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Volumn 54, Issue 4, 2009, Pages 413-420

Purification and characterization of the biological effects of phospholipase A2 from sea anemone Bunodosoma caissarum

Author keywords

Biological effects; Bunodosoma caissarum; Phospholipase A2

Indexed keywords

CHLORIDE; GLUCOSE; MORIN; PHOSPHOLIPASE A2; POTASSIUM; SODIUM;

EID: 67650293590     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2009.05.005     Document Type: Article
Times cited : (36)

References (56)
  • 2
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • Anderluh G., and Macek P. Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). Toxicon 40 (2002) 111-124
    • (2002) Toxicon , vol.40 , pp. 111-124
    • Anderluh, G.1    Macek, P.2
  • 3
    • 0037377170 scopus 로고    scopus 로고
    • Effect of Tityus serrulatus scorpion venom and its major toxin, TsTX-I, on the complement system in vivo
    • Bertazzi. Effect of Tityus serrulatus scorpion venom and its major toxin, TsTX-I, on the complement system in vivo. Toxicon 41 4 (2003) 501-508
    • (2003) Toxicon , vol.41 , Issue.4 , pp. 501-508
    • Bertazzi1
  • 5
    • 0014939327 scopus 로고
    • Gluconeogenesis in the isolated perfused isolated rat kidney
    • Bowman R.H. Gluconeogenesis in the isolated perfused isolated rat kidney. J. Biol. Chem. 245 (1970) 1604-1612
    • (1970) J. Biol. Chem. , vol.245 , pp. 1604-1612
    • Bowman, R.H.1
  • 6
    • 0029840994 scopus 로고    scopus 로고
    • Severe acute renal failure induced by the venom of Lonomia caterpillars
    • Burdmann E.A., Antunes I., Saldanha L.B., and Abdulkader R.C. Severe acute renal failure induced by the venom of Lonomia caterpillars. Clin. Nephrol. 46 (1996) 337-339
    • (1996) Clin. Nephrol. , vol.46 , pp. 337-339
    • Burdmann, E.A.1    Antunes, I.2    Saldanha, L.B.3    Abdulkader, R.C.4
  • 9
    • 0025091499 scopus 로고
    • 2 from snake venom to human secreted forms
    • 2 from snake venom to human secreted forms. J. Mol. Evol. 31 3 (1990) 228-238
    • (1990) J. Mol. Evol. , vol.31 , Issue.3 , pp. 228-238
    • Davidson, F.F.1    Dennis, E.A.2
  • 10
    • 0032549630 scopus 로고    scopus 로고
    • Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4
    • Diochot S., Schweitz H., Béress L., and Lazdunski M. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J. Biol. Chem. 273 12 (1998)
    • (1998) J. Biol. Chem. , vol.273 , Issue.12
    • Diochot, S.1    Schweitz, H.2    Béress, L.3    Lazdunski, M.4
  • 11
    • 0037899621 scopus 로고    scopus 로고
    • APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels
    • Diochot S., Loret E., Bruhn T., Béress L., and Lazdunski M. APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol. Pharmacol. 64 1 (2003) 59-69
    • (2003) Mol. Pharmacol. , vol.64 , Issue.1 , pp. 59-69
    • Diochot, S.1    Loret, E.2    Bruhn, T.3    Béress, L.4    Lazdunski, M.5
  • 12
    • 2342629343 scopus 로고    scopus 로고
    • A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons
    • Diochot S., Baron A., Rash L.D., Deval E., Escoubas P., Scarzello S., Salinas M., and Lazdunski M. A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 23 7 (2004) 1516-1525
    • (2004) EMBO J. , vol.23 , Issue.7 , pp. 1516-1525
    • Diochot, S.1    Baron, A.2    Rash, L.D.3    Deval, E.4    Escoubas, P.5    Scarzello, S.6    Salinas, M.7    Lazdunski, M.8
  • 14
    • 0023025145 scopus 로고
    • Anomalies in sea-urchin egg development induced by a novel purine isolated from the sea-anemone Bunodosoma caissarum
    • Freitas J.C., and Sawaya M.I. Anomalies in sea-urchin egg development induced by a novel purine isolated from the sea-anemone Bunodosoma caissarum. Toxicon 24 8 (1986) 751-755
    • (1986) Toxicon , vol.24 , Issue.8 , pp. 751-755
    • Freitas, J.C.1    Sawaya, M.I.2
  • 15
    • 0024994001 scopus 로고
    • Increase of mammalian intestinal motility by the iminopurine caissarone isolated from the sea anemone Bunodosoma caissarum
    • Freitas J.C., and Sawaya M.I. Increase of mammalian intestinal motility by the iminopurine caissarone isolated from the sea anemone Bunodosoma caissarum. Toxicon 28 9 (1990) 1029-1037
    • (1990) Toxicon , vol.28 , Issue.9 , pp. 1029-1037
    • Freitas, J.C.1    Sawaya, M.I.2
  • 17
    • 0020730261 scopus 로고
    • Support of kidney function by long-fatty acids derived from renal tissue
    • Fonteles M.C., Cohen J.J., Black A.J., and Wertheim S.J. Support of kidney function by long-fatty acids derived from renal tissue. Am. J. Physiol. 244 (1983) 235-246
    • (1983) Am. J. Physiol. , vol.244 , pp. 235-246
    • Fonteles, M.C.1    Cohen, J.J.2    Black, A.J.3    Wertheim, S.J.4
  • 18
    • 0033961566 scopus 로고    scopus 로고
    • 2 component of sea anemone (Aiptasia pallida) nematocyst venom
    • 2 component of sea anemone (Aiptasia pallida) nematocyst venom. Toxicon 38 (2000) 931-943
    • (2000) Toxicon , vol.38 , pp. 931-943
    • Grotendorst, G.R.1    Hessinger, D.A.2
  • 19
    • 27744443755 scopus 로고    scopus 로고
    • Biochemical, pharmacological and structural characterization of a new PLA(2) from Crotalus durissus terrificus (South American rattlesnake) venom
    • Hernandez-Oliveira S., Toyama M.H., Toyama D.O., Marangoni S., Hyslop S., and Rodrigues-Simioni L. Biochemical, pharmacological and structural characterization of a new PLA(2) from Crotalus durissus terrificus (South American rattlesnake) venom. Protein J. 24 4 (2005) 233-242
    • (2005) Protein J. , vol.24 , Issue.4 , pp. 233-242
    • Hernandez-Oliveira, S.1    Toyama, M.H.2    Toyama, D.O.3    Marangoni, S.4    Hyslop, S.5    Rodrigues-Simioni, L.6
  • 21
    • 0033857188 scopus 로고    scopus 로고
    • cDNA cloning and sequencing of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera
    • Kishimura H., Ojima T., Hayashi K., and Nishita K. cDNA cloning and sequencing of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 126 4 (2000) 579-586
    • (2000) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.126 , Issue.4 , pp. 579-586
    • Kishimura, H.1    Ojima, T.2    Hayashi, K.3    Nishita, K.4
  • 25
    • 78651170765 scopus 로고
    • The effect of sympathetic nerve stimulation on vasoconstrictor responses in perfused mesenteric blood vessels of the rat
    • McGregor D.D. The effect of sympathetic nerve stimulation on vasoconstrictor responses in perfused mesenteric blood vessels of the rat. J. Physiol. 177 (1965) 21-30
    • (1965) J. Physiol. , vol.177 , pp. 21-30
    • McGregor, D.D.1
  • 27
    • 0025670449 scopus 로고
    • Antimitotic effect of an extract of the sea anemone Bunodosoma caissarum on sea urchin egg development
    • Malpezzi E.L., and Freitas J.C. Antimitotic effect of an extract of the sea anemone Bunodosoma caissarum on sea urchin egg development. Braz. J. Med. Biol. Res. 23 9 (1990) 811-814
    • (1990) Braz. J. Med. Biol. Res. , vol.23 , Issue.9 , pp. 811-814
    • Malpezzi, E.L.1    Freitas, J.C.2
  • 28
    • 0026361836 scopus 로고
    • Hemolytic activity of the nematocyst venom from the sea anemone Bunodosoma caissarum
    • Malpezzi E.L., and Freitas J.C. Hemolytic activity of the nematocyst venom from the sea anemone Bunodosoma caissarum. Braz. J. Med. Biol. Res. 24 12 (1991) 1245-1249
    • (1991) Braz. J. Med. Biol. Res. , vol.24 , Issue.12 , pp. 1245-1249
    • Malpezzi, E.L.1    Freitas, J.C.2
  • 30
    • 0017902756 scopus 로고
    • Free water clearance curves during saline, mannitol, glucose and urea
    • Martinez-Maldonato M., and Opava-Stitzer S. Free water clearance curves during saline, mannitol, glucose and urea. J. Physiol. 280 (1978) 487-497
    • (1978) J. Physiol. , vol.280 , pp. 487-497
    • Martinez-Maldonato, M.1    Opava-Stitzer, S.2
  • 32
    • 0033580090 scopus 로고    scopus 로고
    • Synaptosomal glutamate release induced by the fraction Bc2 from the venom of the sea anemone Bunodosoma caissarum
    • Migues P.V., Leal R.B., Mantovani M., Nicolau M., and Gabilan N.H. Synaptosomal glutamate release induced by the fraction Bc2 from the venom of the sea anemone Bunodosoma caissarum. NeuroReport 10 (1999) 67-70
    • (1999) NeuroReport , vol.10 , pp. 67-70
    • Migues, P.V.1    Leal, R.B.2    Mantovani, M.3    Nicolau, M.4    Gabilan, N.H.5
  • 33
    • 34548358877 scopus 로고    scopus 로고
    • A protein toxin from the sea anemone Phyllodiscus semoni targets the kidney and causes a severe renal injury with predominant glomerular endothelial damage
    • Mizuno M., Nozaki M., Morine N., Suzuki N., Nishikawa K., Morgan B.P., and Matsuo S. A protein toxin from the sea anemone Phyllodiscus semoni targets the kidney and causes a severe renal injury with predominant glomerular endothelial damage. Am. J. Pathol. 1 2 (2007) 402-414
    • (2007) Am. J. Pathol. , vol.1 , Issue.2 , pp. 402-414
    • Mizuno, M.1    Nozaki, M.2    Morine, N.3    Suzuki, N.4    Nishikawa, K.5    Morgan, B.P.6    Matsuo, S.7
  • 35
    • 3042653199 scopus 로고    scopus 로고
    • The catalytic activity, but not receptor binding, of sPLA(2)s plays a critical role for neurite outgrowth induction in PC12 cells
    • Nakashima S., Kitamoto K., and Arioka M. The catalytic activity, but not receptor binding, of sPLA(2)s plays a critical role for neurite outgrowth induction in PC12 cells. Brain Res. 1015 (2004) 207-211
    • (2004) Brain Res. , vol.1015 , pp. 207-211
    • Nakashima, S.1    Kitamoto, K.2    Arioka, M.3
  • 38
    • 11144224125 scopus 로고    scopus 로고
    • Characterization of the insulinotropic action of a phospholipase A(2) isolated from Crotalus durissus collilineatus rattlesnake venom on rat pancreatic islets
    • Nogueira T.C.A., Ferreira F., Toyama M.H., Spoppiglia L.F., Maragoni S., Boschero A.C., and Carneiro E.M. Characterization of the insulinotropic action of a phospholipase A(2) isolated from Crotalus durissus collilineatus rattlesnake venom on rat pancreatic islets. Toxicon 45 2 (2005) 243-248
    • (2005) Toxicon , vol.45 , Issue.2 , pp. 243-248
    • Nogueira, T.C.A.1    Ferreira, F.2    Toyama, M.H.3    Spoppiglia, L.F.4    Maragoni, S.5    Boschero, A.C.6    Carneiro, E.M.7
  • 40
    • 1442286390 scopus 로고    scopus 로고
    • A new membrane-attack complex/perforin (MACPF) domain lethal toxin from the nematocyst venom of the Okinawan sea anemone Actineria villosa
    • Oshiro N., Kobayashi C., Iwanaga S., Nozaki M., Namikoshi M., Spring J., and Nagai H. A new membrane-attack complex/perforin (MACPF) domain lethal toxin from the nematocyst venom of the Okinawan sea anemone Actineria villosa. Toxicon 43 2 (2004) 225-228
    • (2004) Toxicon , vol.43 , Issue.2 , pp. 225-228
    • Oshiro, N.1    Kobayashi, C.2    Iwanaga, S.3    Nozaki, M.4    Namikoshi, M.5    Spring, J.6    Nagai, H.7
  • 41
    • 33947673334 scopus 로고    scopus 로고
    • Cell adhesion molecules in chemically-induced renal injury
    • Prozialeck W.C., and Edwards J.R. Cell adhesion molecules in chemically-induced renal injury. Pharmacol. Ther. 114 1 (2007) 74-93
    • (2007) Pharmacol. Ther. , vol.114 , Issue.1 , pp. 74-93
    • Prozialeck, W.C.1    Edwards, J.R.2
  • 42
    • 0034551736 scopus 로고    scopus 로고
    • Secreted phospholipase A(2) induces vascular endothelial cell migration
    • Rizzo M.T., Nguyen E., Aldo-Benson M., and Lambeau G. Secreted phospholipase A(2) induces vascular endothelial cell migration. Blood 96 (2000) 3809-3815
    • (2000) Blood , vol.96 , pp. 3809-3815
    • Rizzo, M.T.1    Nguyen, E.2    Aldo-Benson, M.3    Lambeau, G.4
  • 43
    • 1142309648 scopus 로고    scopus 로고
    • The complement system is involved in acute inflammation but not in the hemorrhage produced by a Bothrops atrox snake venom low molecular mass proteinase
    • Rodrigues F.G., PetretskiI J.H., Kanashiro M.M., Lemos L., da Silva W.D., and Kipnis T.L. The complement system is involved in acute inflammation but not in the hemorrhage produced by a Bothrops atrox snake venom low molecular mass proteinase. Mol. Immunol. 40 16 (2004) 1149-1156
    • (2004) Mol. Immunol. , vol.40 , Issue.16 , pp. 1149-1156
    • Rodrigues, F.G.1    PetretskiI, J.H.2    Kanashiro, M.M.3    Lemos, L.4    da Silva, W.D.5    Kipnis, T.L.6
  • 44
    • 0022521821 scopus 로고
    • 2 purified from the venom of the Mexican beaded lizard (Heloderma horridum horridum Wiegmann)
    • 2 purified from the venom of the Mexican beaded lizard (Heloderma horridum horridum Wiegmann). Biochemistry 25 10 (1986) 2927-2933
    • (1986) Biochemistry , vol.25 , Issue.10 , pp. 2927-2933
    • Sosa, B.P.1    Alagón, A.C.2    Martin, B.M.3    Possani, L.D.4
  • 47
    • 0033953366 scopus 로고    scopus 로고
    • Biochemical characterization of two crotamine isoforms isolated by a single step RP-HPLC from Crotalus durissus terrificus (South American rattlesnake) venom and their action on insulin secretion by pancreatic islets
    • Toyama M.H., Carneiro E.M., Marangoni S., Barbosa R.L., Corso G., and Boschero A.C. Biochemical characterization of two crotamine isoforms isolated by a single step RP-HPLC from Crotalus durissus terrificus (South American rattlesnake) venom and their action on insulin secretion by pancreatic islets. Biochim. Biophys. Acta 1474 (2000) 56-60
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 56-60
    • Toyama, M.H.1    Carneiro, E.M.2    Marangoni, S.3    Barbosa, R.L.4    Corso, G.5    Boschero, A.C.6
  • 50
    • 0023189226 scopus 로고
    • Biotoxicology of sea snake venoms
    • Tu A.T. Biotoxicology of sea snake venoms. Ann. Emerg. Med. 16 (1987) 1023-1028
    • (1987) Ann. Emerg. Med. , vol.16 , pp. 1023-1028
    • Tu, A.T.1
  • 52
    • 0033732562 scopus 로고    scopus 로고
    • What can venom phospholipases A(2) tell us about the functional diversity of mammalian secreted phospholipases A(2)
    • Valentin E., and Lambeau G. What can venom phospholipases A(2) tell us about the functional diversity of mammalian secreted phospholipases A(2). Biochimie 82 9 (2000) 815-831
    • (2000) Biochimie , vol.82 , Issue.9 , pp. 815-831
    • Valentin, E.1    Lambeau, G.2
  • 53
    • 0034677892 scopus 로고    scopus 로고
    • Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme
    • Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., and Lambeau G. Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J. Biol. Chem. 17, 275 11 (2000) 7492-7496
    • (2000) J. Biol. Chem. , vol.17-275 , Issue.11 , pp. 7492-7496
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 54
    • 13044277568 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of piratoxin III, a D-49 phospholipase A(2) from the venom of Bothrops pirajai
    • Wen-Hwa L., Toyama M.H., Soares A.M., Giglio J.R., Marangoni S., and Polikarpov I. Crystallization and preliminary X-ray diffraction studies of piratoxin III, a D-49 phospholipase A(2) from the venom of Bothrops pirajai. Acta Crystallogr. 55 (1999) 1229-1230
    • (1999) Acta Crystallogr. , vol.55 , pp. 1229-1230
    • Wen-Hwa, L.1    Toyama, M.H.2    Soares, A.M.3    Giglio, J.R.4    Marangoni, S.5    Polikarpov, I.6
  • 55
    • 77049229047 scopus 로고
    • The renal clearance of alkali-stable inulin
    • Walser M., Davidson D.G., and Orloff J. The renal clearance of alkali-stable inulin. J. Clin. Invest. 34 (1955) 1520-1523
    • (1955) J. Clin. Invest. , vol.34 , pp. 1520-1523
    • Walser, M.1    Davidson, D.G.2    Orloff, J.3
  • 56
    • 0036379701 scopus 로고    scopus 로고
    • Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase
    • Yamamoto C., Tsuru D., Oda Ueda N., Ohno M., Hattori S., and Kim S.T. Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase. Immunology 107 1 (2002) 111-117
    • (2002) Immunology , vol.107 , Issue.1 , pp. 111-117
    • Yamamoto, C.1    Tsuru, D.2    Oda Ueda, N.3    Ohno, M.4    Hattori, S.5    Kim, S.T.6


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