메뉴 건너뛰기




Volumn 7, Issue 3, 2011, Pages

Longistatin, a plasminogen activator, is key to the availability of blood-meals for ixodid ticks

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; FIBRINOGEN; LONGISTATIN; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; ANTICOAGULANT AGENT; CALCIUM BINDING PROTEIN; DOUBLE STRANDED RNA; LONGISTATIN PROTEIN, HAEMAPHYSALIS LONGICORNIS; MESSENGER RNA; PROTOZOAL PROTEIN; SALIVA PROTEIN;

EID: 79953277007     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1001312     Document Type: Article
Times cited : (40)

References (51)
  • 1
    • 0030297416 scopus 로고    scopus 로고
    • Anticoagulant in vector arthropods
    • Stark KR, James AA, (1996) Anticoagulant in vector arthropods. Parasitol Today 12: 430-437.
    • (1996) Parasitol Today , vol.12 , pp. 430-437
    • Stark, K.R.1    James, A.A.2
  • 2
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie EW, Ratnoff OD, (1964) Waterfall sequence for intrinsic blood clotting. Science 145: 1310-1312.
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 4
    • 0030870212 scopus 로고    scopus 로고
    • Networking in the hemostatic system, integrin αIIbβ3 binds prothrobin and influences its activation
    • Byzova TV, Plow EF, (1997) Networking in the hemostatic system, integrin αIIbβ3 binds prothrobin and influences its activation. J Biol Chem 272: 27183-27188.
    • (1997) J Biol Chem , vol.272 , pp. 27183-27188
    • Byzova, T.V.1    Plow, E.F.2
  • 5
    • 51649110213 scopus 로고    scopus 로고
    • Analysis of the spatial and temporal characteristics of platelet-delivered factor VIII-based clots
    • Neyman M, Gewirtz J, Poncz M, (2008) Analysis of the spatial and temporal characteristics of platelet-delivered factor VIII-based clots. Blood 112: 1101-1108.
    • (2008) Blood , vol.112 , pp. 1101-1108
    • Neyman, M.1    Gewirtz, J.2    Poncz, M.3
  • 6
    • 18444386848 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrinolysis
    • Cesarman-Maus G, Hajjar KA, (2005) Molecular mechanisms of fibrinolysis. Br J Haematol 129: 307-321.
    • (2005) Br J Haematol , vol.129 , pp. 307-321
    • Cesarman-Maus, G.1    Hajjar, K.A.2
  • 7
    • 5144220471 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator: a historical perspective and personal account
    • Collen D, Lijnen HR, (2004) Tissue-type plasminogen activator: a historical perspective and personal account. J Thromb Haemost 2: 541-546.
    • (2004) J Thromb Haemost , vol.2 , pp. 541-546
    • Collen, D.1    Lijnen, H.R.2
  • 8
    • 0026644988 scopus 로고
    • Thrombolytic and pharmacokinetic properties of an immunoconjugate of single-chain urokinase-type plasminogen activator (u-PA) and a bispecific monoclonal antibody against fibrin and against u-PA in baboons
    • Imura Y, Stassen JM, Kurokawa T, Iwasa S, Lijnen HR, et al. (1992) Thrombolytic and pharmacokinetic properties of an immunoconjugate of single-chain urokinase-type plasminogen activator (u-PA) and a bispecific monoclonal antibody against fibrin and against u-PA in baboons. Blood 79: 2322-2329.
    • (1992) Blood , vol.79 , pp. 2322-2329
    • Imura, Y.1    Stassen, J.M.2    Kurokawa, T.3    Iwasa, S.4    Lijnen, H.R.5
  • 9
    • 0021206814 scopus 로고
    • Isolation and characterization of a urokinase-type plasminogen activator (Mr = 54,000) from cultured human endothelial cells indistinguishable from urinary urokinase
    • Booyse FM, Osikowicz G, Feder S, Scheinbuks J, (1984) Isolation and characterization of a urokinase-type plasminogen activator (Mr = 54,000) from cultured human endothelial cells indistinguishable from urinary urokinase. J Biol Chem 259: 7198-7205.
    • (1984) J Biol Chem , vol.259 , pp. 7198-7205
    • Booyse, F.M.1    Osikowicz, G.2    Feder, S.3    Scheinbuks, J.4
  • 10
    • 0024459573 scopus 로고
    • Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator
    • Gardell SJ, Duong LT, Diehl RE, York JD, Hare TR, et al. (1989) Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator. J Biol Chem 264: 17947-17952.
    • (1989) J Biol Chem , vol.264 , pp. 17947-17952
    • Gardell, S.J.1    Duong, L.T.2    Diehl, R.E.3    York, J.D.4    Hare, T.R.5
  • 11
    • 41349102554 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation by anopheline antiplatelet protein, a saliva protein from a malaria vector mosquito
    • Yoshida S, Sudo T, Niimi M, Tao L, Sun B, et al. (2008) Inhibition of collagen-induced platelet aggregation by anopheline antiplatelet protein, a saliva protein from a malaria vector mosquito. Blood 111: 2007-2014.
    • (2008) Blood , vol.111 , pp. 2007-2014
    • Yoshida, S.1    Sudo, T.2    Niimi, M.3    Tao, L.4    Sun, B.5
  • 12
    • 59049100529 scopus 로고    scopus 로고
    • Knockdown of proteins involved in iron metabolism limits tick reproduction and development
    • Hajdusek O, Sojka D, Kopacek P, Buresova V, Franta Z, et al. (2009) Knockdown of proteins involved in iron metabolism limits tick reproduction and development. Proc Natl Acad Sci U S A 106: 1033-1038.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 1033-1038
    • Hajdusek, O.1    Sojka, D.2    Kopacek, P.3    Buresova, V.4    Franta, Z.5
  • 13
    • 0004151015 scopus 로고
    • New York, (New York), Oxford University Press
    • Sonenshine DE, (1991) Biology of Ticks. Vol 1, New York, (New York) Oxford University Press.
    • (1991) Biology of Ticks , vol.1
    • Sonenshine, D.E.1
  • 14
    • 0000759663 scopus 로고
    • Blood digestion in ticks
    • In: Obenchain FD, Galun R, editors, Oxford, Pergamon Press
    • Akov S, (1982) Blood digestion in ticks. In: Obenchain FD, Galun R, editors. Physiology of ticks Oxford Pergamon Press pp. 197-212.
    • (1982) Physiology of Ticks , pp. 197-212
    • Akov, S.1
  • 16
    • 33748092082 scopus 로고    scopus 로고
    • Ticks, the ixodida
    • In: Marquardt WC, editors, London, Elsevier Academic Press
    • Klompen H, (2005) Ticks, the ixodida. In: Marquardt WC, editors. Biology of Disease Vectors London Elsevier Academic Press pp. 45-55.
    • (2005) Biology of Disease Vectors , pp. 45-55
    • Klompen, H.1
  • 17
    • 20344397442 scopus 로고    scopus 로고
    • Emerging tick-borne infections: rediscovered and better characterized, or truly 'new'?
    • Telford SR 3rd, Goethert HK, (2004) Emerging tick-borne infections: rediscovered and better characterized, or truly 'new'? Parasitology 129: S301-327.
    • (2004) Parasitology , vol.129
    • Telford III, S.R.1    Goethert, H.K.2
  • 18
    • 0242361756 scopus 로고    scopus 로고
    • Risk and prevention of transfusion-transmitted babesiosis and other tick-borne diseases
    • Cable RG, Leiby DA, (2003) Risk and prevention of transfusion-transmitted babesiosis and other tick-borne diseases. Curr Opin Hematol 10: 405-411.
    • (2003) Curr Opin Hematol , vol.10 , pp. 405-411
    • Cable, R.G.1    Leiby, D.A.2
  • 19
    • 0029098581 scopus 로고
    • Isolation of Coxiella burnetii from dairy cattle and ticks, and some characteristics of the isolates in Japan
    • Ho T, Htwe KK, Yamasaki N, Zhang GQ, Ogawa M, et al. (1995) Isolation of Coxiella burnetii from dairy cattle and ticks, and some characteristics of the isolates in Japan. Micribiol Immunol 39: 663-671.
    • (1995) Micribiol Immunol , vol.39 , pp. 663-671
    • Ho, T.1    Htwe, K.K.2    Yamasaki, N.3    Zhang, G.Q.4    Ogawa, M.5
  • 20
    • 0028366341 scopus 로고
    • The Taxonomy of the bovine Theileria spp
    • Fujisaki K, Kawaju S, Kamio T, (1994) The Taxonomy of the bovine Theileria spp. Parasitol Today 10: 31-33.
    • (1994) Parasitol Today , vol.10 , pp. 31-33
    • Fujisaki, K.1    Kawaju, S.2    Kamio, T.3
  • 21
    • 0001897462 scopus 로고
    • Tick attachment and feeding: role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response
    • In: Obenchain FD, Galun R, editors, New York, Pergamon Press Inc
    • Kemp DH, Stone BF, Binnington KC, (1982) Tick attachment and feeding: role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response. In: Obenchain FD, Galun R, editors. Physiology of Ticks New York Pergamon Press Inc pp. 119-168.
    • (1982) Physiology of Ticks , pp. 119-168
    • Kemp, D.H.1    Stone, B.F.2    Binnington, K.C.3
  • 22
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L, Smith DE, Arcuri KE, Vlasuk GP, (1990) Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248: 593-596.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 24
    • 39849098637 scopus 로고    scopus 로고
    • Salivating for knowledge: potential pharmacological agents in tick saliva
    • Hovius JW, Levi M, Fikrig E, (2008) Salivating for knowledge: potential pharmacological agents in tick saliva. PLoS Med 5: e43.
    • (2008) PLoS Med , vol.5
    • Hovius, J.W.1    Levi, M.2    Fikrig, E.3
  • 25
    • 35748980268 scopus 로고    scopus 로고
    • Variengin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick
    • Koh CY, Kazimirova M, Trimnell A, Takac P, Labuda M, et al. (2007) Variengin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. J Biol Chem 282: 29101-29113.
    • (2007) J Biol Chem , vol.282 , pp. 29101-29113
    • Koh, C.Y.1    Kazimirova, M.2    Trimnell, A.3    Takac, P.4    Labuda, M.5
  • 27
    • 77951299257 scopus 로고    scopus 로고
    • Longistatin, a novel EF-hand protein from the ixodid tick Haemaphysalis longicornis, is required for acquisition of host blood-meals
    • Anisuzzaman, Islam MK, Miyoshi T, Alim MA, Hatta T, et al. (2010) Longistatin, a novel EF-hand protein from the ixodid tick Haemaphysalis longicornis, is required for acquisition of host blood-meals. Int J Parasitol 40: 721-729.
    • (2010) Int J Parasitol , vol.40 , pp. 721-729
    • Anisuzzaman1    Islam, M.K.2    Miyoshi, T.3    Alim, M.A.4    Hatta, T.5
  • 28
    • 0021351054 scopus 로고
    • Kinetics of the activation of plasminogen by natural and recombinant tissue-type plasminogen activator
    • Zamarron C, Lijnen HR, Collen D, (1984) Kinetics of the activation of plasminogen by natural and recombinant tissue-type plasminogen activator. J Biol Chem 259: 2080-2083.
    • (1984) J Biol Chem , vol.259 , pp. 2080-2083
    • Zamarron, C.1    Lijnen, H.R.2    Collen, D.3
  • 29
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin
    • Hoylaerts M, Rijken DC, Lijnen HR, Collen D, (1982) Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 257: 2912-2919.
    • (1982) J Biol Chem , vol.257 , pp. 2912-2919
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3    Collen, D.4
  • 30
    • 0034011175 scopus 로고    scopus 로고
    • The fibrinolytic enzyme system. Basic principles and links to venous and arterial thrombosis
    • Wiman B, (2000) The fibrinolytic enzyme system. Basic principles and links to venous and arterial thrombosis. Hematol Oncol Clin North Am 14: 325-338.
    • (2000) Hematol Oncol Clin North Am , vol.14 , pp. 325-338
    • Wiman, B.1
  • 31
    • 0026544292 scopus 로고
    • Biochemical and biologic properties of rt-PA del (K296-G302), a recombinant human tissue-type plasminogen activator deletion mutant resistant to plasminogen activator inhibitor-1
    • Li XK, Lijnen HR, Nelles L, Van Hoef B, Stassen JM, et al. (1992) Biochemical and biologic properties of rt-PA del (K296-G302), a recombinant human tissue-type plasminogen activator deletion mutant resistant to plasminogen activator inhibitor-1. Blood 79: 417-429.
    • (1992) Blood , vol.79 , pp. 417-429
    • Li, X.K.1    Lijnen, H.R.2    Nelles, L.3    van Hoef, B.4    Stassen, J.M.5
  • 32
    • 74849106257 scopus 로고    scopus 로고
    • The molecular basis of thrombolysis and its clinical application in stroke
    • Murray V, Norrving B, Sandercock PA, Terént A, Wardlaw JM, et al. (2010) The molecular basis of thrombolysis and its clinical application in stroke. J Intern Med 267: 191-208.
    • (2010) J Intern Med , vol.267 , pp. 191-208
    • Murray, V.1    Norrving, B.2    Sandercock, P.A.3    Terént, A.4    Wardlaw, J.M.5
  • 33
    • 0023101988 scopus 로고
    • Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis
    • Tate KM, Higgins DL, Holmes WE, Winkler ME, Heyneker HL, et al. (1987) Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis. Biochemistry 26: 338-343.
    • (1987) Biochemistry , vol.26 , pp. 338-343
    • Tate, K.M.1    Higgins, D.L.2    Holmes, W.E.3    Winkler, M.E.4    Heyneker, H.L.5
  • 35
    • 0037692071 scopus 로고    scopus 로고
    • Identification and characterization of novel salivary thrombin inhibitors from ixodidae tick, Haemaphysalis longicornis
    • Iwanaga S, Okada M, Isawa H, Morita A, Yuda M, et al. (2003) Identification and characterization of novel salivary thrombin inhibitors from ixodidae tick, Haemaphysalis longicornis. Eur J Biochem 270: 1926-1934.
    • (2003) Eur J Biochem , vol.270 , pp. 1926-1934
    • Iwanaga, S.1    Okada, M.2    Isawa, H.3    Morita, A.4    Yuda, M.5
  • 36
    • 0028217639 scopus 로고
    • Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata
    • Karczewski J, Endris R, Connolly TM, (1994) Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata. J Biol Chem 269: 6702-6708.
    • (1994) J Biol Chem , vol.269 , pp. 6702-6708
    • Karczewski, J.1    Endris, R.2    Connolly, T.M.3
  • 37
  • 38
    • 0037904919 scopus 로고    scopus 로고
    • Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis
    • Francischetti IM, Mather TN, Ribeiro JM, (2003) Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem Biophys Res Commun 305: 869-875.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 869-875
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 39
    • 6844240861 scopus 로고    scopus 로고
    • Purification and amino acid sequence of halystase from snake venom of Agkistrodon halys blomhoffii, a serine protease that cleaves specifically fibrinogen and kininogen
    • Matsui T, Sakurai Y, Fujimura Y, Hayashi I, Oh-Ishi S, et al. (1998) Purification and amino acid sequence of halystase from snake venom of Agkistrodon halys blomhoffii, a serine protease that cleaves specifically fibrinogen and kininogen. Eur J Biochem 252: 569-575.
    • (1998) Eur J Biochem , vol.252 , pp. 569-575
    • Matsui, T.1    Sakurai, Y.2    Fujimura, Y.3    Hayashi, I.4    Oh-Ishi, S.5
  • 41
    • 31044445108 scopus 로고    scopus 로고
    • Thrombus formation in vivo
    • Furie B, Furie BC, (2005) Thrombus formation in vivo. J Clin Invest 115: 3355-3362.
    • (2005) J Clin Invest , vol.115 , pp. 3355-3362
    • Furie, B.1    Furie, B.C.2
  • 42
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • MacFarlane RG, (1964) An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202: 498-499.
    • (1964) Nature , vol.202 , pp. 498-499
    • MacFarlane, R.G.1
  • 43
    • 0141707850 scopus 로고    scopus 로고
    • Thrombin and fibrinolysis
    • Nesheim M, (2003) Thrombin and fibrinolysis. Chest 124: 33-39.
    • (2003) Chest , vol.124 , pp. 33-39
    • Nesheim, M.1
  • 44
    • 0028899505 scopus 로고
    • A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning
    • Zhang Y, Wisner A, Xiong Y, Bon C, (1995) A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning. J Biol Chem 270: 10246-10255.
    • (1995) J Biol Chem , vol.270 , pp. 10246-10255
    • Zhang, Y.1    Wisner, A.2    Xiong, Y.3    Bon, C.4
  • 45
    • 0037321482 scopus 로고    scopus 로고
    • Vampire bat salivary plasminogen activator (desmoteplase): a unique fibrinolytic enzyme that does not promote neurodegeneration
    • Liberatore GT, Samson A, Bladin C, Schleuning WD, Medcalf RL, (2003) Vampire bat salivary plasminogen activator (desmoteplase): a unique fibrinolytic enzyme that does not promote neurodegeneration. Stroke 34: 537-543.
    • (2003) Stroke , vol.34 , pp. 537-543
    • Liberatore, G.T.1    Samson, A.2    Bladin, C.3    Schleuning, W.D.4    Medcalf, R.L.5
  • 46
  • 47
    • 70049095289 scopus 로고    scopus 로고
    • The Kunitz-like modulatory protein, Haemangin, is vital for hard tick blood feeding success
    • Islam MK, Tsuji N, Miyoshi T, Alim MA, Huang X, et al. (2009) The Kunitz-like modulatory protein, Haemangin, is vital for hard tick blood feeding success. PLoS Pathog 5: e1000497.
    • (2009) PLoS Pathog , vol.5
    • Islam, M.K.1    Tsuji, N.2    Miyoshi, T.3    Alim, M.A.4    Huang, X.5
  • 48
    • 44949197678 scopus 로고    scopus 로고
    • A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks
    • Tsuji N, Miyoshi T, Battsetseg B, Matsuo T, Xuan X, et al. (2008) A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks. PLoS Pathog 4: e1000062.
    • (2008) PLoS Pathog , vol.4
    • Tsuji, N.1    Miyoshi, T.2    Battsetseg, B.3    Matsuo, T.4    Xuan, X.5
  • 49
    • 0038392822 scopus 로고    scopus 로고
    • Effects of DX-9065a, an inhibitor of factor Xa, on ellagic acid-induced plantar skin thrombosis assessed in tetrodotoxin- and N(omega)-nitro-L-arginine-treated rats
    • Chino D, Fujita Y, Ishii K, Nakayama K, (2003) Effects of DX-9065a, an inhibitor of factor Xa, on ellagic acid-induced plantar skin thrombosis assessed in tetrodotoxin- and N(omega)-nitro-L-arginine-treated rats. J Pharmacol Sci 91: 319-329.
    • (2003) J Pharmacol Sci , vol.91 , pp. 319-329
    • Chino, D.1    Fujita, Y.2    Ishii, K.3    Nakayama, K.4
  • 50
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • Alim MA, Tsuji N, Miyoshi T, Islam MK, Huang X, et al. (2007) Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis. Insect Biochem Mol Biol 37: 911-922.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 911-922
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Huang, X.5
  • 51
    • 0032521423 scopus 로고    scopus 로고
    • Binding of tissue-plasminogen activator to fibrin: effect of ultrasound
    • Siddiqi F, Odrljin TM, Fay PJ, Cox C, Francis CW, (1998) Binding of tissue-plasminogen activator to fibrin: effect of ultrasound. Blood 91: 2019-2025.
    • (1998) Blood , vol.91 , pp. 2019-2025
    • Siddiqi, F.1    Odrljin, T.M.2    Fay, P.J.3    Cox, C.4    Francis, C.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.