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Volumn 105, Issue 6, 2011, Pages 1032-1045

A novel family of RGD-containing disintegrins (Tablysin-15) from the salivary gland of the horsefly Tabanus yao targets αIIbβ3 or αVβ3 and inhibits platelet aggregation and angiogenesis

Author keywords

Blood sucking; Disintegrin; Haematophagy; Sialogenins; Thrombosis

Indexed keywords

ABCIXIMAB; ADENOSINE DIPHOSPHATE; ALPHA2B BETA3 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; COLLAGEN; CONVULXIN; DISINTEGRIN; EDETIC ACID; FIBRINOGEN; FIBROBLAST GROWTH FACTOR; FIBRONECTIN; INTEGRIN; TABLYSIN 15; UNCLASSIFIED DRUG; UROKINASE; VITRONECTIN; VITRONECTIN RECEPTOR;

EID: 79958217683     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH11-01-0029     Document Type: Article
Times cited : (60)

References (50)
  • 2
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood JD, Cheresh DA. Role of integrins in cell invasion and migration. Nat Rev Cancer 2002; 2: 91-100.
    • (2002) Nat Rev Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 3
    • 69349090351 scopus 로고    scopus 로고
    • Imaging of alpha(v)beta(3) expression by a bifunctional chimeric RGD peptide not cross-reacting with alpha(v)beta(5)
    • Zannetti A, Del Vecchio S, Iommelli F, et al. Imaging of alpha(v)beta(3) expression by a bifunctional chimeric RGD peptide not cross-reacting with alpha(v)beta(5). Clin Cancer Res 2009; 15: 5224-5233.
    • (2009) Clin Cancer Res , vol.15 , pp. 5224-5233
    • Zannetti, A.1    del Vecchio, S.2    Iommelli, F.3
  • 4
    • 0031814234 scopus 로고    scopus 로고
    • What have snakes taught us about integrins?
    • Huang TF. What have snakes taught us about integrins? Cell Mol Life Sci 1998; 54: 527-540.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 527-540
    • Huang, T.F.1
  • 5
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland FS. Snake venoms and the hemostatic system. Toxicon 1998; 36: 1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 6
    • 14744294145 scopus 로고    scopus 로고
    • Structure-function correlations of snake venom disintegrins
    • Calvete JJ. Structure-function correlations of snake venom disintegrins. Curr Pharm Des 2005; 11: 829-835.
    • (2005) Curr Pharm Des , vol.11 , pp. 829-835
    • Calvete, J.J.1
  • 7
    • 5644292205 scopus 로고    scopus 로고
    • Differential recognition of snake venom proteins expressing specific Arg-Gly-Asp (RGD) sequence motifs by wild-type and variant integrin alphaIIbbeta3: Further evidence for distinct sites of RGD ligand recognition exhibiting negative allostery
    • Rahman S, Flynn G, Aitken A, et al. Differential recognition of snake venom proteins expressing specific Arg-Gly-Asp (RGD) sequence motifs by wild-type and variant integrin alphaIIbbeta3: further evidence for distinct sites of RGD ligand recognition exhibiting negative allostery. Biochem J 2000; 345: 701-709.
    • (2000) Biochem J , vol.345 , pp. 701-709
    • Rahman, S.1    Flynn, G.2    Aitken, A.3
  • 8
    • 33846052755 scopus 로고    scopus 로고
    • Structure-activity relationship studies on ADAM protein-integrin interactions
    • Lu X, Lu D, Scully MF, et al. Structure-activity relationship studies on ADAM protein-integrin interactions. Cardiovasc Hematol Agents Med Chem 2007; 5: 29-42.
    • (2007) Cardiovasc Hematol Agents Med Chem , vol.5 , pp. 29-42
    • Lu, X.1    Lu, D.2    Scully, M.F.3
  • 9
    • 33645789298 scopus 로고    scopus 로고
    • Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: Insight into the evolution of the snake venom integrin-inhibition system
    • Sanz L, Bazaa A, Marrakchi N, et al. Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: insight into the evolution of the snake venom integrin-inhibition system. Biochem J 2006; 395: 385-392.
    • (2006) Biochem J , vol.395 , pp. 385-392
    • Sanz, L.1    Bazaa, A.2    Marrakchi, N.3
  • 10
    • 44349151718 scopus 로고    scopus 로고
    • Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
    • Fox JW, Serrano SM. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J 2008; 275: 3016-3030.
    • (2008) FEBS J , vol.275 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.2
  • 11
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • Kini RM, Evans HJ. Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon 1992; 30: 265-293.
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 12
    • 26444535506 scopus 로고    scopus 로고
    • GPVI and integrin alphaIIb beta3 signaling in platelets
    • Watson SP, Auger JM, McCarty OJ, et al. GPVI and integrin alphaIIb beta3 signaling in platelets. J Thromb Haemost 2005; 3: 1752-1762.
    • (2005) J Thromb Haemost , vol.3 , pp. 1752-1762
    • Watson, S.P.1    Auger, J.M.2    McCarty, O.J.3
  • 13
  • 15
    • 0242300217 scopus 로고    scopus 로고
    • Antiplatelet therapy: In search of the 'magic bullet'
    • Jackson SP, Schoenwaelder SM. Antiplatelet therapy: in search of the 'magic bullet'. Nat Rev Drug Discov 2003; 2: 775-789.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 775-789
    • Jackson, S.P.1    Schoenwaelder, S.M.2
  • 17
    • 38449122195 scopus 로고    scopus 로고
    • Anti-angiogenesis and RGD-containing snake venom disintegrins
    • Swenson S, Ramu S, Markland FS. Anti-angiogenesis and RGD-containing snake venom disintegrins. Curr Pharm Des 2007; 13: 2860-2871.
    • (2007) Curr Pharm Des , vol.13 , pp. 2860-2871
    • Swenson, S.1    Ramu, S.2    Markland, F.S.3
  • 18
    • 77957900996 scopus 로고    scopus 로고
    • Platelet aggregation inhibitors from hematophagous animals
    • Francischetti IM. Platelet aggregation inhibitors from hematophagous animals. Toxicon 2010; 56: 1130-1144.
    • (2010) Toxicon , vol.56 , pp. 1130-1144
    • Francischetti, I.M.1
  • 19
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro JM, Francischetti IM. Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives. Annu Rev Entomol 2003; 48: 73-88.
    • (2003) Annu Rev Entomol , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 21
    • 0037077268 scopus 로고    scopus 로고
    • Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold
    • Mans BJ, Louw AI, Neitz AW. Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold. J Biol Chem 2002; 277: 21371-21378.
    • (2002) J Biol Chem , vol.277 , pp. 21371-21378
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 22
    • 0029898540 scopus 로고    scopus 로고
    • Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis
    • Wang X, Coons LB, Taylor DB, et al. Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis. J Biol Chem 1996; 271: 17785-17790.
    • (1996) J Biol Chem , vol.271 , pp. 17785-17790
    • Wang, X.1    Coons, L.B.2    Taylor, D.B.3
  • 23
    • 0026331936 scopus 로고
    • Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata
    • Mazur P, Henzel WJ, Seymour JL, et al. Ornatins: potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur J Biochem 1991; 202: 1073-1082.
    • (1991) Eur J Biochem , vol.202 , pp. 1073-1082
    • Mazur, P.1    Henzel, W.J.2    Seymour, J.L.3
  • 24
    • 0028817868 scopus 로고
    • A comparison of the effect of decorsin and two disintegrins, albolabrin and eristostatin, on platelet function
    • McLane MA, Gabbeta J, Rao AK, et al. A comparison of the effect of decorsin and two disintegrins, albolabrin and eristostatin, on platelet function. Thromb Haemost 1995; 74: 1316-1322.
    • (1995) Thromb Haemost , vol.74 , pp. 1316-1322
    • McLane, M.A.1    Gabbeta, J.2    Rao, A.K.3
  • 25
    • 41549145257 scopus 로고    scopus 로고
    • Toward an understanding of the molecular mechanism for successful blood feeding by coupling proteomics analysis with pharmacological testing of horsefly salivary glands
    • Xu X, Yang H, Ma D, et al. Toward an understanding of the molecular mechanism for successful blood feeding by coupling proteomics analysis with pharmacological testing of horsefly salivary glands. Mol Cell Proteomics 2008; 7: 582-590.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 582-590
    • Xu, X.1    Yang, H.2    Ma, D.3
  • 26
    • 71049174810 scopus 로고    scopus 로고
    • Anti-thrombosis repertoire of blood-feeding horsefly salivary glands
    • Ma D, Wang Y, Yang H, et al. Anti-thrombosis repertoire of blood-feeding horsefly salivary glands. Mol Cell Proteomics 2009; 8: 2071-2079.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2071-2079
    • Ma, D.1    Wang, Y.2    Yang, H.3
  • 27
    • 0030801096 scopus 로고    scopus 로고
    • Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets
    • Francischetti IM, Saliou B, Leduc M, et al. Convulxin, a potent platelet-aggregating protein from Crotalus durissus terrificus venom, specifically binds to platelets. Toxicon 1997; 35: 1217-1228.
    • (1997) Toxicon , vol.35 , pp. 1217-1228
    • Francischetti, I.M.1    Saliou, B.2    Leduc, M.3
  • 28
    • 34848895497 scopus 로고    scopus 로고
    • Aegyptin, a novel mosquito salivary gland protein, specifically binds to collagen and prevents its interaction with platelet glycoprotein VI, integrin alpha2beta1, and von Willebrand factor
    • Calvo E, Tokumasu F, Marinotti O, et al. Aegyptin, a novel mosquito salivary gland protein, specifically binds to collagen and prevents its interaction with platelet glycoprotein VI, integrin alpha2beta1, and von Willebrand factor. J Biol Chem 2007; 282: 26928-26938.
    • (2007) J Biol Chem , vol.282 , pp. 26928-26938
    • Calvo, E.1    Tokumasu, F.2    Marinotti, O.3
  • 29
    • 0032901931 scopus 로고    scopus 로고
    • Quantifying GPIIb/IIIa receptor binding using 2 monoclonal antibodies: Discriminating abciximab and small molecular weight antagonists
    • Quinn M, Deering A, Stewart M, et al. Quantifying GPIIb/IIIa receptor binding using 2 monoclonal antibodies: discriminating abciximab and small molecular weight antagonists. Circulation 1999; 99: 2231-2238.
    • (1999) Circulation , vol.99 , pp. 2231-2238
    • Quinn, M.1    Deering, A.2    Stewart, M.3
  • 30
    • 18744389435 scopus 로고    scopus 로고
    • Occupancy of glycoprotein IIb/IIIa by B-6 vitamers inhibits human platelet aggregation
    • Chang SJ, Chang CN, Chen CW. Occupancy of glycoprotein IIb/IIIa by B-6 vitamers inhibits human platelet aggregation. J Nutr 2002; 132: 3603-3606.
    • (2002) J Nutr , vol.132 , pp. 3603-3606
    • Chang, S.J.1    Chang, C.N.2    Chen, C.W.3
  • 31
    • 22144494698 scopus 로고    scopus 로고
    • Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis
    • Francischetti IM, Mather TN, Ribeiro JM. Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis. Thromb Haemost 2005; 94: 167-174.
    • (2005) Thromb Haemost , vol.94 , pp. 167-174
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 32
    • 78649858721 scopus 로고    scopus 로고
    • Dipetalodipin, a novel multifunctional salivary lipocalin that inhibits platelet aggregation, vasoconstriction, and angiogenesis through unique binding specificity for TXA2, PGF2alpha, and 15(S)-HETE
    • Assumpcao TC, Alvarenga PH, Ribeiro JM, et al. Dipetalodipin, a novel multifunctional salivary lipocalin that inhibits platelet aggregation, vasoconstriction, and angiogenesis through unique binding specificity for TXA2, PGF2alpha, and 15(S)-HETE. J Biol Chem 2010; 285: 39001-39012.
    • (2010) J Biol Chem , vol.285 , pp. 39001-39012
    • Assumpcao, T.C.1    Alvarenga, P.H.2    Ribeiro, J.M.3
  • 33
    • 34548827704 scopus 로고    scopus 로고
    • Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation
    • Sperzel M, Huetter J. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost 2007; 5: 2113-2118.
    • (2007) J Thromb Haemost , vol.5 , pp. 2113-2118
    • Sperzel, M.1    Huetter, J.2
  • 34
    • 0019982226 scopus 로고
    • Bleeding time in rats: A comparison of different experimental conditions
    • Dejana E, Villa S, de Gaetano G. Bleeding time in rats: a comparison of different experimental conditions. Thromb Haemost 1982; 48: 108-111.
    • (1982) Thromb Haemost , vol.48 , pp. 108-111
    • Dejana, E.1    Villa, S.2    de Gaetano, G.3
  • 35
    • 0030049002 scopus 로고    scopus 로고
    • Defects in hemostasis in P-selectin-deficient mice
    • Subramaniam M, Frenette PS, Saffaripour S, et al. Defects in hemostasis in P-selectin-deficient mice. Blood 1996; 87: 1238-1242.
    • (1996) Blood , vol.87 , pp. 1238-1242
    • Subramaniam, M.1    Frenette, P.S.2    Saffaripour, S.3
  • 36
    • 0025329916 scopus 로고
    • Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
    • Seymour JL, Henzel WJ, Nevins B, et al. Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J Biol Chem 1990; 265: 10143-10147.
    • (1990) J Biol Chem , vol.265 , pp. 10143-10147
    • Seymour, J.L.1    Henzel, W.J.2    Nevins, B.3
  • 37
    • 0025096297 scopus 로고
    • Disintegrins: A family of integrin inhibitory proteins from viper venoms
    • Gould RJ, Polokoff MA, Friedman PA, et al. Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc Soc Exp Biol Med 1990; 195: 168-171.
    • (1990) Proc Soc Exp Biol Med , vol.195 , pp. 168-171
    • Gould, R.J.1    Polokoff, M.A.2    Friedman, P.A.3
  • 38
    • 0026471735 scopus 로고
    • Structure, function and evolutionary relationship of proteins containing a disintegrin domain
    • Blobel CP, White JM. Structure, function and evolutionary relationship of proteins containing a disintegrin domain. Curr Opin Cell Biol 1992; 4: 760-765.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 760-765
    • Blobel, C.P.1    White, J.M.2
  • 39
    • 0027508996 scopus 로고
    • Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms
    • Scarborough RM, Rose JW, Naughton MA, et al. Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms. J Biol Chem 1993; 268: 1058-1065.
    • (1993) J Biol Chem , vol.268 , pp. 1058-1065
    • Scarborough, R.M.1    Rose, J.W.2    Naughton, M.A.3
  • 40
    • 79955421119 scopus 로고    scopus 로고
    • Insight into the Salivary Transcriptome and Proteome of Dipetalogaster maxima
    • Assumpcao TC, Charneau S, Santiago PB, et al. Insight into the Salivary Transcriptome and Proteome of Dipetalogaster maxima. J Proteome Res 2011; 10: 1669-1679.
    • (2011) J Proteome Res , vol.10 , pp. 1669-1679
    • Assumpcao, T.C.1    Charneau, S.2    Santiago, P.B.3
  • 41
    • 0028057308 scopus 로고
    • Convulxin-induced platelet aggregation is accompanied by a powerful activation of the phospholipase C pathway
    • Faili A, Randon J, Francischetti IM, et al. Convulxin-induced platelet aggregation is accompanied by a powerful activation of the phospholipase C pathway. Biochem J 1994; 298: 87-91.
    • (1994) Biochem J , vol.298 , pp. 87-91
    • Faili, A.1    Randon, J.2    Francischetti, I.M.3
  • 43
    • 54249128761 scopus 로고    scopus 로고
    • Regulation of angiogenesis: Apoptotic cues from the ECM
    • Cheresh DA, Stupack DG. Regulation of angiogenesis: apoptotic cues from the ECM. Oncogene 2008; 27: 6285-6298.
    • (2008) Oncogene , vol.27 , pp. 6285-6298
    • Cheresh, D.A.1    Stupack, D.G.2
  • 44
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: The end game
    • Shattil SJ, Kim C, Ginsberg MH. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 2010; 11: 288-300.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.H.3
  • 45
    • 67049134054 scopus 로고    scopus 로고
    • Angiostasis as a way to improve immunotherapy
    • Griffioen AW, Vyth-Dreese FA. Angiostasis as a way to improve immunotherapy. Thromb Haemost 2009; 101: 1025-1031.
    • (2009) Thromb Haemost , vol.101 , pp. 1025-1031
    • Griffioen, A.W.1    Vyth-Dreese, F.A.2
  • 46
    • 14744285652 scopus 로고    scopus 로고
    • Functional characteristic of snake venom disintegrins: Potential therapeutic implication
    • Marcinkiewicz C. Functional characteristic of snake venom disintegrins: potential therapeutic implication. Curr Pharm Des 2005; 11: 815-827.
    • (2005) Curr Pharm Des , vol.11 , pp. 815-827
    • Marcinkiewicz, C.1
  • 47
    • 72949093138 scopus 로고    scopus 로고
    • Platelet response heterogeneity in thrombus formation
    • Munnix IC, Cosemans JM, Auger JM, et al. Platelet response heterogeneity in thrombus formation. Thromb Haemost 2009; 102: 1149-1156.
    • (2009) Thromb Haemost , vol.102 , pp. 1149-1156
    • Munnix, I.C.1    Cosemans, J.M.2    Auger, J.M.3
  • 48
    • 65649124530 scopus 로고    scopus 로고
    • Platelet activation by extracellular matrix proteins in haemostasis and thrombosis
    • Watson SP. Platelet activation by extracellular matrix proteins in haemostasis and thrombosis. Curr Pharm Des 2009; 15: 1358-1372.
    • (2009) Curr Pharm Des , vol.15 , pp. 1358-1372
    • Watson, S.P.1
  • 49
    • 70350459370 scopus 로고    scopus 로고
    • Mechanisms of platelet activation: Need for new strategies to protect against platelet-mediated atherothrombosis
    • Jennings LK. Mechanisms of platelet activation: need for new strategies to protect against platelet-mediated atherothrombosis. Thromb Haemost 2009; 102: 248-257.
    • (2009) Thromb Haemost , vol.102 , pp. 248-257
    • Jennings, L.K.1


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