메뉴 건너뛰기




Volumn 1760, Issue 12, 2006, Pages 1762-1771

Biochemical characterization and molecular cloning of a plasminogen activator proteinase (LV-PA) from bushmaster snake venom

Author keywords

Bushmaster; cDNA; Fibrinolysis; Lachesis muta; Plasminogen activator; Serine proteinase

Indexed keywords

ASPARAGINE; CHROMOGENIC SUBSTRATE; COMPLEMENTARY DNA; ENZYME; N GLYCOSIDASE F; PLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR PROTEINASE; PLASMINOGEN ACTIVATOR PROTEINASE INHIBITOR; PROTEINASE; SNAKE VENOM; TRYPSIN; UNCLASSIFIED DRUG;

EID: 33750630967     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.08.023     Document Type: Article
Times cited : (30)

References (41)
  • 1
    • 0032696699 scopus 로고    scopus 로고
    • Matrix metalloproteinases system deficiencies and matrix degradation
    • Lijnen H.R., and Collen D. Matrix metalloproteinases system deficiencies and matrix degradation. Thromb. Haemost. 82 (1999) 837-845
    • (1999) Thromb. Haemost. , vol.82 , pp. 837-845
    • Lijnen, H.R.1    Collen, D.2
  • 2
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • Collen D., and Lijnen H.R. Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 78 (1991) 3114-3124
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 3
    • 0029102856 scopus 로고
    • Gene targeting and gene transfer studies of the plasminogen/plasmin system: implications in thrombosis, hemostasis, neointima formation, and atherosclerosis
    • Carmeliet P., and Collen D. Gene targeting and gene transfer studies of the plasminogen/plasmin system: implications in thrombosis, hemostasis, neointima formation, and atherosclerosis. FASEB J. 9 (1995) 934-938
    • (1995) FASEB J. , vol.9 , pp. 934-938
    • Carmeliet, P.1    Collen, D.2
  • 4
    • 0034923623 scopus 로고    scopus 로고
    • Extracellular proteolysis and angiogenesis
    • Pepper M.S. Extracellular proteolysis and angiogenesis. Thromb. Haemost. 86 (2001) 346-355
    • (2001) Thromb. Haemost. , vol.86 , pp. 346-355
    • Pepper, M.S.1
  • 5
    • 0033965923 scopus 로고    scopus 로고
    • Molecular mechanism of plasminogen activation: bacterial cofactors provide clues
    • Parry A.A., Zhang X.C., and Bode W. Molecular mechanism of plasminogen activation: bacterial cofactors provide clues. TIBS 25 (2000) 53-59
    • (2000) TIBS , vol.25 , pp. 53-59
    • Parry, A.A.1    Zhang, X.C.2    Bode, W.3
  • 6
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chandler H.A. Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr. Opin. Cell Biol. 9 (1997) 714-724
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 714-724
    • Chandler, H.A.1
  • 7
    • 0035225553 scopus 로고    scopus 로고
    • Ham-Wasserman Lecture: Role of the plasminogen system in fibrin-homeostasis and tissue remodeling
    • Collen D. Ham-Wasserman Lecture: Role of the plasminogen system in fibrin-homeostasis and tissue remodeling. Hematology 2001 (2001) 1-9
    • (2001) Hematology , vol.2001 , pp. 1-9
    • Collen, D.1
  • 8
    • 1542476175 scopus 로고
    • Development of a new fibrinolytic agents
    • Bloom A.L., Forbes C.D., Thomas D.P., and Tuddenham E.G.D. (Eds), Churchill Livingstone, Edinburgh
    • Lijnen H.R., and Collen D. Development of a new fibrinolytic agents. In: Bloom A.L., Forbes C.D., Thomas D.P., and Tuddenham E.G.D. (Eds). Haemostasis and Thrombosis (1994), Churchill Livingstone, Edinburgh 625-637
    • (1994) Haemostasis and Thrombosis , pp. 625-637
    • Lijnen, H.R.1    Collen, D.2
  • 9
    • 0033741151 scopus 로고    scopus 로고
    • Snake venom proteins acting on hemostasis
    • Braud S., Bon C., and Wisner A. Snake venom proteins acting on hemostasis. Biochimie 82 (2000) 851-859
    • (2000) Biochimie , vol.82 , pp. 851-859
    • Braud, S.1    Bon, C.2    Wisner, A.3
  • 10
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland F.S. Snake venoms and the hemostatic system. Toxicon 36 (1998) 1749-1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 11
    • 19544362198 scopus 로고    scopus 로고
    • Practical applications of snake venom toxins in haemostasis
    • Marsh N., and Williams V. Practical applications of snake venom toxins in haemostasis. Toxicon 45 (2005) 1171-1181
    • (2005) Toxicon , vol.45 , pp. 1171-1181
    • Marsh, N.1    Williams, V.2
  • 12
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • Perona J.J., and Craik C.S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272 (1997) 29987-29990
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 14
    • 0030714651 scopus 로고    scopus 로고
    • Snake venoms
    • Markland F.S. Snake venoms. Drugs 3 (1997) 1-10
    • (1997) Drugs , vol.3 , pp. 1-10
    • Markland, F.S.1
  • 15
    • 0028899505 scopus 로고
    • A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning
    • Zhang Y., Wisner A., Xiong Y., and Bon C. A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning. J. Biol. Chem. 270 (1995) 10246-10255
    • (1995) J. Biol. Chem. , vol.270 , pp. 10246-10255
    • Zhang, Y.1    Wisner, A.2    Xiong, Y.3    Bon, C.4
  • 17
    • 0342359205 scopus 로고    scopus 로고
    • Action of metalloproteinases mutalysin I and II on several components of hemostatic and fibrinolytic systems
    • Estevao-Costa M.I., Diniz C.R., Magalhaes A., Markland F.S., and Sanchez E.F. Action of metalloproteinases mutalysin I and II on several components of hemostatic and fibrinolytic systems. Thromb. Res. 99 (2000) 363-376
    • (2000) Thromb. Res. , vol.99 , pp. 363-376
    • Estevao-Costa, M.I.1    Diniz, C.R.2    Magalhaes, A.3    Markland, F.S.4    Sanchez, E.F.5
  • 18
    • 33750605786 scopus 로고    scopus 로고
    • Mutalysins
    • Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds), Elsevier Ltd
    • Sanchez E.F. Mutalysins. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes. 2nd Ed. (2004), Elsevier Ltd 692-694
    • (2004) Handbook of Proteolytic Enzymes. 2nd Ed. , pp. 692-694
    • Sanchez, E.F.1
  • 20
    • 10944240203 scopus 로고    scopus 로고
    • Biochemical properties of a bushmaster snake venom serine proteinase (LV-Ka), and its kining releasing activity evaluated in mesenteric arterial rings
    • Weinberg M.L.D., Felicori L.F., Bello C., Magalhaes H.P.B., Almeida A.P., Magalhaes A., and Sanchez E.F. Biochemical properties of a bushmaster snake venom serine proteinase (LV-Ka), and its kining releasing activity evaluated in mesenteric arterial rings. J. Pharmacol. Sci. 96 (2004) 333-342
    • (2004) J. Pharmacol. Sci. , vol.96 , pp. 333-342
    • Weinberg, M.L.D.1    Felicori, L.F.2    Bello, C.3    Magalhaes, H.P.B.4    Almeida, A.P.5    Magalhaes, A.6    Sanchez, E.F.7
  • 23
    • 0032403414 scopus 로고    scopus 로고
    • Expression and characterization of a novel plasminogen activator from Agkistrodon halys venom
    • Park D., Kim H., Chung K., Kim D.-S., and Yun Y. Expression and characterization of a novel plasminogen activator from Agkistrodon halys venom. Toxicon 36 (1998) 1807-1819
    • (1998) Toxicon , vol.36 , pp. 1807-1819
    • Park, D.1    Kim, H.2    Chung, K.3    Kim, D.-S.4    Yun, Y.5
  • 24
    • 15944361904 scopus 로고    scopus 로고
    • Specific identification of Lachesis muta muta snake venom using antibodies against the plasminogen activator enzyme. LV-PA
    • Felicori L.F., Chavez-Olortegui C., and Sanchez E.F. Specific identification of Lachesis muta muta snake venom using antibodies against the plasminogen activator enzyme. LV-PA. Toxicon 45 (2005) 803-806
    • (2005) Toxicon , vol.45 , pp. 803-806
    • Felicori, L.F.1    Chavez-Olortegui, C.2    Sanchez, E.F.3
  • 26
    • 0025620159 scopus 로고
    • Statistical treatment for solution of a family of simultaneous equations derived from enzyme inhibition studies
    • Junqueira R.G., and Mares-Guia M. Statistical treatment for solution of a family of simultaneous equations derived from enzyme inhibition studies. Braz. J. Med. Biol. Res. 23 (1990) 773-784
    • (1990) Braz. J. Med. Biol. Res. , vol.23 , pp. 773-784
    • Junqueira, R.G.1    Mares-Guia, M.2
  • 27
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin J.M., Przybyla A.E., MacDonald R.J., and Rutter W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18 (1979) 5294-5299
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 28
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • Pelham H.R., and Jackson R.J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur. J. Biochem. 67 (1976) 247-256
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.1    Jackson, R.J.2
  • 29
    • 0035955692 scopus 로고    scopus 로고
    • Molecular cloning and expression of a functional snake venom vascular endothelium growh factor (VEGF) from the Bothrops insularis pit viper. A new member of the VEGF family of proteins
    • Junqueira de Acevedo I.L., Farsky S.H., Oliveira M.L., and Ho P.L. Molecular cloning and expression of a functional snake venom vascular endothelium growh factor (VEGF) from the Bothrops insularis pit viper. A new member of the VEGF family of proteins. J. Biol. Chem. 276 (2001) 39836-39842
    • (2001) J. Biol. Chem. , vol.276 , pp. 39836-39842
    • Junqueira de Acevedo, I.L.1    Farsky, S.H.2    Oliveira, M.L.3    Ho, P.L.4
  • 33
    • 0032919106 scopus 로고    scopus 로고
    • Diet and snake venom evolution: can local selection alone explain intraspecific venom variation?
    • Sasa M. Diet and snake venom evolution: can local selection alone explain intraspecific venom variation?. Toxicon 37 (1999) 249-252
    • (1999) Toxicon , vol.37 , pp. 249-252
    • Sasa, M.1
  • 34
    • 0030878832 scopus 로고    scopus 로고
    • Trimeresurus stejnegeri snake venom plasminogen activator. Site directed mutagenesis and molecular modeling
    • Zhang Y., Wisner A., Maroun R.C., Choumet V., Xiong Y., and Bon C. Trimeresurus stejnegeri snake venom plasminogen activator. Site directed mutagenesis and molecular modeling. J. Biol. Chem. 272 (1997) 20531-20537
    • (1997) J. Biol. Chem. , vol.272 , pp. 20531-20537
    • Zhang, Y.1    Wisner, A.2    Maroun, R.C.3    Choumet, V.4    Xiong, Y.5    Bon, C.6
  • 35
    • 0035865501 scopus 로고    scopus 로고
    • Serine proteinase isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis
    • Wang Y.-M., Wang S.-R., and Tsai I.-H. Serine proteinase isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis. Biochem. J. 354 (2001) 161-168
    • (2001) Biochem. J. , vol.354 , pp. 161-168
    • Wang, Y.-M.1    Wang, S.-R.2    Tsai, I.-H.3
  • 36
    • 19544394247 scopus 로고    scopus 로고
    • Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved
    • Serrano M.T., and Maroun R.C. Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved. Toxicon 45 (2005) 1115-1132
    • (2005) Toxicon , vol.45 , pp. 1115-1132
    • Serrano, M.T.1    Maroun, R.C.2
  • 37
    • 0035743546 scopus 로고    scopus 로고
    • Molecular basis for the partition of the essential functions of thrombin among snake venom serine proteinases
    • Maroun R.C. Molecular basis for the partition of the essential functions of thrombin among snake venom serine proteinases. Haemostasis 31 (2001) 247-256
    • (2001) Haemostasis , vol.31 , pp. 247-256
    • Maroun, R.C.1
  • 39
    • 0027305178 scopus 로고
    • The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta)
    • Magalhaes A., Da Fonseca B.B.C., Diniz C.R., Gilroy J., and Richardson M. The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta). FEBS Lett. 329 (1993) 116-120
    • (1993) FEBS Lett. , vol.329 , pp. 116-120
    • Magalhaes, A.1    Da Fonseca, B.B.C.2    Diniz, C.R.3    Gilroy, J.4    Richardson, M.5
  • 40
    • 0037376318 scopus 로고    scopus 로고
    • The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody
    • Harrison R.A., Wüster W., and Theakston R.D.G. The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody. Toxicon 41 (2003) 441-449
    • (2003) Toxicon , vol.41 , pp. 441-449
    • Harrison, R.A.1    Wüster, W.2    Theakston, R.D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.