메뉴 건너뛰기




Volumn 54, Issue 4, 2009, Pages 408-412

Molecular cloning and characterization of ecto-5′-nucleotidase from the venoms of Gloydius blomhoffi

Author keywords

cDNA; Ecto 5 nucleotidase; Exosome; Gloydius blomhoffi; Snake venom

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; ECTO 5' NUCLEOTIDASE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; SNAKE VENOM;

EID: 67650363710     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2009.05.004     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 0036135117 scopus 로고    scopus 로고
    • Ophidian envenomation strategies and the role of purines
    • Aird S.D. Ophidian envenomation strategies and the role of purines. Toxicon 40 (2002) 335-393
    • (2002) Toxicon , vol.40 , pp. 335-393
    • Aird, S.D.1
  • 2
    • 33747761323 scopus 로고    scopus 로고
    • Anticoagulant effect of Naja naja venom 5′nucleotidase: demonstration through the use of novel specific inhibitor, vanillic acid
    • Dhananjaya B.L., Nataraju A., Rajesh R., Raghavendra Gowda C.D., Sharath B.K., Vishwanath B.S., and D'Souza C.J. Anticoagulant effect of Naja naja venom 5′nucleotidase: demonstration through the use of novel specific inhibitor, vanillic acid. Toxicon 48 (2006) 411-421
    • (2006) Toxicon , vol.48 , pp. 411-421
    • Dhananjaya, B.L.1    Nataraju, A.2    Rajesh, R.3    Raghavendra Gowda, C.D.4    Sharath, B.K.5    Vishwanath, B.S.6    D'Souza, C.J.7
  • 3
    • 0022358681 scopus 로고
    • An improved procedure for purifying 5′-nucleotidase from various sources. Evidence for tissue and species differences in their molecular mass and affinity for F-actin
    • Dieckhoff J., Knebel H., Heidemann M., and Mannherz H.G. An improved procedure for purifying 5′-nucleotidase from various sources. Evidence for tissue and species differences in their molecular mass and affinity for F-actin. Eur. J. Biochem. 151 (1985) 377-383
    • (1985) Eur. J. Biochem. , vol.151 , pp. 377-383
    • Dieckhoff, J.1    Knebel, H.2    Heidemann, M.3    Mannherz, H.G.4
  • 4
    • 0014249131 scopus 로고
    • Fractionation of Vipera russelli venom by gel filtration. I
    • Dimitrov G.D., and Kankonkar R.C. Fractionation of Vipera russelli venom by gel filtration. I. Toxicon 5 (1968) 213-221
    • (1968) Toxicon , vol.5 , pp. 213-221
    • Dimitrov, G.D.1    Kankonkar, R.C.2
  • 6
    • 0025779164 scopus 로고
    • Purification of 5′-nucleotidase from human seminal plasma
    • Fini C., Coli M., and Floridi A. Purification of 5′-nucleotidase from human seminal plasma. Biochim. Biophys. Acta 1075 (1991) 20-27
    • (1991) Biochim. Biophys. Acta , vol.1075 , pp. 20-27
    • Fini, C.1    Coli, M.2    Floridi, A.3
  • 7
    • 0025216517 scopus 로고
    • 5′-Nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein
    • Fini C., Palmerini C.A., Damiani P., Stochaj U., Mannherz H.G., and Floridi A. 5′-Nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein. Biochim. Biophys. Acta 1038 (1990) 18-22
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 18-22
    • Fini, C.1    Palmerini, C.A.2    Damiani, P.3    Stochaj, U.4    Mannherz, H.G.5    Floridi, A.6
  • 8
    • 0038676998 scopus 로고    scopus 로고
    • Biochemical and mass spectrometric characterization of soluble ecto-5′-nucleotidase from bull seminal plasma
    • Fini C., Talamo F., Cherri S., Coli M., Floridi A., Ferrara L., and Scaloni A. Biochemical and mass spectrometric characterization of soluble ecto-5′-nucleotidase from bull seminal plasma. Biochem. J. 372 (2003) 443-451
    • (2003) Biochem. J. , vol.372 , pp. 443-451
    • Fini, C.1    Talamo, F.2    Cherri, S.3    Coli, M.4    Floridi, A.5    Ferrara, L.6    Scaloni, A.7
  • 9
    • 0025952271 scopus 로고
    • Pharmacological receptors on blood platelets
    • Hourani S.M.O., and Cusack N.J. Pharmacological receptors on blood platelets. Pharmacol. Rev. 43 (1991) 243-298
    • (1991) Pharmacol. Rev. , vol.43 , pp. 243-298
    • Hourani, S.M.O.1    Cusack, N.J.2
  • 10
    • 0002370964 scopus 로고
    • Enzymes in snake venom
    • Snake Venoms. Lee C.-Y. (Ed), Springer Verlag, New York
    • Iwanaga S., and Suzuki T. Enzymes in snake venom. In: Lee C.-Y. (Ed). Snake Venoms. Handbook of Experimental Pharmacology vol. 52 (1979), Springer Verlag, New York 61-158
    • (1979) Handbook of Experimental Pharmacology , vol.52 , pp. 61-158
    • Iwanaga, S.1    Suzuki, T.2
  • 11
    • 0032725002 scopus 로고    scopus 로고
    • 5′-Nucleotidase as a marker of both general and local inflammation in rheumatoid arthritis patients
    • Johnson S.M., Patel S., Bruckner F.E., and Collins D.A. 5′-Nucleotidase as a marker of both general and local inflammation in rheumatoid arthritis patients. Rheumatology (Oxford) 38 (1999) 391-396
    • (1999) Rheumatology (Oxford) , vol.38 , pp. 391-396
    • Johnson, S.M.1    Patel, S.2    Bruckner, F.E.3    Collins, D.A.4
  • 12
    • 33645314949 scopus 로고    scopus 로고
    • Exosomes biological significance: a concise review
    • Johnstone R.M. Exosomes biological significance: a concise review. Blood Cells Mol. Dis. 36 (2006) 315-321
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 315-321
    • Johnstone, R.M.1
  • 13
    • 0025147709 scopus 로고
    • Effects of snake venom proteins on blood platelets
    • Kini R.M., and Evans H.J. Effects of snake venom proteins on blood platelets. Toxicon 28 (1990) 1387-1422
    • (1990) Toxicon , vol.28 , pp. 1387-1422
    • Kini, R.M.1    Evans, H.J.2
  • 15
    • 0033136411 scopus 로고    scopus 로고
    • Cloning and expression of ecto 5′-nucleotidase from the cattle tick Boophilus microplus
    • Liyou N., Hamilton S., Elvin C., and Willadsen P. Cloning and expression of ecto 5′-nucleotidase from the cattle tick Boophilus microplus. Insect Mol. Biol. 8 (1999) 257-266
    • (1999) Insect Mol. Biol. , vol.8 , pp. 257-266
    • Liyou, N.1    Hamilton, S.2    Elvin, C.3    Willadsen, P.4
  • 16
    • 0025709722 scopus 로고
    • Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form
    • Misumi Y., Ogata S., Ohkubo K., Hirose S., and Ikehara Y. Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form. Eur. J. Biochem. 191 (1990) 563-569
    • (1990) Eur. J. Biochem. , vol.191 , pp. 563-569
    • Misumi, Y.1    Ogata, S.2    Ohkubo, K.3    Hirose, S.4    Ikehara, Y.5
  • 17
    • 0025004134 scopus 로고
    • Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid
    • Misumi Y., Ogata S., Hirose S., and Ikehara Y. Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid. J. Biol. Chem. 265 (1990) 2178-2183
    • (1990) J. Biol. Chem. , vol.265 , pp. 2178-2183
    • Misumi, Y.1    Ogata, S.2    Hirose, S.3    Ikehara, Y.4
  • 18
    • 33747782553 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of dipeptidyl peptidase IV from the venom of Gloydius blomhoffi brevicaudus
    • Ogawa Y., Mamura Y., Murayama N., and Yanoshita R. Characterization and cDNA cloning of dipeptidyl peptidase IV from the venom of Gloydius blomhoffi brevicaudus. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 145 (2006) 35-42
    • (2006) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.145 , pp. 35-42
    • Ogawa, Y.1    Mamura, Y.2    Murayama, N.3    Yanoshita, R.4
  • 19
    • 34249031902 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of aminopeptidase A from the venom of Gloydius blomhoffi brevicaudus
    • Ogawa Y., Murayama N., Fujita Y., and Yanoshita R. Characterization and cDNA cloning of aminopeptidase A from the venom of Gloydius blomhoffi brevicaudus. Toxicon 49 (2007) 1172-1181
    • (2007) Toxicon , vol.49 , pp. 1172-1181
    • Ogawa, Y.1    Murayama, N.2    Fujita, Y.3    Yanoshita, R.4
  • 21
    • 0021038657 scopus 로고
    • Inhibition of platelet aggregation by 5′-nucleotidase purified from Trimeresurus gramineus snake venom
    • Ouyang C., and Huang T.F. Inhibition of platelet aggregation by 5′-nucleotidase purified from Trimeresurus gramineus snake venom. Toxicon 21 (1983) 491-501
    • (1983) Toxicon , vol.21 , pp. 491-501
    • Ouyang, C.1    Huang, T.F.2
  • 22
    • 0022998890 scopus 로고
    • Platelet aggregation inhibitors from Agkistrodon acutus snake venom
    • Ouyang C., and Huang T.F. Platelet aggregation inhibitors from Agkistrodon acutus snake venom. Toxicon 24 (1986) 1099-1106
    • (1986) Toxicon , vol.24 , pp. 1099-1106
    • Ouyang, C.1    Huang, T.F.2
  • 23
    • 0022201056 scopus 로고
    • Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes
    • Pan B.T., Teng K., Wu C., Adam M., and Johnstone R.M. Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. J. Cell. Biol. 101 (1985) 942-948
    • (1985) J. Cell. Biol. , vol.101 , pp. 942-948
    • Pan, B.T.1    Teng, K.2    Wu, C.3    Adam, M.4    Johnstone, R.M.5
  • 24
    • 36749065757 scopus 로고    scopus 로고
    • Venom phosphatases and 5′-nucleotidase
    • Bailey G.S. (Ed), Alaken, Inc., Colorado
    • Rael E.D. Venom phosphatases and 5′-nucleotidase. In: Bailey G.S. (Ed). Enzymes From Snake Venom (1998), Alaken, Inc., Colorado 405-423
    • (1998) Enzymes From Snake Venom , pp. 405-423
    • Rael, E.D.1
  • 26
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 28
    • 43149120419 scopus 로고    scopus 로고
    • Exosome function: from tumor immunology to pathogen biology
    • Schorey J.S., and Bhatnagar S. Exosome function: from tumor immunology to pathogen biology. Traffic 9 (2008) 871-881
    • (2008) Traffic , vol.9 , pp. 871-881
    • Schorey, J.S.1    Bhatnagar, S.2
  • 29
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: current perspectives
    • Simpson R.J., Jensen S.S., and Lim J.W. Proteomic profiling of exosomes: current perspectives. Proteomics 8 (2008) 4083-4099
    • (2008) Proteomics , vol.8 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 30
    • 34047250594 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase: structure function relationships
    • Sträter N. Ecto-5′-nucleotidase: structure function relationships. Purinergic Signal. 2 (2006) 343-350
    • (2006) Purinergic Signal. , vol.2 , pp. 343-350
    • Sträter, N.1
  • 31
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles
    • Thery C., Boussac M., Veron P., Ricciardi-Castagnoli P., Raposo G., Garin J., and Amigorena S. Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles. J. Immunol. 166 (2001) 7309-7318
    • (2001) J. Immunol. , vol.166 , pp. 7309-7318
    • Thery, C.1    Boussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5    Garin, J.6    Amigorena, S.7
  • 33
    • 0026343113 scopus 로고
    • 5′-Nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes
    • Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., and Zimmermann H. 5′-Nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes. Eur. J. Biochem. 202 (1991) 855-861
    • (1991) Eur. J. Biochem. , vol.202 , pp. 855-861
    • Volknandt, W.1    Vogel, M.2    Pevsner, J.3    Misumi, Y.4    Ikehara, Y.5    Zimmermann, H.6
  • 34
    • 0016369672 scopus 로고
    • Purification of rat liver 5′-nucleotidase as a complex with sphingomyelin
    • Widnell C.C. Purification of rat liver 5′-nucleotidase as a complex with sphingomyelin. Methods Enzymol. 32 Part B (1974) 368-374
    • (1974) Methods Enzymol. , vol.32 , Issue.PART B , pp. 368-374
    • Widnell, C.C.1
  • 35
    • 0026729643 scopus 로고
    • 5′-Nucleotidase: molecular structure and functional aspects
    • Zimmermann H. 5′-Nucleotidase: molecular structure and functional aspects. Biochem. J. 285 (1992) 345-365
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 36
    • 0033766981 scopus 로고    scopus 로고
    • Extracellular metabolism of ATP and other nucleotides
    • Zimmermann H. Extracellular metabolism of ATP and other nucleotides. Naunyn. Schmiedebergs Arch. Pharmacol. 362 (2000) 299-309
    • (2000) Naunyn. Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 299-309
    • Zimmermann, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.