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Volumn 129, Issue 7, 2017, Pages 883-895

A novel mechanism regulating human platelet activation by MMP-2-mediated PAR1 biased signaling

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA1 INTEGRIN; GELATINASE A; HEMOPEXIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEINASE ACTIVATED RECEPTOR 1; FIBRINOGEN RECEPTOR; MMP2 PROTEIN, HUMAN;

EID: 85014973270     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2016-06-724245     Document Type: Article
Times cited : (61)

References (62)
  • 1
    • 0037155057 scopus 로고    scopus 로고
    • Matrix metalloproteinases in vascular remodeling and atherogenesis: The good, the bad, and the ugly
    • Galis ZS, Khatri JJ. Matrix metalloproteinases in vascular remodeling and atherogenesis: the good, the bad, and the ugly. Circ Res. 2002;90(3):251-262.
    • (2002) Circ Res , vol.90 , Issue.3 , pp. 251-262
    • Galis, Z.S.1    Khatri, J.J.2
  • 2
    • 84887014442 scopus 로고    scopus 로고
    • Platelets and matrix metalloproteinases
    • Seizer P, May AE. Platelets and matrix metalloproteinases. Thromb Haemost. 2013;110(5):903-909.
    • (2013) Thromb Haemost , vol.110 , Issue.5 , pp. 903-909
    • Seizer, P.1    May, A.E.2
  • 3
    • 76049125185 scopus 로고    scopus 로고
    • Matrix metalloproteinases and peripheral arterial disease
    • Busti C, Falcinelli E, Momi S, Gresele P. Matrix metalloproteinases and peripheral arterial disease. Intern Emerg Med. 2010;5(1):13-25.
    • (2010) Intern Emerg Med , vol.5 , Issue.1 , pp. 13-25
    • Busti, C.1    Falcinelli, E.2    Momi, S.3    Gresele, P.4
  • 5
    • 0037205285 scopus 로고    scopus 로고
    • Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function
    • Galt SW, Lindemann S, Allen L, et al. Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function. Circ Res. 2002;90(10):1093-1099.
    • (2002) Circ Res , vol.90 , Issue.10 , pp. 1093-1099
    • Galt, S.W.1    Lindemann, S.2    Allen, L.3
  • 6
    • 0034331185 scopus 로고    scopus 로고
    • Platelet release of trimolecular complex components MT1-MMP/TIMP2/MMP2: Involvement in MMP2 activation and platelet aggregation
    • Kazes I, Elalamy I, Sraer JD, Hatmi M, Nguyen G. Platelet release of trimolecular complex components MT1-MMP/TIMP2/MMP2: involvement in MMP2 activation and platelet aggregation. Blood. 2000;96(9):3064-3069.
    • (2000) Blood , vol.96 , Issue.9 , pp. 3064-3069
    • Kazes, I.1    Elalamy, I.2    Sraer, J.D.3    Hatmi, M.4    Nguyen, G.5
  • 7
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase A during platelet activation mediates aggregation
    • Sawicki G, Salas E, Murat J, Miszta-Lane H, Radomski MW. Release of gelatinase A during platelet activation mediates aggregation. Nature. 1997;386(6625):616-619.
    • (1997) Nature , vol.386 , Issue.6625 , pp. 616-619
    • Sawicki, G.1    Salas, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 8
    • 80051907306 scopus 로고    scopus 로고
    • Megakaryocytes differentially sort mRNAs for matrix metalloproteinases and their inhibitors into platelets: A mechanism for regulating synthetic events
    • Cecchetti L, Tolley ND, Michetti N, Bury L, Weyrich AS, Gresele P. Megakaryocytes differentially sort mRNAs for matrix metalloproteinases and their inhibitors into platelets: a mechanism for regulating synthetic events. Blood. 2011;118(7):1903-1911.
    • (2011) Blood , vol.118 , Issue.7 , pp. 1903-1911
    • Cecchetti, L.1    Tolley, N.D.2    Michetti, N.3    Bury, L.4    Weyrich, A.S.5    Gresele, P.6
  • 9
    • 28444487916 scopus 로고    scopus 로고
    • Intraplatelet signaling mechanisms of the priming effect of matrix metalloproteinase-2 on platelet aggregation
    • Falcinelli E, Guglielmini G, Torti M, Gresele P. Intraplatelet signaling mechanisms of the priming effect of matrix metalloproteinase-2 on platelet aggregation. J Thromb Haemost. 2005;3(11):2526-2535.
    • (2005) J Thromb Haemost , vol.3 , Issue.11 , pp. 2526-2535
    • Falcinelli, E.1    Guglielmini, G.2    Torti, M.3    Gresele, P.4
  • 10
    • 70449711236 scopus 로고    scopus 로고
    • Loss of matrix metalloproteinase 2 in platelets reduces arterial thrombosis in vivo
    • Momi S, Falcinelli E, Giannini S, et al. Loss of matrix metalloproteinase 2 in platelets reduces arterial thrombosis in vivo. J Exp Med. 2009;206(11):2365-2379.
    • (2009) J Exp Med , vol.206 , Issue.11 , pp. 2365-2379
    • Momi, S.1    Falcinelli, E.2    Giannini, S.3
  • 11
    • 34250817676 scopus 로고    scopus 로고
    • Platelets release active matrix metalloproteinase-2 in vivo in humans at a site of vascular injury: Lack of inhibition by aspirin
    • Falcinelli E, Giannini S, Boschetti E, Gresele P. Platelets release active matrix metalloproteinase-2 in vivo in humans at a site of vascular injury: lack of inhibition by aspirin. Br J Haematol. 2007;138(2):221-230.
    • (2007) Br J Haematol , vol.138 , Issue.2 , pp. 221-230
    • Falcinelli, E.1    Giannini, S.2    Boschetti, E.3    Gresele, P.4
  • 12
    • 79751508250 scopus 로고    scopus 로고
    • Platelets release matrix metalloproteinase-2 in the coronary circulation of patients with acute coronary syndromes: Possible role in sustained platelet activation
    • Gresele P, Falcinelli E, Loffredo F, et al. Platelets release matrix metalloproteinase-2 in the coronary circulation of patients with acute coronary syndromes: possible role in sustained platelet activation. Eur Heart J. 2011;32(3):316-325.
    • (2011) Eur Heart J , vol.32 , Issue.3 , pp. 316-325
    • Gresele, P.1    Falcinelli, E.2    Loffredo, F.3
  • 13
    • 84901952299 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 of human carotid atherosclerotic plaques promotes platelet activation. Correlation with ischaemic events
    • Lenti M, Falcinelli E, Pompili M, et al. Matrix metalloproteinase-2 of human carotid atherosclerotic plaques promotes platelet activation. Correlation with ischaemic events. Thromb Haemost. 2014;111(6):1089-1101.
    • (2014) Thromb Haemost , vol.111 , Issue.6 , pp. 1089-1101
    • Lenti, M.1    Falcinelli, E.2    Pompili, M.3
  • 14
    • 84891887337 scopus 로고    scopus 로고
    • Intracellular matrix metalloproteinase-2 (MMP-2) regulates human platelet activation via hydrolysis of talin
    • Soslau G, Mason C, Lynch S, et al. Intracellular matrix metalloproteinase-2 (MMP-2) regulates human platelet activation via hydrolysis of talin. Thromb Haemost. 2014;111(1):140-153.
    • (2014) Thromb Haemost , vol.111 , Issue.1 , pp. 140-153
    • Soslau, G.1    Mason, C.2    Lynch, S.3
  • 15
    • 37549064277 scopus 로고    scopus 로고
    • Talin is required for integrin-mediated platelet function in hemostasis and thrombosis
    • Petrich BG, Marchese P, Ruggeri ZM, et al. Talin is required for integrin-mediated platelet function in hemostasis and thrombosis. J Exp Med. 2007;204(13):3103-3111.
    • (2007) J Exp Med , vol.204 , Issue.13 , pp. 3103-3111
    • Petrich, B.G.1    Marchese, P.2    Ruggeri, Z.M.3
  • 16
    • 39549089084 scopus 로고    scopus 로고
    • MMP-2 regulates human platelet activation by interacting with integrin alphaIIbbeta3
    • Choi WS, Jeon OH, Kim HH, Kim DS. MMP-2 regulates human platelet activation by interacting with integrin alphaIIbbeta3. J Thromb Haemost. 2008;6(3):517-523.
    • (2008) J Thromb Haemost , vol.6 , Issue.3 , pp. 517-523
    • Choi, W.S.1    Jeon, O.H.2    Kim, H.H.3    Kim, D.S.4
  • 17
    • 84888121509 scopus 로고    scopus 로고
    • Molecular determinants of PI3Kγ-mediated activation downstream of G-protein-coupled receptors (GPCRs)
    • Vadas O, Dbouk HA, Shymanets A, et al. Molecular determinants of PI3Kγ-mediated activation downstream of G-protein-coupled receptors (GPCRs). Proc Natl Acad Sci USA. 2013;110(47):18862-18867.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.47 , pp. 18862-18867
    • Vadas, O.1    Dbouk, H.A.2    Shymanets, A.3
  • 18
    • 0032748545 scopus 로고    scopus 로고
    • Protease-activated receptors and platelet function
    • Coughlin SR. Protease-activated receptors and platelet function. Thromb Haemost. 1999;82(2):353-356.
    • (1999) Thromb Haemost , vol.82 , Issue.2 , pp. 353-356
    • Coughlin, S.R.1
  • 19
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • Coughlin SR. Protease-activated receptors in hemostasis, thrombosis and vascular biology. J Thromb Haemost. 2005;3(8):1800-1814.
    • (2005) J Thromb Haemost , vol.3 , Issue.8 , pp. 1800-1814
    • Coughlin, S.R.1
  • 20
    • 84877615610 scopus 로고    scopus 로고
    • Senescent fibroblasts enhance early skin carcinogenic events via a paracrine MMP-PAR-1 axis
    • Malaquin N, Vercamer C, Bouali F, et al. Senescent fibroblasts enhance early skin carcinogenic events via a paracrine MMP-PAR-1 axis. PLoS One. 2013;8(5):e63607.
    • (2013) PLoS One , vol.8 , Issue.5
    • Malaquin, N.1    Vercamer, C.2    Bouali, F.3
  • 21
    • 77956194977 scopus 로고    scopus 로고
    • Alpha-synuclein activates microglia by inducing the expressions of matrix metalloproteinases and the subsequent activation of protease-activated receptor-1
    • Lee EJ, Woo MS, Moon PG, et al. Alpha-synuclein activates microglia by inducing the expressions of matrix metalloproteinases and the subsequent activation of protease-activated receptor-1. J Immunol. 2010;185(1):615-623.
    • (2010) J Immunol , vol.185 , Issue.1 , pp. 615-623
    • Lee, E.J.1    Woo, M.S.2    Moon, P.G.3
  • 22
    • 13544255506 scopus 로고    scopus 로고
    • PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells
    • Boire A, Covic L, Agarwal A, Jacques S, Sherifi S, Kuliopulos A. PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells. Cell. 2005;120(3):303-313.
    • (2005) Cell , vol.120 , Issue.3 , pp. 303-313
    • Boire, A.1    Covic, L.2    Agarwal, A.3    Jacques, S.4    Sherifi, S.5    Kuliopulos, A.6
  • 23
    • 64249129547 scopus 로고    scopus 로고
    • Platelet matrix metalloprotease-1 mediates thrombogenesis by activating PAR1 at a cryptic ligand site
    • Trivedi V, Boire A, Tchernychev B, et al. Platelet matrix metalloprotease-1 mediates thrombogenesis by activating PAR1 at a cryptic ligand site. Cell. 2009;137(2):332-343.
    • (2009) Cell , vol.137 , Issue.2 , pp. 332-343
    • Trivedi, V.1    Boire, A.2    Tchernychev, B.3
  • 24
    • 84862583259 scopus 로고    scopus 로고
    • β-adrenergic receptor stimulation transactivates protease-activated receptor 1 via matrix metalloproteinase 13 in cardiac cells
    • Jaffré F, Friedman AE, Hu Z, Mackman N, Blaxall BC. β-adrenergic receptor stimulation transactivates protease-activated receptor 1 via matrix metalloproteinase 13 in cardiac cells. Circulation. 2012;125(24):2993-3003.
    • (2012) Circulation , vol.125 , Issue.24 , pp. 2993-3003
    • Jaffré, F.1    Friedman, A.E.2    Hu, Z.3    Mackman, N.4    Blaxall, B.C.5
  • 25
    • 84872461768 scopus 로고    scopus 로고
    • Matrix metalloproteases and PAR1 activation
    • Austin KM, Covic L, Kuliopulos A. Matrix metalloproteases and PAR1 activation. Blood. 2013;121(3):431-439.
    • (2013) Blood , vol.121 , Issue.3 , pp. 431-439
    • Austin, K.M.1    Covic, L.2    Kuliopulos, A.3
  • 26
    • 84984981936 scopus 로고    scopus 로고
    • Biased signaling: Potential agonist and antagonist of PAR2
    • Kakarala KK, Jamil K. Biased signaling: potential agonist and antagonist of PAR2. J Biomol Struct Dyn. 2016;34(6):1363-1376.
    • (2016) J Biomol Struct Dyn , vol.34 , Issue.6 , pp. 1363-1376
    • Kakarala, K.K.1    Jamil, K.2
  • 27
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • Kleiner DE, Stetler-Stevenson WG. Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem. 1994;218(2):325-329.
    • (1994) Anal Biochem , vol.218 , Issue.2 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 28
    • 84877043171 scopus 로고    scopus 로고
    • Platelet and endothelial activation in catastrophic and quiescent antiphospholipid syndrome
    • Bontadi A, Ruffatti A, Falcinelli E, et al. Platelet and endothelial activation in catastrophic and quiescent antiphospholipid syndrome. Thromb Haemost. 2013;109(5):901-908.
    • (2013) Thromb Haemost , vol.109 , Issue.5 , pp. 901-908
    • Bontadi, A.1    Ruffatti, A.2    Falcinelli, E.3
  • 29
    • 0027126642 scopus 로고
    • Activation of phospholipase A2 and beta-thromboglobulin release in human platelets: Comparative effects of thrombin and fluoroaluminate stimulation
    • Stasi M, Gresele P, Porcellati S, Quero E, Nenci GG, Goracci G. Activation of phospholipase A2 and beta-thromboglobulin release in human platelets: comparative effects of thrombin and fluoroaluminate stimulation. Biochim Biophys Acta. 1992;1124(3):279-287.
    • (1992) Biochim Biophys Acta , vol.1124 , Issue.3 , pp. 279-287
    • Stasi, M.1    Gresele, P.2    Porcellati, S.3    Quero, E.4    Nenci, G.G.5    Goracci, G.6
  • 31
    • 84952938421 scopus 로고    scopus 로고
    • Cytoskeletal perturbation leads to platelet dysfunction and thrombocytopenia in variant forms of Glanzmann thrombasthenia
    • Bury L, Falcinelli E, Chiasserini D, Springer TA, Italiano JE Jr, Gresele P. Cytoskeletal perturbation leads to platelet dysfunction and thrombocytopenia in variant forms of Glanzmann thrombasthenia. Haematologica. 2016;101(1):46-56.
    • (2016) Haematologica , vol.101 , Issue.1 , pp. 46-56
    • Bury, L.1    Falcinelli, E.2    Chiasserini, D.3    Springer, T.A.4    Italiano, J.E.5    Gresele, P.6
  • 33
    • 0033119035 scopus 로고    scopus 로고
    • Flow cytometric kinetic assay of calcium mobilization in whole blood platelets using Fluo-3 and CD41
    • do Céu Monteiro M, Sansonetty F, Gonçalves MJ, O'Connor JE. Flow cytometric kinetic assay of calcium mobilization in whole blood platelets using Fluo-3 and CD41. Cytometry. 1999;35(4):302-310.
    • (1999) Cytometry , vol.35 , Issue.4 , pp. 302-310
    • Do Céu Monteiro, M.1    Sansonetty, F.2    Gonçalves, M.J.3    O'Connor, J.E.4
  • 34
    • 67650865950 scopus 로고    scopus 로고
    • Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies
    • Edelheit O, Hanukoglu A, Hanukoglu I. Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies. BMC Biotechnol. 2009;9:61.
    • (2009) BMC Biotechnol , vol.9 , pp. 61
    • Edelheit, O.1    Hanukoglu, A.2    Hanukoglu, I.3
  • 35
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 1991;64(6):1057-1068.
    • (1991) Cell , vol.64 , Issue.6 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 36
    • 0026690665 scopus 로고
    • Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation
    • Hung DT, Vu TK, Wheaton VI, Ishii K, Coughlin SR. Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation. J Clin Invest. 1992;89(4):1350-1353.
    • (1992) J Clin Invest , vol.89 , Issue.4 , pp. 1350-1353
    • Hung, D.T.1    Vu, T.K.2    Wheaton, V.I.3    Ishii, K.4    Coughlin, S.R.5
  • 37
    • 0033559805 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin
    • Kahn ML, Nakanishi-Matsui M, Shapiro MJ, Ishihara H, Coughlin SR. Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J Clin Invest. 1999;103(6):879-887.
    • (1999) J Clin Invest , vol.103 , Issue.6 , pp. 879-887
    • Kahn, M.L.1    Nakanishi-Matsui, M.2    Shapiro, M.J.3    Ishihara, H.4    Coughlin, S.R.5
  • 38
    • 0033528761 scopus 로고    scopus 로고
    • Plasmin desensitization of the PAR1 thrombin receptor: Kinetics, sites of truncation, and implications for thrombolytic therapy
    • Kuliopulos A, Covic L, Seeley SK, Sheridan PJ, Helin J, Costello CE. Plasmin desensitization of the PAR1 thrombin receptor: kinetics, sites of truncation, and implications for thrombolytic therapy. Biochemistry. 1999;38(14):4572-4585.
    • (1999) Biochemistry , vol.38 , Issue.14 , pp. 4572-4585
    • Kuliopulos, A.1    Covic, L.2    Seeley, S.K.3    Sheridan, P.J.4    Helin, J.5    Costello, C.E.6
  • 39
    • 0344668870 scopus 로고    scopus 로고
    • Structural basis for thrombin activation of a protease-activated receptor: Inhibition of intramolecular liganding
    • Seeley S, Covic L, Jacques SL, Sudmeier J, Baleja JD, Kuliopulos A. Structural basis for thrombin activation of a protease-activated receptor: inhibition of intramolecular liganding. Chem Biol. 2003;10(11):1033-1041.
    • (2003) Chem Biol , vol.10 , Issue.11 , pp. 1033-1041
    • Seeley, S.1    Covic, L.2    Jacques, S.L.3    Sudmeier, J.4    Baleja, J.D.5    Kuliopulos, A.6
  • 40
    • 84871411930 scopus 로고    scopus 로고
    • High-resolution crystal structure of human protease-activated receptor 1
    • Zhang C, Srinivasan Y, Arlow DH, et al. High-resolution crystal structure of human protease-activated receptor 1. Nature. 2012;492(7429):387-392.
    • (2012) Nature , vol.492 , Issue.7429 , pp. 387-392
    • Zhang, C.1    Srinivasan, Y.2    Arlow, D.H.3
  • 41
    • 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, et al. Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling. J Biol Chem. 1994;269(4):2943-2952.
    • (1994) J Biol Chem , vol.269 , Issue.4 , pp. 2943-2952
    • Brass, L.F.1    Pizarro, S.2    Ahuja, M.3
  • 42
    • 33947654354 scopus 로고    scopus 로고
    • Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins
    • Piccard H, Van den Steen PE, Opdenakker G. Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J Leukoc Biol. 2007;81(4):870-892.
    • (2007) J Leukoc Biol , vol.81 , Issue.4 , pp. 870-892
    • Piccard, H.1    Van Den Steen, P.E.2    Opdenakker, G.3
  • 43
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin SR. Thrombin signalling and protease-activated receptors. Nature. 2000;407(6801):258-264.
    • (2000) Nature , vol.407 , Issue.6801 , pp. 258-264
    • Coughlin, S.R.1
  • 44
    • 0034828616 scopus 로고    scopus 로고
    • Activation of the alpha(2A)-adrenoceptor mediates deceleration of the deaggregation component of the response to ADP or 5-HT in human platelets in vitro
    • Maayani S, Schwarz T, Craddock-Royal B, Tagliente TM. Activation of the alpha(2A)-adrenoceptor mediates deceleration of the deaggregation component of the response to ADP or 5-HT in human platelets in vitro. Platelets. 2001;12(6):359-375.
    • (2001) Platelets , vol.12 , Issue.6 , pp. 359-375
    • Maayani, S.1    Schwarz, T.2    Craddock-Royal, B.3    Tagliente, T.M.4
  • 46
    • 84873557748 scopus 로고    scopus 로고
    • Calcium mobilization and protein kinase C activation downstream of protease activated receptor 4 (PAR4) is negatively regulated by PAR3 in mouse platelets
    • published correction appears in PLoS One. 2013;8(12)
    • Arachiche A, de la Fuente M, Nieman MT. Calcium mobilization and protein kinase C activation downstream of protease activated receptor 4 (PAR4) is negatively regulated by PAR3 in mouse platelets [published correction appears in PLoS One. 2013;8(12)]. PLoS One. 2013;8(2):e55740.
    • (2013) PLoS One , vol.8 , Issue.2
    • Arachiche, A.1    De La Fuente, M.2    Nieman, M.T.3
  • 47
    • 84957575238 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 enhances platelet deposition on collagen under flow conditions
    • Guglielmini G, Appolloni V, Momi S, et al. Matrix metalloproteinase-2 enhances platelet deposition on collagen under flow conditions. Thromb Haemost. 2016;115(2):333-343.
    • (2016) Thromb Haemost , vol.115 , Issue.2 , pp. 333-343
    • Guglielmini, G.1    Appolloni, V.2    Momi, S.3
  • 48
    • 84948095487 scopus 로고    scopus 로고
    • Platelet-associated matrix metalloproteinases regulate thrombus formation and exert local collagenolytic activity
    • Mastenbroek TG, Feijge MA, Kremers RM, et al. Platelet-associated matrix metalloproteinases regulate thrombus formation and exert local collagenolytic activity. Arterioscler Thromb Vasc Biol. 2015;35(12):2554-2561.
    • (2015) Arterioscler Thromb Vasc Biol , vol.35 , Issue.12 , pp. 2554-2561
    • Mastenbroek, T.G.1    Feijge, M.A.2    Kremers, R.M.3
  • 50
    • 0037092952 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 do not stimulate G(i) signaling pathways in the absence of secreted ADP and cause human platelet aggregation independently of G(i) signaling
    • Kim S, Foster C, Lecchi A, et al. Protease-activated receptors 1 and 4 do not stimulate G(i) signaling pathways in the absence of secreted ADP and cause human platelet aggregation independently of G(i) signaling. Blood. 2002;99(10):3629-3636.
    • (2002) Blood , vol.99 , Issue.10 , pp. 3629-3636
    • Kim, S.1    Foster, C.2    Lecchi, A.3
  • 51
    • 0034235316 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 and macrophage-derived chemokine: 2 Chemokines that activate platelets
    • Kowalska MA, Ratajczak MZ, Majka M, et al. Stromal cell-derived factor-1 and macrophage-derived chemokine: 2 chemokines that activate platelets. Blood. 2000;96(1):50-57.
    • (2000) Blood , vol.96 , Issue.1 , pp. 50-57
    • Kowalska, M.A.1    Ratajczak, M.Z.2    Majka, M.3
  • 52
    • 0035098077 scopus 로고    scopus 로고
    • Activation of the murine EP3 receptor for PGE2 inhibits cAMP production and promotes platelet aggregation
    • Fabre JE, Nguyen M, Athirakul K, et al. Activation of the murine EP3 receptor for PGE2 inhibits cAMP production and promotes platelet aggregation. J Clin Invest. 2001;107(5):603-610.
    • (2001) J Clin Invest , vol.107 , Issue.5 , pp. 603-610
    • Fabre, J.E.1    Nguyen, M.2    Athirakul, K.3
  • 53
    • 45849092207 scopus 로고    scopus 로고
    • Potentiation and priming of platelet activation: A potential target for antiplatelet therapy
    • Gresele P, Falcinelli E, Momi S. Potentiation and priming of platelet activation: a potential target for antiplatelet therapy. Trends Pharmacol Sci. 2008;29(7):352-360.
    • (2008) Trends Pharmacol Sci , vol.29 , Issue.7 , pp. 352-360
    • Gresele, P.1    Falcinelli, E.2    Momi, S.3
  • 54
    • 84887852110 scopus 로고    scopus 로고
    • Neutrophil elastase and proteinase-3 trigger G protein-biased signaling through proteinase-activated receptor-1 (PAR1)
    • Mihara K, Ramachandran R, Renaux B, Saifeddine M, Hollenberg MD. Neutrophil elastase and proteinase-3 trigger G protein-biased signaling through proteinase-activated receptor-1 (PAR1). J Biol Chem. 2013;288(46):32979-32990.
    • (2013) J Biol Chem , vol.288 , Issue.46 , pp. 32979-32990
    • Mihara, K.1    Ramachandran, R.2    Renaux, B.3    Saifeddine, M.4    Hollenberg, M.D.5
  • 55
    • 84907916606 scopus 로고    scopus 로고
    • Cathepsin S causes inflammatory pain via biased agonism of PAR2 and TRPV4
    • Zhao P, Lieu T, Barlow N, et al. Cathepsin S causes inflammatory pain via biased agonism of PAR2 and TRPV4. J Biol Chem. 2014;289(39):27215-27234.
    • (2014) J Biol Chem , vol.289 , Issue.39 , pp. 27215-27234
    • Zhao, P.1    Lieu, T.2    Barlow, N.3
  • 56
    • 0027205029 scopus 로고
    • A peptide ligand of the human thrombin receptor antagonizes alpha-thrombin and partially activates platelets
    • Rasmussen UB, Gachet C, Schlesinger Y, et al. A peptide ligand of the human thrombin receptor antagonizes alpha-thrombin and partially activates platelets. J Biol Chem. 1993;268(19):14322-14328.
    • (1993) J Biol Chem , vol.268 , Issue.19 , pp. 14322-14328
    • Rasmussen, U.B.1    Gachet, C.2    Schlesinger, Y.3
  • 57
    • 84895156496 scopus 로고    scopus 로고
    • Biased signalling and proteinase-activated receptors (PARs): Targeting inflammatory disease
    • Hollenberg MD, Mihara K, Polley D, et al. Biased signalling and proteinase-activated receptors (PARs): targeting inflammatory disease. Br J Pharmacol. 2014;171(5):1180-1194.
    • (2014) Br J Pharmacol , vol.171 , Issue.5 , pp. 1180-1194
    • Hollenberg, M.D.1    Mihara, K.2    Polley, D.3
  • 58
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    • Brooks PC, Strömblad S, Sanders LC, et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell. 1996;85(5):683-693.
    • (1996) Cell , vol.85 , Issue.5 , pp. 683-693
    • Brooks, P.C.1    Strömblad, S.2    Sanders, L.C.3
  • 59
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem. 1995;270(10):5331-5338.
    • (1995) J Biol Chem , vol.270 , Issue.10 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 60
    • 77955496933 scopus 로고    scopus 로고
    • MMP-2 alters VEGF expression via alphaVbeta3 integrin-mediated PI3K/AKT signaling in A549 lung cancer cells
    • Chetty C, Lakka SS, Bhoopathi P, Rao JS. MMP-2 alters VEGF expression via alphaVbeta3 integrin-mediated PI3K/AKT signaling in A549 lung cancer cells. Int J Cancer. 2010;127(5):1081-1095.
    • (2010) Int J Cancer , vol.127 , Issue.5 , pp. 1081-1095
    • Chetty, C.1    Lakka, S.S.2    Bhoopathi, P.3    Rao, J.S.4
  • 61
    • 33747610734 scopus 로고    scopus 로고
    • Crystal structure of an active form of human MMP-1
    • Iyer S, Visse R, Nagase H, Acharya KR. Crystal structure of an active form of human MMP-1. J Mol Biol. 2006;362(1):78-88.
    • (2006) J Mol Biol , vol.362 , Issue.1 , pp. 78-88
    • Iyer, S.1    Visse, R.2    Nagase, H.3    Acharya, K.R.4
  • 62
    • 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, De Cristofaro R. Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets. J Biol Chem. 2001;276(7):4692-4698.
    • (2001) J Biol Chem , vol.276 , Issue.7 , 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


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