sedehizade, F.2    Sabel, B.A.3    Reiser, G.4
  • 15
    • 0029113121 scopus 로고
    • Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2
    • Nystedt, S., Emilsson, K., Larsson, A. K., Strombeck, B. & 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
  • 16
    • 0030008312 scopus 로고    scopus 로고
    • Role of the thrombin receptor in development and evidence for a second receptor
    • Connolly, A. J., Ishihara, H., Kahn, M. L., Farese, R. V. Jr & Coughlin, S. R. 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
  • 17
    • 0032510949 scopus 로고    scopus 로고
    • The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets
    • Schmidt, V. A. et al. The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets. J. Biol. Chem. 273, 15061-15068 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15061-15068
    • Schmidt, V.A.1
  • 18
    • 0032514474 scopus 로고    scopus 로고
    • A dual thrombin receptor system for platelet activation
    • Kahn, M. L. et al. A dual thrombin receptor system for platelet activation. Nature 394, 690-694 (1998).
    • (1998) Nature , vol.394 , pp. 690-694
    • Kahn, M.L.1
  • 19
    • 0034611727 scopus 로고    scopus 로고
    • PAR3 is a co-factor for PAR4 activation by thrombin
    • Nakanishi-Matsui, M. et al. PAR3 is a co-factor for PAR4 activation by thrombin. Nature 404, 609-613 (2000).
    • (2000) Nature , vol.404 , pp. 609-613
    • Nakanishi-Matsui, M.1
  • 20
    • 0033559805 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin
    • Kahn, M. L., Nakanishi-Matsui, M., Shapiro, M. J., Ishihara, H. & Coughlin, S. R. Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J. Clin. Invest. 103, 879-887 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 879-887
    • Kahn, M.L.1    Nakanishi-Matsui, M.2    Shapiro, M.J.3    Ishihara, H.4    Coughlin, S.R.5
  • 21
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • Riewald, M., Petrovan, R. J., Donner, A., Mueller, B. M. & 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
  • 22
    • 0034324177 scopus 로고    scopus 로고
    • Factor Xa activates endothelial cells by a receptor cascade between EPR-1 and PAR-2
    • Bono, F. et al. Factor Xa activates endothelial cells by a receptor cascade between EPR-1 and PAR-2. Arterioscler. Thromb. Vasc. Biol. 20, E107-E112 (2000).
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20
    • Bono, F.1
  • 23
    • 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. et al. 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
  • 25
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin, S. R. Thrombin signalling and protease-activated receptors. Nature 407, 258-264 (2000).
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 26
    • 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
  • 27
    • 0030774851 scopus 로고    scopus 로고
    • Protease-activated receptor-2 (PAR-2) is present in the rat hippocampus and is associated with neurodegeneration
    • Smith-Swintosky, V. L. et al. Protease-activated receptor-2 (PAR-2) is present in the rat hippocampus and is associated with neurodegeneration. J. Neurochem. 69, 1890-1896 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 1890-1896
    • Smith-Swintosky, V.L.1
  • 28
    • 0036285822 scopus 로고    scopus 로고
    • Four different types of protease-activated receptors are widely expressed in the brain and are up-regulated in hippocampus by severe ischemia
    • Striggow, F. et al. Four different types of protease-activated receptors are widely expressed in the brain and are up-regulated in hippocampus by severe ischemia. Eur. J. Neurosci. 14, 595-608 (2001). Determination of the neuronal localization of the four PAR subtypes and their altered expression during ischaemia.
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 595-608
    • Striggow, F.1
  • 29
    • 0036006726 scopus 로고    scopus 로고
    • Four subtypes of protease-activated receptors, co-expressed in rat astrocytes, evoke different physiological signaling
    • Wang, H., Ubl, J. J. & Reiser, G. Four subtypes of protease-activated receptors, co-expressed in rat astrocytes, evoke different physiological signaling. Glia 37, 53-63 (2002). Demonstration of the expression of all four PARs on rodent astrocytes, as well as of some downstream proliferative effects of PAR activation on astrocytes.
    • (2002) Glia , vol.37 , pp. 53-63
    • Wang, H.1    Ubl, J.J.2    Reiser, G.3
  • 30
    • 0032578046 scopus 로고    scopus 로고
    • Thrombin induced inhibition of neurite outgrowth from dorsal root ganglion neurons
    • Gill, J. S., Pitts, K., Rusnak, F. M., Owen, W. G. & Windebank, A. J. 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
  • 31
    • 0033971235 scopus 로고    scopus 로고
    • Agonists of proteinase-activated receptor 2 induce inflammation by a neurogenic mechanism
    • Steinhoff, M. et al. Agonists of proteinase-activated receptor 2 induce inflammation by a neurogenic mechanism Nature Med. 6, 151-158 (2000). This study showed the production of proinflammatory neuropeptides, calcitonin gene-related peptide and substance P on PAR2-expressing primary spinal afferent neurons, and their release on PAR2 activation.
    • (2000) Nature Med. , vol.6 , pp. 151-158
    • Steinhoff, M.1
  • 32
    • 0345004978 scopus 로고    scopus 로고
    • Thrombin and mast cell tryptase regulate guinea-pig myenteric neurons through proteinase-activated receptors-1 and -2
    • Corvera, C. U. et al. Thrombin and mast cell tryptase regulate guinea-pig myenteric neurons through proteinase-activated receptors-1 and -2. J. Physiol. (Lond.) 517, 741-756 (1999).
    • (1999) J. Physiol. (Lond.) , vol.517 , pp. 741-756
    • Corvera, C.U.1
  • 33
    • 0037335786 scopus 로고    scopus 로고
    • Mast cell tryptase and proteinase-activated receptor 2 induce hyperexcitability of guinea-pig submucosal neurons
    • Reed, D. E. et al. Mast cell tryptase and proteinase-activated receptor 2 induce hyperexcitability of guinea-pig submucosal neurons. J. Physiol. (Lond.) 547, 531-542 (2003). Demonstration that the activation of Par2 on submucosal neurons by mast-cell tryptase led to neuronal depolarization and hyperexcitability.
    • (2003) J. Physiol. (Lond.) , vol.547 , pp. 531-542
    • Reed, D.E.1
  • 34
    • 0025857712 scopus 로고
    • Prothrombin mRNA is expressed by cells of the nervous system
    • Dihanich, M., Kaser, M., Reinhard, E. Cunningham, D. & Monard, D. Prothrombin mRNA is expressed by cells of the nervous system. Neuron 6, 575-581 (1991).
    • (1991) Neuron , vol.6 , pp. 575-581
    • Dihanich, M.1    Kaser, M.2    Reinhard, E.3    Cunningham, D.4    Monard, D.5
  • 35
  • 36
    • 0028914068 scopus 로고
    • Cellular localization of thrombin receptor mRNA in rat brain: Expression by mesencephalic dopaminergic neurons and codistribution with prothrombin mRNA
    • Weinstein, J. R., Gold, S. J., Cunningham, D. D. & Gall, C. M. 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
  • 37
    • 0033435136 scopus 로고    scopus 로고
    • Expression of factor X in both the rat brain and cells of the central nervous system
    • Shikamoto, Y. & Morita, T. Expression of factor X in both the rat brain and cells of the central nervous system. FEBS Lett. 463, 387-389 (1999).
    • (1999) FEBS Lett. , vol.463 , pp. 387-389
    • Shikamoto, Y.1    Morita, T.2
  • 38
    • 0023332815 scopus 로고
    • Intestinal mucosal mast cells in normal and nematode-infected rat intestines are in intimate contact with peptidergic nerves
    • Stead, R. H. et al. 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
  • 39
    • 0025055444 scopus 로고
    • Mast cells: The immune gate to the brain
    • Thecharides, T. C. Mast cells: the immune gate to the brain. Life Sci 46, 607-617 (1990).
    • (1990) Life Sci , vol.46 , pp. 607-617
    • Thecharides, T.C.1
  • 40
    • 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. & 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
  • 41
    • 0027743598 scopus 로고
    • Cloning of the cDNA encoding human brain trypsinogen and characterization of its product
    • Wiegand, U., Corbach, S., Minn, A., Kang, J. & Muller-Hill, B. Cloning of the cDNA encoding human brain trypsinogen and characterization of its product. Gene 136, 167-175 (1993).
    • (1993) Gene , vol.136 , pp. 167-175
    • Wiegand, U.1    Corbach, S.2    Minn, A.3    Kang, J.4    Muller-Hill, B.5
  • 42
    • 0025255579 scopus 로고
    • Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1
    • Cavanaugh, K. P., Gurwitz, D., Cunningham, D. D. & Bradshaw, R. A. Reciprocal modulation of astrocyte stellation by thrombin and protease nexin-1. J. Neurochem. 54, 1736-1743 (1990).
    • (1990) J. Neurochem. , vol.54 , pp. 1736-1743
    • Cavanaugh, K.P.1    Gurwitz, D.2    Cunningham, D.D.3    Bradshaw, R.A.4
  • 43
    • 0028085095 scopus 로고
    • Thrombin receptor peptides induce shape change in neonatal murine astrocytes in culture
    • Beecher, K. L., Andersen, T. T., Fenton, J. W. & Festoff, B. W. 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.3    Festoff, B.W.4
  • 44
    • 0028873060 scopus 로고
    • Thrombin receptor activation stimulates astrocyte proliferation and reversal of stellation by distinct pathways: Involvement of tyrosine phosphorylation
    • Grabham, P. & Cunningham, D. D. Thrombin receptor activation stimulates astrocyte proliferation and reversal of stellation by distinct pathways: involvement of tyrosine phosphorylation. J. Neurochem. 64, 583-591 (1995).
    • (1995) J. Neurochem. , vol.64 , pp. 583-591
    • Grabham, P.1    Cunningham, D.D.2
  • 46
    • 0036838021 scopus 로고    scopus 로고
    • Thrombin (PAR-1)-induced proliferation in astrocytes via MAPK involves multiple signaling pathways
    • Wang, H., Ubl, J. J., Stricker, R. & Reiser, G. Thrombin (PAR-1)-induced proliferation in astrocytes via MAPK involves multiple signaling pathways Am. J. Physiol. Cell. Physiol. 283, C1351-C1364 (2002). Demonstration of the involvement of the extracellular signal-regulated kinase and PLC pathways in thrombin-induced astrocytic proliferation.
    • (2002) Am. J. Physiol. Cell. Physiol. , vol.283
    • Wang, H.1    Ubl, J.J.2    Stricker, R.3    Reiser, G.4
  • 47
    • 0037332454 scopus 로고    scopus 로고
    • 2+-sensitive tyrosine kinase Pyk2 and Src in thrombin signalling in rat astrocytes
    • 2+-sensitive tyrosine kinase Pyk2 and Src in thrombin signalling in rat astrocytes. J. Neurochem. 84, 1349-1357 (2003).
    • (2003) J. Neurochem. , vol.84 , pp. 1349-1357
    • Wang, H.1    Reiser, G.2
  • 48
    • 0027470910 scopus 로고
    • Thrombin is a regulator of astrocytic endothelin-1
    • Ehrenreich, H. et al. Thrombin is a regulator of astrocytic endothelin-1 Brain Res. 600, 201-207 (1993).
    • (1993) Brain Res. , vol.600 , pp. 201-207
    • Ehrenreich, H.1
  • 49
    • 0027510492 scopus 로고
    • Enhancement of the synthesis and secretion of nerve growth factor in primary cultures of glial cells by proteases: A possible involvement of thrombin
    • Neveu, I., Jehan, F., Jandrot-Perrus, M., Wion, D. & Brachet, P. Enhancement of the synthesis and secretion of nerve growth factor in primary cultures of glial cells by proteases: a possible involvement of thrombin. J. Neurochem. 60, 858-867 (1993).
    • (1993) J. Neurochem. , vol.60 , pp. 858-867
    • Neveu, I.1    Jehan, F.2    Jandrot-Perrus, M.3    Wion, D.4    Brachet, P.5
  • 50
    • 0029896145 scopus 로고    scopus 로고
    • Transduction mechanisms involved in thrombin receptor-induced nerve growth factor secretion and cell division in primary cultures of astrocytes
    • Debeir, T., Gueugnon, J., Vige, X. & Benavides, J. Transduction mechanisms involved in thrombin receptor-induced nerve growth factor secretion and cell division in primary cultures of astrocytes. J. Neurochem. 66, 2320-2328 (1996).
    • (1996) J. Neurochem. , vol.66 , pp. 2320-2328
    • Debeir, T.1    Gueugnon, J.2    Vige, X.3    Benavides, J.4
  • 51
    • 0029790022 scopus 로고    scopus 로고
    • Exposure of astrocytes to thrombin reduces levels of the metabotropic glutamate receptor mGluR5
    • Miller, S., Sehati, N., Romano, C. & Cotman, C. W. Exposure of astrocytes to thrombin reduces levels of the metabotropic glutamate receptor mGluR5. J. Neurochem. 67, 1435-1447 (1996).
    • (1996) J. Neurochem. , vol.67 , pp. 1435-1447
    • Miller, S.1    Sehati, N.2    Romano, C.3    Cotman, C.W.4
  • 52
    • 0027196148 scopus 로고
    • Glutamate induces the growth factors NGF, bFGE the receptor FGF-R1 and c-fos mRNA expression in rat astrocyte culture
    • Pechan, P. A., Chowdhury, K., Gerdes, W. & Seifert, W. Glutamate induces the growth factors NGF, bFGE the receptor FGF-R1 and c-fos mRNA expression in rat astrocyte culture. Neurosci. Lett. 153, 111-114 (1993).
    • (1993) Neurosci. Lett. , vol.153 , pp. 111-114
    • Pechan, P.A.1    Chowdhury, K.2    Gerdes, W.3    Seifert, W.4
  • 53
    • 0030886438 scopus 로고    scopus 로고
    • The metabotropic glutamate receptor mGluR5 induces calcium oscillations in cultured astrocytes via protein kinase C phosphorylation
    • Nakahara, K., Okada, M. & Nakanishi, S. The metabotropic glutamate receptor mGluR5 induces calcium oscillations in cultured astrocytes via protein kinase C phosphorylation. J. Neurochem. 69, 1467-1475 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 1467-1475
    • Nakahara, K.1    Okada, M.2    Nakanishi, S.3
  • 54
    • 0033083661 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor agonists reduce glutamate release from cultured astrocytes
    • Ye, Z. C. & Sontheimer, H. Metabotropic glutamate receptor agonists reduce glutamate release from cultured astrocytes Glia 25, 270-281 (1999).
    • (1999) Glia , vol.25 , pp. 270-281
    • Ye, Z.C.1    Sontheimer, H.2
  • 55
    • 0011811083 scopus 로고
    • Thrombin modulates and reverses neuroblastoma neurite outgrowth
    • Gurwitz, D. & Cunningham, D. D. 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
  • 56
    • 0022897760 scopus 로고
    • A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins
    • Gloor, S., Odink, K., Guenther, J., Nick, H. & Monard, D. A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins. Cell 47, 687-893 (1986).
    • (1986) Cell , vol.47 , pp. 687-893
    • Gloor, S.1    Odink, K.2    Guenther, J.3    Nick, H.4    Monard, D.5
  • 57
    • 0343742615 scopus 로고    scopus 로고
    • Involvement of protease-activated receptor-1 in the in vitro development of mesencephalic dopaminergic neurons
    • Debeir, T., Benavides, J. & Vige, X. Involvement of protease-activated receptor-1 in the in vitro development of mesencephalic dopaminergic neurons. Neuroscience 82, 739-752 (1998).
    • (1998) Neuroscience , vol.82 , pp. 739-752
    • Debeir, T.1    Benavides, J.2    Vige, X.3
  • 58
    • 17344365478 scopus 로고    scopus 로고
    • Thrombin perturbs neurite outgrowth and induces apoptotic cell death in enriched chick spinal motoneuron cultures through caspase activation
    • Turgeon, V. L., Lloyd, E. D., Wang, S., Festoff, B. W. & Houenou, L. J. 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
  • 59
    • 0023698784 scopus 로고
    • Cell-derived proteases and protease inhibitors as regulators of neurite outgrowth
    • Monard, D. Cell-derived proteases and protease inhibitors as regulators of neurite outgrowth. Trends Neurosci. 11, 541-544 (1988).
    • (1988) Trends Neurosci. , vol.11 , pp. 541-544
    • Monard, D.1
  • 60
    • 0027948168 scopus 로고
    • Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction
    • Liu, Y., Fields, R. D., Festoff, B. W. & Nelson, P. G. Proteolytic action of thrombin is required for electrical activity-dependent synapse reduction. Proc. Natl Acad. Sci. USA 91, 10300-10304 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10300-10304
    • Liu, Y.1    Fields, R.D.2    Festoff, B.W.3    Nelson, P.G.4
  • 62
    • 0034660448 scopus 로고    scopus 로고
    • Potentiation of NMDA receptor function by the serine protease thrombin
    • Gingdch, M. B., Junge, C. E., Lyuboslavsky, P. & Traynelis, S. F. Potentiation of NMDA receptor function by the serine protease thrombin. J. Neurosci. 20, 4582-4595 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 4582-4595
    • Gingdch, M.B.1    Junge, C.E.2    Lyuboslavsky, P.3    Traynelis, S.F.4
  • 63
    • 0034888212 scopus 로고    scopus 로고
    • Agonists of proteinase-activated receptor 1 induce plasma extravasation by a neurogenic mechanism
    • de Garavilla, L. et al. Agonists of proteinase-activated receptor 1 induce plasma extravasation by a neurogenic mechanism. Br. J. Pharmacol. 133, 975-987 (2001).
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 975-987
    • De Garavilla, L.1
  • 64
    • 0035941170 scopus 로고    scopus 로고
    • Agonists of proteinase-activated receptor 2 excite guinea pig ileal myenteric neurons
    • Linden, D. R., Manning, B. P., Bunnett, N. W. & Mawe, G. M. 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
  • 65
    • 0142243114 scopus 로고    scopus 로고
    • Stimulation of the proteinase-activated receptor 2 excites jejunal afferent nerves in anaesthetised rats
    • Kirkup, A. J., Jiang, W., Bunnett, N. W. & Grundy, D. Stimulation of the proteinase-activated receptor 2 excites jejunal afferent nerves in anaesthetised rats. J. Physiol. 552, 589-601 (2003).
    • (2003) J. Physiol. , vol.552 , pp. 589-601
    • Kirkup, A.J.1    Jiang, W.2    Bunnett, N.W.3    Grundy, D.4
  • 66
    • 0036828264 scopus 로고    scopus 로고
    • Serine proteases excite myenteric neurons through protease-activated receptors in guinea pig small intestine
    • Gao, C. et al. 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
  • 67
    • 0036193921 scopus 로고    scopus 로고
    • Proteinase-activated receptor-1 agonists attenuate nociception in response to noxious stimuli
    • Asfaha, S., Brussee, V., Chapman, K., Zochodne, D. W. & 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
  • 68
    • 0034927070 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2 and hyperalgesia: A novel pain pathway
    • Vergnolle, N. et al. Proteinase-activated receptor-2 and hyperalgesia: a novel pain pathway. Nature Med. 7, 821-826 (2001). Demonstration of neurokinin-1-receptor-dependent and PAR2-induced thermal and mechanical hyperalgesia.
    • (2001) Nature Med. , vol.7 , pp. 821-826
    • Vergnolle, N.1
  • 69
    • 0035890075 scopus 로고    scopus 로고
    • The proteinase-activated receptor 2 is involved in nociception
    • Hoogerwerf, W. A. et al. The proteinase-activated receptor 2 is involved in nociception. J. Neurosci. 21, 9036-9042 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 9036-9042
    • Hoogerwerf, W.A.1
  • 70
    • 0038720558 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2 mediates itch: A novel pathway for pruritus in human skin
    • Steinhoff, M. et al. Proteinase-activated receptor-2 mediates itch: a novel pathway for pruritus in human skin. J. Neurosci. 23, 6176-6180 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 6176-6180
    • Steinhoff, M.1
  • 71
    • 0032968080 scopus 로고    scopus 로고
    • Injury-induced gelatinase and thrombin-like activities in regenerating and nonregenerating nervous systems
    • Friedmann, I., Faber-Elman, A., Yoles, E. & Schwartz, M. Injury-induced gelatinase and thrombin-like activities in regenerating and nonregenerating nervous systems. FASEB J. 13, 533-543 (1999).
    • (1999) FASEB J. , vol.13 , pp. 533-543
    • Friedmann, I.1    Faber-Elman, A.2    Yoles, E.3    Schwartz, M.4
  • 72
    • 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, S. P., Suidan, H. S., Pavlik, A., Vejsada, R. & 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
  • 73
    • 0033798625 scopus 로고    scopus 로고
    • Intestinal type 2 proteinase-activated receptors: Expression in opioid-sensitive secretomotor neural circuits that mediate epithelial ion transport
    • Green, B. T., Bunnett, N. W., Kulkarni-Narla, A., Steinhoff, M. & Brown, D. R. 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
  • 74
    • 0034983372 scopus 로고    scopus 로고
    • The protease-activated receptor-2 agonist induces gastric mucus secretion and mucosal cytoprotection
    • Kawabata, A. et al. The protease-activated receptor-2 agonist induces gastric mucus secretion and mucosal cytoprotection. J. Clin. Invest 107, 1443-1450 (2001).
    • (2001) J. Clin. Invest. , vol.107 , pp. 1443-1450
    • Kawabata, A.1
  • 75
    • 0037040862 scopus 로고    scopus 로고
    • Protease-activated receptor-2 activation causes EDHF-like coronary vasodilaton: Selective preservation in ischemia/reperfusion injury: Involvement of lipoxygenase products, VR1 receptors, and C-fibers
    • McLean, P. G., Aston, D., Sarkar, D. & Ahluwalia, A. Protease-activated receptor-2 activation causes EDHF-like coronary vasodilaton: selective preservation in ischemia/reperfusion injury: involvement of lipoxygenase products, VR1 receptors, and C-fibers. Circ. Res. 90, 465-472 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 465-472
    • McLean, P.G.1    Aston, D.2    Sarkar, D.3    Ahluwalia, A.4
  • 77
    • 0030007646 scopus 로고    scopus 로고
    • Thrombin, its receptor and protease nexin I, its potent serpin, in the nervous system
    • Festoff, B. W., Smirnova, I. V., Ma, J. & Citron, B. A. 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
  • 78
    • 16944366731 scopus 로고    scopus 로고
    • Thrombin induces apoptosis in cultured neurons and astrocytes via a pathway requiring tyrosine kinase and RhoA activities
    • Donovan, F. M., Pike, C. J., Cotman, C. W. & Cunningham, D. D. 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
  • 79
    • 0029012029 scopus 로고
    • Thrombin receptor activation protects neurons and astrocytes from cell death produced by environmental insults
    • Vaughan, P. J., Pike, C. J., Cotman, C. W. & Cunningham, D. D. Thrombin receptor activation protects neurons and astrocytes from cell death produced by environmental insults. J. Neurosci. 15, 5389-5401 (1995). This report showed that PAR1 activation could protect neurons and astrocytes from the deleterious effects of glucose/growth supplement deprivation or oxidative stress.
    • (1995) J. Neurosci. , vol.15 , pp. 5389-5401
    • Vaughan, P.J.1    Pike, C.J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 81
    • 0034186091 scopus 로고    scopus 로고
    • Motor neuron cell death in wobbler mutant mice follows overexpression of the G-protein-coupled, protease-activated receptor for thrombin
    • Festoff, B. W. et al. Motor neuron cell death in wobbler mutant mice follows overexpression of the G-protein-coupled, protease-activated receptor for thrombin. Mol. Med. 6, 410-429 (2000).
    • (2000) Mol. Med. , vol.6 , pp. 410-429
    • Festoff, B.W.1
  • 82
    • 0344923324 scopus 로고    scopus 로고
    • Up-regulation of proteinase-activated receptor 1 expression in astrocytes during HIV encephalitis
    • Boven, L. A. et al. Up-regulation of proteinase-activated receptor 1 expression in astrocytes during HIV encephalitis. J. Immunol. 170, 2638-2646 (2003). Demonstration of the proinflammatory role of astrocytic PAR1 activation in HIV encephalitis.
    • (2003) J. Immunol. , vol.170 , pp. 2638-2646
    • Boven, L.A.1
  • 83
    • 0033822556 scopus 로고    scopus 로고
    • Thrombin-induced activation of cultured rodent microglia
    • Moller, T., Hanisch, U. K. & Ransom, B. R. Thrombin-induced activation of cultured rodent microglia J. Neurochem. 75, 1539-1547 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 1539-1547
    • Moller, T.1    Hanisch, U.K.2    Ransom, B.R.3
  • 84
    • 0036326804 scopus 로고    scopus 로고
    • Participation of protease-activated receptor-1 in thrombin-induced microglial activation
    • Suo, Z. et al. Participation of protease-activated receptor-1 in thrombin-induced microglial activation. J. Neurochem. 80, 655-666 (2002).
    • (2002) J. Neurochem. , vol.80 , pp. 655-666
    • Suo, Z.1
  • 85
    • 0032557654 scopus 로고    scopus 로고
    • Signaling pathways involved in thrombin-induced cell protection
    • Donovan, F. M. & Cunningham, D. D. 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
  • 86
    • 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. et al. 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). Report of the neuroprotective/degenerative roles of the thrombin/PAR1 axis in ischaemia.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2264-2269
    • Striggow, F.1
  • 87
    • 0033000918 scopus 로고    scopus 로고
    • Attenuation of thrombin-induced brain edema by cerebral thrombin preconditioning
    • Xi, G., Keep, R. F., Hua, Y., Xiang, J. & Hoff, J. T. Attenuation of thrombin-induced brain edema by cerebral thrombin preconditioning. Stroke 30, 1247-1255 (1999).
    • (1999) Stroke , vol.30 , pp. 1247-1255
    • Xi, G.1    Keep, R.F.2    Hua, Y.3    Xiang, J.4    Hoff, J.T.5
  • 88
    • 0035937433 scopus 로고    scopus 로고
    • Activation of p44/42 mitogen activated protein kinases in thrombin-induced brain tolerance
    • Xi, G., Hua, Y., Keep, R. F., Duong, H. K. & Hoff, J. T. Activation of p44/42 mitogen activated protein kinases in thrombin-induced brain tolerance. Brain Res 895, 153-159 (2001).
    • (2001) Brain Res , vol.895 , pp. 153-159
    • Xi, G.1    Hua, Y.2    Keep, R.F.3    Duong, H.K.4    Hoff, J.T.5
  • 89
    • 0027326873 scopus 로고
    • Thrombin may contribute to the pathophysiology of central nervous system injury
    • Nishino, A. et al. Thrombin may contribute to the pathophysiology of central nervous system injury. J. Neurotrauma 10, 167-179 (1993).
    • (1993) J. Neurotrauma , vol.10 , pp. 167-179
    • Nishino, A.1
  • 90
    • 0030829885 scopus 로고    scopus 로고
    • The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system
    • Turgeon, V. L. & Houenou, L. J. The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system. Brain Res. Brain Res. Rev. 25, 85-95 (1997).
    • (1997) Brain Res. Brain Res. Rev. , vol.25 , pp. 85-95
    • Turgeon, V.L.1    Houenou, L.J.2
  • 91
    • 0028566867 scopus 로고
    • Protease nexin-1, a potent thrombin inhibitor, is reduced around cerebral blood vessels in Alzheimer's disease
    • Vaughan, P. J., Su, J., Cotman, C. W. & Cunningham, D. D. Protease nexin-1, a potent thrombin inhibitor, is reduced around cerebral blood vessels in Alzheimer's disease. Brain Res. 668, 160-170 (1994).
    • (1994) Brain Res. , vol.668 , pp. 160-170
    • Vaughan, P.J.1    Su, J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 92
    • 0029914487 scopus 로고    scopus 로고
    • Thrombin attenuates neuronal cell death and modulates astrocyte reactivity induced by β-amyloid in vitro
    • Pike, C. J., Vaughan, P. J., Cunningham, D. D. & Cotman, C. W. Thrombin attenuates neuronal cell death and modulates astrocyte reactivity induced by β-amyloid in vitro. J. Neurochem 66, 1374-1382 (1996).
    • (1996) J. Neurochem. , vol.66 , pp. 1374-1382
    • Pike, C.J.1    Vaughan, P.J.2    Cunningham, D.D.3    Cotman, C.W.4
  • 93
    • 0035235444 scopus 로고    scopus 로고
    • Neuroimmune and neurovirological aspects of human immunodeficiency virus infection
    • Power, C. & Johnson, R. T. Neuroimmune and neurovirological aspects of human immunodeficiency virus infection. Adv. Virus Res. 56, 389-433 (2001).
    • (2001) Adv. Virus Res. , vol.56 , pp. 389-433
    • Power, C.1    Johnson, R.T.2
  • 94
    • 0036194251 scopus 로고    scopus 로고
    • Progress in clinical neurosciences: The neuropathogenesis of HIV infection: Host-virus interaction and the impact of therapy
    • Power, C., Gill, M. J. & Johnson, R. T. Progress in clinical neurosciences: the neuropathogenesis of HIV infection: host-virus interaction and the impact of therapy. Can. J. Neurol. Sci. 29, 19-32 (2002).
    • (2002) Can. J. Neurol. Sci. , vol.29 , pp. 19-32
    • Power, C.1    Gill, M.J.2    Johnson, R.T.3
  • 95
    • 0025969914 scopus 로고
    • The V3 loops of the HIV-1 and HIV-2 surface glycoproteins contain proteolytic cleavage sites: A possible function in viral fusion?
    • Clements, G. J. et al. The V3 loops of the HIV-1 and HIV-2 surface glycoproteins contain proteolytic cleavage sites: a possible function in viral fusion? AIDS Res. Hum. Retroviruses 7, 3-16 (1991).
    • (1991) AIDS Res. Hum. Retroviruses , vol.7 , pp. 3-16
    • Clements, G.J.1
  • 96
    • 0027481774 scopus 로고
    • Effect of mutations in the V3 loop of HIV-1 gp120 on infectivity and susceptibility to proteolytic cleavage
    • Schulz, T. F. et al. Effect of mutations in the V3 loop of HIV-1 gp120 on infectivity and susceptibility to proteolytic cleavage. AIDS Res. Hum. Retroviruses 9, 159-166 (1993).
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 159-166
    • Schulz, T.F.1
  • 97
    • 0028103736 scopus 로고
    • Conformational rearrangements required of the V3 loop of HIV-1 gp120 for proteolytic cleavage and infection
    • Johnson, M. E., Lin, Z., Padmanabhan, K., Tulinsky, A. & Kahn, M. Conformational rearrangements required of the V3 loop of HIV-1 gp120 for proteolytic cleavage and infection. FEBS Lett. 337, 4-8 (1994).
    • (1994) FEBS Lett. , vol.337 , pp. 4-8
    • Johnson, M.E.1    Lin, Z.2    Padmanabhan, K.3    Tulinsky, A.4    Kahn, M.5
  • 99
    • 0030445074 scopus 로고    scopus 로고
    • Cellular proteases involved in the pathogenicity of enveloped animal viruses, human immunodeficiency virus, infuenza virus A and Sendai virus
    • Kido, H., Niwa, Y., Beppu, Y. & Towatari, T. Cellular proteases involved in the pathogenicity of enveloped animal viruses, human immunodeficiency virus, infuenza virus A and Sendai virus. Adv. Enzyme Regul. 36, 325-347 (1996).
    • (1996) Adv. Enzyme Regul. , vol.36 , pp. 325-347
    • Kido, H.1    Niwa, Y.2    Beppu, Y.3    Towatari, T.4
  • 100
    • 0030339827 scopus 로고    scopus 로고
    • Cellular proteases involved in the pathogenicity of human immunodeficiency and influenza viruses
    • Kido, H., Towatari, T., Niwa, Y., Okumura, Y. & Beppu, Y. Cellular proteases involved in the pathogenicity of human immunodeficiency and influenza viruses. Adv. Exp. Med. Biol. 389, 233-240 (1996).
    • (1996) Adv. Exp. Med. Biol. , vol.389 , pp. 233-240
    • Kido, H.1    Towatari, T.2    Niwa, Y.3    Okumura, Y.4    Beppu, Y.5
  • 101
    • 0029876273 scopus 로고    scopus 로고
    • T-cell membrane-associated serine protease, tryptase TL2, binds human immunodeficiency virus type 1 gp120 and cleaves the third-variable-domain loop of gp120, Neutralizing antibodies of human immunodeficiency virus type 1 inhibit cleavage of gp120
    • Niwa, Y., Yano, M., Futaki, S., Okumura, Y. & Kido, H. T-cell membrane-associated serine protease, tryptase TL2, binds human immunodeficiency virus type 1 gp120 and cleaves the third-variable-domain loop of gp120, Neutralizing antibodies of human immunodeficiency virus type 1 inhibit cleavage of gp120. Eur. J. Biochem. 237, 64-70 (1996).
    • (1996) Eur. J. Biochem. , vol.237 , pp. 64-70
    • Niwa, Y.1    Yano, M.2    Futaki, S.3    Okumura, Y.4    Kido, H.5
  • 102
    • 0027536055 scopus 로고
    • Interaction between a membrane-associated serine proteinase of U-937 monocytes and peptides from the V3 loop of the human immunodeficiency virus type 1 (HIV-1) gp120 envelope glycoprotein
    • Avril, L. E., Di Martino-Ferrer, M., Barin, F. & Gauthier, F. Interaction between a membrane-associated serine proteinase of U-937 monocytes and peptides from the V3 loop of the human immunodeficiency virus type 1 (HIV-1) gp120 envelope glycoprotein. FEBS Lett. 317, 167-172 (1993).
    • (1993) FEBS Lett. , vol.317 , pp. 167-172
    • Avril, L.E.1    Di Martino-Ferrer, M.2    Barin, F.3    Gauthier, F.4
  • 103
    • 0028360298 scopus 로고
    • Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G
    • Avril, L. E., Di Martino-Ferrer, M., Pignede, G., Seman, M. & Gauthier, F. Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 345, 81-86 (1994).
    • (1994) FEBS Lett. , vol.345 , pp. 81-86
    • Avril, L.E.1    Di Martino-Ferrer, M.2    Pignede, G.3    Seman, M.4    Gauthier, F.5
  • 104
    • 0029075688 scopus 로고
    • Inhibition of U-937 membrane-associated cathepsin G by GP120 (IIIB) and V3 loop-derived peptides from several strains of HIV-1
    • Avdl, L. E., di Martino-Ferrer, M., Brillard-Bourdet, M. & Gauthier, F. Inhibition of U-937 membrane-associated cathepsin G by GP120 (IIIB) and V3 loop-derived peptides from several strains of HIV-1. FEBS Lett. 367, 251-256 (1995).
    • (1995) FEBS Lett. , vol.367 , pp. 251-256
    • Avdl, L.E.1    Di Martino-Ferrer, M.2    Brillard-Bourdet, M.3    Gauthier, F.4
  • 105
    • 0027092473 scopus 로고
    • Characterization of a neutralizing monoclonal antibody to the external glycoprotein of HIV-1
    • Pal, R. et al. Characterization of a neutralizing monoclonal antibody to the external glycoprotein of HIV-1. Intervirology 34, 86-93 (1992).
    • (1992) Intervirology , vol.34 , pp. 86-93
    • Pal, R.1
  • 106
    • 0027332080 scopus 로고
    • Role of HIV-1 envelope V3 loop cleavage in cell tropism
    • Gu, R., Westervelt, P. & Ratner, L. Role of HIV-1 envelope V3 loop cleavage in cell tropism. AIDS Res. Hum. Retroviruses. 9, 1007-1015 (1993).
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1007-1015
    • Gu, R.1    Westervelt, P.2    Ratner, L.3
  • 107
    • 0037265689 scopus 로고    scopus 로고
    • The role of thrombin and thrombin receptors in ischemic, hemorrhagic and traumatic brain injury: Deleterious or protective?
    • Xi, G., Reiser, G. & Keep, R. F. The role of thrombin and thrombin receptors in ischemic, hemorrhagic and traumatic brain injury: deleterious or protective? J. Neurochem. 84, 3-9 (2003).
    • (2003) J. Neurochem. , vol.84 , pp. 3-9
    • Xi, G.1    Reiser, G.2    Keep, R.F.3
  • 108
    • 0034731502 scopus 로고    scopus 로고
    • Proteinase-activated receptor-1 regulation of macrophage elastase (MMP-12) secretion by serine proteinases
    • Raza, S. L., Nehring, L. C., Shapiro, S. D. & Cornelius, L. A. Proteinase-activated receptor-1 regulation of macrophage elastase (MMP-12) secretion by serine proteinases. J. Biol. Chem. 275, 41243-41250 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 41243-41250
    • Raza, S.L.1    Nehring, L.C.2    Shapiro, S.D.3    Cornelius, L.A.4
  • 109
    • 0038443057 scopus 로고    scopus 로고
    • Intracerebral hemorrhage induces macrophage activation and matrix metalloproteinases
    • Power, C. et al. Intracerebral hemorrhage induces macrophage activation and matrix metalloproteinases. Ann. Neurol. 53, 731-742 (2003).
    • (2003) Ann. Neurol. , vol.53 , pp. 731-742
    • Power, C.1
  • 110
    • 0025107628 scopus 로고
    • Identification of IgE-positive cells and mast cells in frozen sections of multiple sclerosis brains
    • Toms, R., Weiner H. L. & Johnson, D. Identification of IgE-positive cells and mast cells in frozen sections of multiple sclerosis brains. J. Neuroimmunol. 30, 169-177 (1990).
    • (1990) J. Neuroimmunol. , vol.30 , pp. 169-177
    • Toms, R.1    Weiner, H.L.2    Johnson, D.3
  • 112
    • 0037452593 scopus 로고    scopus 로고
    • Multiple elements of the allergic arm of the immune response modulate autoimmune demyelination
    • Pedotti, R. et al. Multiple elements of the allergic arm of the immune response modulate autoimmune demyelination. Proc. Natl Acad. Sci. USA 100, 1867-1872 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1867-1872
    • Pedotti, R.1
  • 113
    • 0036105484 scopus 로고    scopus 로고
    • Gene-microarray analysis of multiple sclerosis lesions yields new targets validated in autoimmune encephalomyelitis
    • Lock, C. et al. Gene-microarray analysis of multiple sclerosis lesions yields new targets validated in autoimmune encephalomyelitis. Nature Med. 8, 500-508 (2002).
    • (2002) Nature Med. , vol.8 , pp. 500-508
    • Lock, C.1
  • 114
    • 0028908819 scopus 로고
    • Elevated mast cell tryptase in cerebrospinal fluid of multiple sclerosis patients
    • Rozniecki, J. J., Hauser, S. L., Stein, M., Lincoln, R. & Theoharides, T. C. Elevated mast cell tryptase in cerebrospinal fluid of multiple sclerosis patients. Ann. Neurol. 37, 63-66 (1995).
    • (1995) Ann. Neurol. , vol.37 , pp. 63-66
    • Rozniecki, J.J.1    Hauser, S.L.2    Stein, M.3    Lincoln, R.4    Theoharides, T.C.5
  • 115
    • 0033982381 scopus 로고    scopus 로고
    • Proteinase-activated receptors (PARs): Activation of PAR1 and PAR2 by a proteolytic fragment of the neuronal growth associated protein B-50/GAP-43
    • Hollenberg, M. D., Saifeddine, M. & Zwiers, H. Proteinase-activated receptors (PARs): activation of PAR1 and PAR2 by a proteolytic fragment of the neuronal growth associated protein B-50/GAP-43. Can. J. Physiol. Pharmacol. 78, 81-85 (2000).
    • (2000) Can. J. Physiol. Pharmacol. , vol.78 , pp. 81-85
    • Hollenberg, M.D.1    Saifeddine, M.2    Zwiers, H.3
  • 116
    • 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. et al. 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
  • 117
    • 0033532076 scopus 로고    scopus 로고
    • Thrombin induces proteinase-activated receptor-1 gene expression in endothelial cells via activation of Gi-linked Ras/mitogen-activated protein kinase pathway
    • Ellis, C. A. et al. Thrombin induces proteinase-activated receptor-1 gene expression in endothelial cells via activation of Gi-linked Ras/mitogen-activated protein kinase pathway J. Biol. Chem. 274, 13718-13727 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13718-13727
    • Ellis, C.A.1


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