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Volumn 394, Issue 6694, 1998, Pages 690-694

A dual thrombin receptor system for platelet activation

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM 45; MESSENGER RNA; PEPTIDE; THROMBIN; THROMBIN RECEPTOR;

EID: 0032514474     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/29325     Document Type: Article
Times cited : (902)

References (28)
  • 1
    • 0014191175 scopus 로고
    • Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets
    • Davey, M. & Luscher, E. Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets. Nature 216, 857-858 (1967).
    • (1967) Nature , vol.216 , pp. 857-858
    • Davey, M.1    Luscher, E.2
  • 2
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T.-K. H., 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).
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.-K.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 3
    • 0026690665 scopus 로고
    • The cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation. Blocking antiserum to the thrombin receptor's hirudin-like domain
    • Hung, D. T., Vu, T.-K. H., Wheaton, V. I., Ishii, K. & Coughlin, S. R. The cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation. Blocking antiserum to the thrombin receptor's hirudin-like domain. J. Clin. Invest. 89, 1350-1353 (1992).
    • (1992) J. Clin. Invest. , vol.89 , pp. 1350-1353
    • Hung, D.T.1    Vu, T.-K.H.2    Wheaton, V.I.3    Ishii, K.4    Coughlin, S.R.5
  • 4
    • 0026631543 scopus 로고
    • Structure and function of the human platelet thrombin receptor. Studies using monoclonal antibodies directed against a defined domain within the receptor N terminus
    • Brass, L. F. et al. Structure and function of the human platelet thrombin receptor. Studies using monoclonal antibodies directed against a defined domain within the receptor N terminus. J. Biol. Chem. 267, 13795-13798 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13795-13798
    • Brass, L.F.1
  • 5
    • 0026775223 scopus 로고
    • Structure-function relationships in the activation of platelet thrombin receptors by receptor-derived peptides
    • Vassallo, R. J., Kieber, E. T., Cichowski, K. & Brass, L. F. Structure-function relationships in the activation of platelet thrombin receptors by receptor-derived peptides. J. Biol. Chem. 267, 6081-6085 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 6081-6085
    • Vassallo, R.J.1    Kieber, E.T.2    Cichowski, K.3    Brass, L.F.4
  • 6
    • 0026629249 scopus 로고
    • Tethered ligand agonist peptides. Structural requirements for thrombin receptor activation reveal mechanism of proteolytic unmasking of agonist function
    • Scarborough, R. M. et al. 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
  • 7
    • 0028040603 scopus 로고
    • Species variability in platelet and other cellular responsiveness to thrombin receptor-derived peptides
    • Connolly, T. M. et al. Species variability in platelet and other cellular responsiveness to thrombin receptor-derived peptides. Thromb. Hemost. 72, 627-633 (1994).
    • (1994) Thromb. Hemost. , vol.72 , pp. 627-633
    • Connolly, T.M.1
  • 8
    • 0029016907 scopus 로고
    • Species differences in platelet responses to thrombin and SFLLRN. Receptor-mediated calcium mobilization and aggregation and regulation by protein kinases
    • Derian, C. K., Santulli, R. J., Tomko, K. A., Haertlein, B. J. & Andrade-Gordon, P. Species differences in platelet responses to thrombin and SFLLRN. Receptor-mediated calcium mobilization and aggregation and regulation by protein kinases. Thromb. Res. 6, 505-519 (1995).
    • (1995) Thromb. Res. , vol.6 , pp. 505-519
    • Derian, C.K.1    Santulli, R.J.2    Tomko, K.A.3    Haertlein, B.J.4    Andrade-Gordon, P.5
  • 9
    • 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. & 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, R.V.4    Coughlin, S.R.5
  • 10
    • 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
  • 11
    • 0023750445 scopus 로고
    • Cocoa: A new mouse model for platelet storage pool deficiency
    • Novak, E. K. et al. Cocoa: a new mouse model for platelet storage pool deficiency. Br. J. Haematol. 69, 371-378 (1988).
    • (1988) Br. J. Haematol. , vol.69 , pp. 371-378
    • Novak, E.K.1
  • 12
    • 0026072517 scopus 로고
    • Domains specifying thrombin-receptor interaction
    • Vu, T.-K. H., Wheaton, V. I., Hung, D. T. & Coughlin, S. R. Domains specifying thrombin-receptor interaction. Nature 353, 674-677 (1991).
    • (1991) Nature , vol.353 , pp. 674-677
    • Vu, T.-K.H.1    Wheaton, V.I.2    Hung, D.T.3    Coughlin, S.R.4
  • 13
    • 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. & Coughlin, S. R. 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
  • 14
    • 0026802136 scopus 로고
    • Molecular cloning of the rat vascular smooth muscle thrombin receptor. Evidence for in vitro regulation by basic fibroblast growth factor
    • Zhong, C., Hayzer, D. J., Corson, M. A. & Runge, M. S. Molecular cloning of the rat vascular smooth muscle thrombin receptor. Evidence for in vitro regulation by basic fibroblast growth factor. J. Biol. Chem. 267, 16975-16979 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16975-16979
    • Zhong, C.1    Hayzer, D.J.2    Corson, M.A.3    Runge, M.S.4
  • 15
    • 0027309290 scopus 로고
    • Kinetics of thrombin receptor cleavage on intact cells: Relation to signalling
    • Ishii, K., Hein, L., Kobilka, B. & Coughlin, S. R. Kinetics of thrombin receptor cleavage on intact cells: relation to signalling. 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
  • 16
    • 0018750813 scopus 로고
    • 2Cl: A selective affinity label for thrombin
    • 2Cl: a selective affinity label for thrombin. Thromb. Res. 14, 969-973 (1979).
    • (1979) Thromb. Res. , vol.14 , pp. 969-973
    • Kettner, C.1    Shaw, E.2
  • 17
    • 0018777994 scopus 로고
    • Thrombin-induced platelet secretion
    • Shuman, M., Botney, M. & Fenton, J. I. Thrombin-induced platelet secretion. J. Clin. Invest. 63, 1211-1218 (1979).
    • (1979) J. Clin. Invest. , vol.63 , pp. 1211-1218
    • Shuman, M.1    Botney, M.2    Fenton, J.I.3
  • 18
    • 0028100526 scopus 로고
    • Thrombin receptor activating peptide does not stimulate platelet procoagulant activity
    • Goodwin, C. A. et al. Thrombin receptor activating peptide does not stimulate platelet procoagulant activity. Biochem. Biophys. Res. Commun. 202, 321-327 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 321-327
    • Goodwin, C.A.1
  • 19
    • 0029036494 scopus 로고
    • Differential activation of cytosolic phospholipase A2 (cPLA2) by thrombin and thrombin receptor agonist peptide in human platelets. Evidence for activation of cPLA2 independent of the mitogen-activated protein kinases ERK1/2
    • Kramer, R. M. et al. Differential activation of cytosolic phospholipase A2 (cPLA2) by thrombin and thrombin receptor agonist peptide in human platelets. Evidence for activation of cPLA2 independent of the mitogen-activated protein kinases ERK1/2. J. Biol. Chem. 270, 14816-14823 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14816-14823
    • Kramer, R.M.1
  • 20
    • 0031458388 scopus 로고    scopus 로고
    • Thrombin-induced thromboxane synthesis by human platelets. Properties of anion binding exosite I-independent receptor
    • Henriksen, R. A., Samokhin, G. P. & Tracy, P. B. Thrombin-induced thromboxane synthesis by human platelets. Properties of anion binding exosite I-independent receptor. Arterioscler. Thromb. Vasc. Biol. 17, 3519-3526 (1997).
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 3519-3526
    • Henriksen, R.A.1    Samokhin, G.P.2    Tracy, P.B.3
  • 22
    • 12644304902 scopus 로고    scopus 로고
    • Disruption of the acyl-CoA:cholesterol acyltransferase gene in mice: Evidence suggesting multiple cholesterol esterification enzymes in mammals
    • Meiner, V. L. et al. Disruption of the acyl-CoA:cholesterol acyltransferase gene in mice: evidence suggesting multiple cholesterol esterification enzymes in mammals. Proc. Natl Acad. Sci. USA 93, 14041-14046 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14041-14046
    • Meiner, V.L.1
  • 23
    • 0032101592 scopus 로고    scopus 로고
    • Antibodies to protease-activated receptor 3 inhibit activation of mouse platelets by thrombin
    • Ishihara, H., Zeng, D., Connolly, A. J., Tam, C. & Coughlin, S. R. Antibodies to protease-activated receptor 3 inhibit activation of mouse platelets by thrombin. Blood 91, 4152-4157 (1998).
    • (1998) Blood , vol.91 , pp. 4152-4157
    • Ishihara, H.1    Zeng, D.2    Connolly, A.J.3    Tam, C.4    Coughlin, S.R.5
  • 25
    • 0024328536 scopus 로고
    • Altering the genome by homologous recombination
    • Capecchi, M. R. Altering the genome by homologous recombination. Science 244, 1288-1292 (1989).
    • (1989) Science , vol.244 , pp. 1288-1292
    • Capecchi, M.R.1
  • 26
    • 0026003287 scopus 로고
    • The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity
    • Liu, L., Vu, T.-K. H., Esmon, C. T. & Coughlin, S. R. The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity. J. Biol. Chem. 266, 16977-16980 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 16977-16980
    • Liu, L.1    Vu, T.-K.H.2    Esmon, C.T.3    Coughlin, S.R.4
  • 27
    • 0028209977 scopus 로고
    • Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes
    • Mathews, I. I. et al. Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Biochemistry 33, 3266-3279 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3266-3279
    • Mathews, I.I.1
  • 28
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.