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Volumn 52, Issue 3, 2008, Pages 428-439

Secretory phospholipases A2 isolated from Bothrops asper and from Crotalus durissus terrificus snake venoms induce distinct mechanisms for biosynthesis of prostaglandins E2 and D2 and expression of cyclooxygenases

Author keywords

Arachidonic acid; cPLA2; Crotoxin B; Cyclooxygenases; iPLA2; Macrophages; Prostaglandins; Venom phospholipase A2

Indexed keywords

ARACHIDONIC ACID; ARACHIDONYL TRIFLUOROMETHYL KETONE; CROTOXIN; CROTOXIN B; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ENZYME INHIBITOR; MYOTOXIN 3; PHOSPHOLIPASE A2; PROSTAGLANDIN D2; PROSTAGLANDIN E2; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 50549090862     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2008.06.012     Document Type: Article
Times cited : (38)

References (75)
  • 1
    • 0028122237 scopus 로고
    • Fatty acids in erythrocytes measured by isocratic HPLC
    • Abushufa R., Reed P., and Weinkove C. Fatty acids in erythrocytes measured by isocratic HPLC. Clin. Chem. 40 (1994) 1707-1712
    • (1994) Clin. Chem. , vol.40 , pp. 1707-1712
    • Abushufa, R.1    Reed, P.2    Weinkove, C.3
  • 3
    • 0035839557 scopus 로고    scopus 로고
    • Functional coupling between secretory and cytosolic phospholipase A(2) modulates tumor necrosis factor-alpha-and interleukin-1 beta-induced NF-kappa B activation
    • Anthonsen M.W., Solhaug A., and Johansen B. Functional coupling between secretory and cytosolic phospholipase A(2) modulates tumor necrosis factor-alpha-and interleukin-1 beta-induced NF-kappa B activation. J. Biol. Chem. 276 (2001) 30527-30536
    • (2001) J. Biol. Chem. , vol.276 , pp. 30527-30536
    • Anthonsen, M.W.1    Solhaug, A.2    Johansen, B.3
  • 5
    • 0027485552 scopus 로고
    • Antisense inhibition of group II phospholipase A2 expression blocks the production of prostaglandin E2 by P388D1 cells
    • Barbour S.E., and Dennis E.A. Antisense inhibition of group II phospholipase A2 expression blocks the production of prostaglandin E2 by P388D1 cells. J. Biol. Chem. 268 (1993) 21875-21882
    • (1993) J. Biol. Chem. , vol.268 , pp. 21875-21882
    • Barbour, S.E.1    Dennis, E.A.2
  • 6
    • 4644248139 scopus 로고    scopus 로고
    • Phospholipase A2 and remodeling in inflammatory cells
    • Fonteh A.N., and Wykle R.L. (Eds), Birkhäuser, Switzerland
    • Barbour S.E., Al-Darmaki S., and Manguikian A.D. Phospholipase A2 and remodeling in inflammatory cells. In: Fonteh A.N., and Wykle R.L. (Eds). Arachidonate Remodeling and Inflammation (2004), Birkhäuser, Switzerland 13-36
    • (2004) Arachidonate Remodeling and Inflammation , pp. 13-36
    • Barbour, S.E.1    Al-Darmaki, S.2    Manguikian, A.D.3
  • 7
    • 0033611544 scopus 로고    scopus 로고
    • TpL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105
    • Belich M.P., Salmeron A., Johnston L.H., and Ley S.C. TpL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105. Nature 397 (1999) 363-368
    • (1999) Nature , vol.397 , pp. 363-368
    • Belich, M.P.1    Salmeron, A.2    Johnston, L.H.3    Ley, S.C.4
  • 8
    • 0034284215 scopus 로고    scopus 로고
    • Type IIA secretory phospholipase A2 up-regulates cyclooxygenase-2 and amplifies cytokine-mediated prostaglandin production in human rheumatoid synoviocytes
    • Bidgood M.J., Jamal O.S., Cunningham A.M., Brooks P.M., and Scott K.F. Type IIA secretory phospholipase A2 up-regulates cyclooxygenase-2 and amplifies cytokine-mediated prostaglandin production in human rheumatoid synoviocytes. J. Immunol. 165 (2000) 2790-2797
    • (2000) J. Immunol. , vol.165 , pp. 2790-2797
    • Bidgood, M.J.1    Jamal, O.S.2    Cunningham, A.M.3    Brooks, P.M.4    Scott, K.F.5
  • 11
    • 0030047930 scopus 로고    scopus 로고
    • Functional and molecular aspects of renal prostaglandin receptors
    • Breyer M.D., Jacobson H.R., and Breyer R.M. Functional and molecular aspects of renal prostaglandin receptors. J. Am. Soc. Nephrol. 7 (1996) 8-17
    • (1996) J. Am. Soc. Nephrol. , vol.7 , pp. 8-17
    • Breyer, M.D.1    Jacobson, H.R.2    Breyer, R.M.3
  • 14
    • 0037408174 scopus 로고    scopus 로고
    • Hyperalgesia induced by Asp49 and Lys49 phospholipases A2 from Bothrops asper snake venom: pharmacological mediation and molecular determinants
    • Chacur M., Longo I., Picolo G., Gutiérrez J.M., Lomonte B., Guerra J.L., Teixeira C.F., and Cury Y. Hyperalgesia induced by Asp49 and Lys49 phospholipases A2 from Bothrops asper snake venom: pharmacological mediation and molecular determinants. Toxicon 41 (2003) 667-678
    • (2003) Toxicon , vol.41 , pp. 667-678
    • Chacur, M.1    Longo, I.2    Picolo, G.3    Gutiérrez, J.M.4    Lomonte, B.5    Guerra, J.L.6    Teixeira, C.F.7    Cury, Y.8
  • 15
    • 0038399752 scopus 로고    scopus 로고
    • 2 isoforms: a perspectiva
    • 2 isoforms: a perspectiva. Cell Signal 15 (2003) 637-665
    • (2003) Cell Signal , vol.15 , pp. 637-665
    • Chakraborti, S.1
  • 17
    • 85047680629 scopus 로고    scopus 로고
    • A phospholipase A2-related snake venom (from Crotalus durissus terrificus) stimulates neuroendocrine and immune functions: determination of different sites of action
    • Chisari A., Spinedi E., Voirol M.J., Giovambattista A., and Gaillard R.C. A phospholipase A2-related snake venom (from Crotalus durissus terrificus) stimulates neuroendocrine and immune functions: determination of different sites of action. Endocrinology 139 (1998) 617-625
    • (1998) Endocrinology , vol.139 , pp. 617-625
    • Chisari, A.1    Spinedi, E.2    Voirol, M.J.3    Giovambattista, A.4    Gaillard, R.C.5
  • 18
    • 0034013715 scopus 로고    scopus 로고
    • Membrane-perturbing activity of Viperidae myotoxins: an electrostatic surface potential approach to a puzzling problem
    • Falconi M., Desideri A., and Rufini S. Membrane-perturbing activity of Viperidae myotoxins: an electrostatic surface potential approach to a puzzling problem. J. Mol. Recognit. 13 (2000) 14-19
    • (2000) J. Mol. Recognit. , vol.13 , pp. 14-19
    • Falconi, M.1    Desideri, A.2    Rufini, S.3
  • 19
    • 1442301515 scopus 로고    scopus 로고
    • Cyclooxygenase enzymes: regulation and function
    • Fitzpatrick F.A. Cyclooxygenase enzymes: regulation and function. Curr. Pharm. Des. 10 (2004) 577-588
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 577-588
    • Fitzpatrick, F.A.1
  • 20
    • 0030679647 scopus 로고    scopus 로고
    • Tumor necrosis factor-α inversely regulates prostaglandin D2 and prostaglandin E2 production in murine macrophages
    • Fournier T., Fadok V., and Hendon P.M. Tumor necrosis factor-α inversely regulates prostaglandin D2 and prostaglandin E2 production in murine macrophages. J. Biol. Chem. 49 (1997) 31065-31072
    • (1997) J. Biol. Chem. , vol.49 , pp. 31065-31072
    • Fournier, T.1    Fadok, V.2    Hendon, P.M.3
  • 21
    • 0025909387 scopus 로고
    • Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment
    • Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., and Fitzgerald G.A. Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. FASEB J. 5 (1991) 2304-2312
    • (1991) FASEB J. , vol.5 , pp. 2304-2312
    • Funk, C.D.1    Funk, L.B.2    Kennedy, M.E.3    Pong, A.S.4    Fitzgerald, G.A.5
  • 22
    • 0028972997 scopus 로고
    • 2 myotoxins from Bothrops snake venoms
    • 2 myotoxins from Bothrops snake venoms. Toxicon 33 (1995) 1405-1424
    • (1995) Toxicon , vol.33 , pp. 1405-1424
    • Gutiérrez, J.M.1    Lomonte, B.2
  • 23
    • 1042287114 scopus 로고    scopus 로고
    • 2: insights into the mechanisms of local and systemic myotoxicity
    • 2: insights into the mechanisms of local and systemic myotoxicity. Toxicon 42 (2003) 915-931
    • (2003) Toxicon , vol.42 , pp. 915-931
    • Gutiérrez, J.M.1    Ownby, C.L.2
  • 24
    • 38049077979 scopus 로고    scopus 로고
    • Systemic and local myotoxicity induced by snake venom group II phospholipases A2: comparison between crotoxin, crotoxin B and a Lys49 PLA2 homologue
    • Gutiérrez J.M., Ponce-Soto L.A., Maragoni S., and Lomonte B. Systemic and local myotoxicity induced by snake venom group II phospholipases A2: comparison between crotoxin, crotoxin B and a Lys49 PLA2 homologue. Toxicon 51 (2008) 80-92
    • (2008) Toxicon , vol.51 , pp. 80-92
    • Gutiérrez, J.M.1    Ponce-Soto, L.A.2    Maragoni, S.3    Lomonte, B.4
  • 25
    • 0017919089 scopus 로고
    • The crotoxin complex - an example of biochemical and pharmacological protein complementation
    • (mini-review)
    • Habermann E., and Breithaupt H. The crotoxin complex - an example of biochemical and pharmacological protein complementation. Toxicon 16 (1978) 19-30 (mini-review)
    • (1978) Toxicon , vol.16 , pp. 19-30
    • Habermann, E.1    Breithaupt, H.2
  • 26
    • 0141958256 scopus 로고    scopus 로고
    • Prostaglandin D2 inhibits airway dendritic cell migration and function in steady state conditions by selective activation in the D prostanóide receptor 1
    • Hammad H., de Heer H.J., Soullie T., Hoogsteden H.C., Trottein F., and Lambrecht B.N. Prostaglandin D2 inhibits airway dendritic cell migration and function in steady state conditions by selective activation in the D prostanóide receptor 1. J. Immunol. 171 (2003) 3936-3940
    • (2003) J. Immunol. , vol.171 , pp. 3936-3940
    • Hammad, H.1    de Heer, H.J.2    Soullie, T.3    Hoogsteden, H.C.4    Trottein, F.5    Lambrecht, B.N.6
  • 27
    • 0026201181 scopus 로고
    • Augmentation of prostaglandin E2 production by mammalian phospholipase A2 added exogenously
    • Hara S., Kudo I., and Inoue K. Augmentation of prostaglandin E2 production by mammalian phospholipase A2 added exogenously. J. Biochem. 110 (1991) 163-165
    • (1991) J. Biochem. , vol.110 , pp. 163-165
    • Hara, S.1    Kudo, I.2    Inoue, K.3
  • 29
    • 4444262310 scopus 로고    scopus 로고
    • Pharmacology and signaling of prostaglandin receptors: multiple roles in inflammation and immune modulation
    • Hata A.N., and Breyer R.M. Pharmacology and signaling of prostaglandin receptors: multiple roles in inflammation and immune modulation. Pharmacol. Ther. 103 (2004) 147-166
    • (2004) Pharmacol. Ther. , vol.103 , pp. 147-166
    • Hata, A.N.1    Breyer, R.M.2
  • 31
    • 30144441424 scopus 로고    scopus 로고
    • Positioning prostanoids of the D and J series in the immunopathogenic scheme
    • Herlong J.L., and Scott T.R. Positioning prostanoids of the D and J series in the immunopathogenic scheme. Immunol. Lett. 102 (2006) 121-131
    • (2006) Immunol. Lett. , vol.102 , pp. 121-131
    • Herlong, J.L.1    Scott, T.R.2
  • 32
    • 0037059514 scopus 로고    scopus 로고
    • 2 elicits proinflammatory changes and upregulates the surface expression of fas ligand in monocytic cells: potential relevance for atherogenesis
    • 2 elicits proinflammatory changes and upregulates the surface expression of fas ligand in monocytic cells: potential relevance for atherogenesis. Circ. Res. 90 (2002) 38-45
    • (2002) Circ. Res. , vol.90 , pp. 38-45
    • Hernández, M.1    Fuentes, L.2    Fernandez Avilles, F.J.3    Crespo, M.S.4    Nieto, M.L.5
  • 33
    • 33845696273 scopus 로고    scopus 로고
    • BK-induced COX-2 expression via PKC-δ-dependent activation of p42/p44 MAPK and NF-κB in astrocytes
    • Hsieh H.L., Wang H.H., Wu C.Y., Jou M.J., Yen M.H., Parker P., and Yang C.M. BK-induced COX-2 expression via PKC-δ-dependent activation of p42/p44 MAPK and NF-κB in astrocytes. Cell Signal 19 (2007) 330-340
    • (2007) Cell Signal , vol.19 , pp. 330-340
    • Hsieh, H.L.1    Wang, H.H.2    Wu, C.Y.3    Jou, M.J.4    Yen, M.H.5    Parker, P.6    Yang, C.M.7
  • 35
    • 0024203219 scopus 로고
    • Leucocytes in asthma
    • Kay A.B. Leucocytes in asthma. Immunol. Invest. 17 (1988) 679-705
    • (1988) Immunol. Invest. , vol.17 , pp. 679-705
    • Kay, A.B.1
  • 37
    • 0022589884 scopus 로고
    • Muscle necrosis caused by the sub-units of crotoxin
    • Kouyoumdjian J.A., Harris J.B., and Johnson M.A. Muscle necrosis caused by the sub-units of crotoxin. Toxicon 24 (1986) 575-583
    • (1986) Toxicon , vol.24 , pp. 575-583
    • Kouyoumdjian, J.A.1    Harris, J.B.2    Johnson, M.A.3
  • 39
    • 0031594888 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 is required for cytokine-induced expression of type IIA secretory phospholipase A2 that mediates optimal cyclooxygenase-2-dependent delayed prostaglandin E2 generation in rat 3Y1 fibroblasts
    • Kuwata H., Nakatani Y., Murakami M., and Kudo I. Cytosolic phospholipase A2 is required for cytokine-induced expression of type IIA secretory phospholipase A2 that mediates optimal cyclooxygenase-2-dependent delayed prostaglandin E2 generation in rat 3Y1 fibroblasts. J. Biol. Chem. 273 (1998) 1733-1740
    • (1998) J. Biol. Chem. , vol.273 , pp. 1733-1740
    • Kuwata, H.1    Nakatani, Y.2    Murakami, M.3    Kudo, I.4
  • 40
    • 34547106075 scopus 로고    scopus 로고
    • A novel role of group VIB calcium-independent phospholipase A2 (iPLA2γ) in the inducible expression of group IIA secretory PLA2 in rat fibroblastic cells
    • Kuwata H., Fujimoto C., Yoda E., Shimbara S., Nakatani N., Hara S., Murakami M., and Kudo I. A novel role of group VIB calcium-independent phospholipase A2 (iPLA2γ) in the inducible expression of group IIA secretory PLA2 in rat fibroblastic cells. J. Biol. Chem. 282 (2007) 20124-20132
    • (2007) J. Biol. Chem. , vol.282 , pp. 20124-20132
    • Kuwata, H.1    Fujimoto, C.2    Yoda, E.3    Shimbara, S.4    Nakatani, N.5    Hara, S.6    Murakami, M.7    Kudo, I.8
  • 43
    • 0024412266 scopus 로고
    • A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo)
    • Lomonte B., and Gutiérrez J.M. A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo). Toxicon 27 (1989) 725-733
    • (1989) Toxicon , vol.27 , pp. 725-733
    • Lomonte, B.1    Gutiérrez, J.M.2
  • 44
    • 0027534529 scopus 로고
    • Host response to Bothorps asper snake venom. Analysis of oedema formation, inflammatory cells and cytokine release in a mouse model
    • Lomonte B., Tarkaweshi A., and Hanson L.A. Host response to Bothorps asper snake venom. Analysis of oedema formation, inflammatory cells and cytokine release in a mouse model. Inflammation 17 (1993) 93-105
    • (1993) Inflammation , vol.17 , pp. 93-105
    • Lomonte, B.1    Tarkaweshi, A.2    Hanson, L.A.3
  • 49
    • 0031550246 scopus 로고    scopus 로고
    • Concordant induction of prostaglandin E2 synthase with cyclooxygenase-2 leads to preferred production of prostaglandin E2 over thromboxane and prostaglandin D2 in lipopolysaccharide-stimulated rat peritoneal macrophages
    • Matsumoto H., Naraba H., Murakami M., Kudo I., Yamaki K., Ueno A., and Oh-ishi S. Concordant induction of prostaglandin E2 synthase with cyclooxygenase-2 leads to preferred production of prostaglandin E2 over thromboxane and prostaglandin D2 in lipopolysaccharide-stimulated rat peritoneal macrophages. Biochem. Biophys. Res. Commun. 230 (1997) 110-114
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 110-114
    • Matsumoto, H.1    Naraba, H.2    Murakami, M.3    Kudo, I.4    Yamaki, K.5    Ueno, A.6    Oh-ishi, S.7
  • 51
    • 0021739394 scopus 로고
    • The non-eicosanoid functions of the essential fatty acids
    • Mead J.F. The non-eicosanoid functions of the essential fatty acids. J. Lipid. Res. 25 (1984) 1517-1521
    • (1984) J. Lipid. Res. , vol.25 , pp. 1517-1521
    • Mead, J.F.1
  • 52
    • 0023855416 scopus 로고
    • Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)
    • Merlie J.P., Fagan D., Mudd J., and Needleman P. Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase). J. Biol. Chem. 263 (1988) 3550-3553
    • (1988) J. Biol. Chem. , vol.263 , pp. 3550-3553
    • Merlie, J.P.1    Fagan, D.2    Mudd, J.3    Needleman, P.4
  • 56
    • 0037860748 scopus 로고    scopus 로고
    • Perinuclear localization of cytosolic phospholipase A(2)alpha is important but not obligatory for coupling with cyclooxygenases
    • Murakami M., Das S., Young-Jun K., Cho W., and Kudo I. Perinuclear localization of cytosolic phospholipase A(2)alpha is important but not obligatory for coupling with cyclooxygenases. FEBS Lett. 546 (2003) 251-256
    • (2003) FEBS Lett. , vol.546 , pp. 251-256
    • Murakami, M.1    Das, S.2    Young-Jun, K.3    Cho, W.4    Kudo, I.5
  • 59
    • 0027293391 scopus 로고
    • Expression of mRNA for cyclooxygenase-1 and cyclooxygenase-2 in human tissues
    • O'Neill G.P., and Ford-Hutchinson A.W. Expression of mRNA for cyclooxygenase-1 and cyclooxygenase-2 in human tissues. FEBS Lett. 330 (1993) 156-160
    • (1993) FEBS Lett. , vol.330 , pp. 156-160
    • O'Neill, G.P.1    Ford-Hutchinson, A.W.2
  • 61
    • 0027365347 scopus 로고
    • 2 by rat mesanglial cells: its contribution to arachidonic acid release and prostaglandin synthesis by cultured rat glomerular cells
    • 2 by rat mesanglial cells: its contribution to arachidonic acid release and prostaglandin synthesis by cultured rat glomerular cells. J. Clin. Invest. 92 (1993) 2516-2523
    • (1993) J. Clin. Invest. , vol.92 , pp. 2516-2523
    • Pfeilschifter, J.1    Schalkwijk, C.2    Briner, V.A.3    van den Bosch, H.4
  • 62
    • 0022074792 scopus 로고
    • Enzyme immunoassays of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay
    • Pradelles P., Grassi J., and Mac Louf J. Enzyme immunoassays of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay. Anal. Chem. 57 (1985) 1170-1173
    • (1985) Anal. Chem. , vol.57 , pp. 1170-1173
    • Pradelles, P.1    Grassi, J.2    Mac Louf, J.3
  • 63
    • 14244265550 scopus 로고    scopus 로고
    • Immunosuppresive role of principal toxin (crotoxin) of Crotalus durissus terrificus venom
    • Rangel-Santos A., Lima C., Lopes-Ferreira M., and Cardoso D.F. Immunosuppresive role of principal toxin (crotoxin) of Crotalus durissus terrificus venom. Toxicon 44 (2004) 609-616
    • (2004) Toxicon , vol.44 , pp. 609-616
    • Rangel-Santos, A.1    Lima, C.2    Lopes-Ferreira, M.3    Cardoso, D.F.4
  • 65
    • 0034680768 scopus 로고    scopus 로고
    • Human calcium-independent phospholipase A2 mediates lymphocyte proliferation
    • Roshak A.K., Capper E.A., Stevenson C., Eichman C., and Marshall L.A. Human calcium-independent phospholipase A2 mediates lymphocyte proliferation. J. Biol. Chem. 275 (2000) 35692-35698
    • (2000) J. Biol. Chem. , vol.275 , pp. 35692-35698
    • Roshak, A.K.1    Capper, E.A.2    Stevenson, C.3    Eichman, C.4    Marshall, L.A.5
  • 66
    • 15044359151 scopus 로고    scopus 로고
    • Inhibitory effect of phospholipase A(2) isolated from Crotalus durissus terrificus venom on macrophage function
    • Sampaio S.C., Rangel-Santos A.C., Peres C.M., Curi R., and Cury Y. Inhibitory effect of phospholipase A(2) isolated from Crotalus durissus terrificus venom on macrophage function. Toxicon 45 (2005) 671-676
    • (2005) Toxicon , vol.45 , pp. 671-676
    • Sampaio, S.C.1    Rangel-Santos, A.C.2    Peres, C.M.3    Curi, R.4    Cury, Y.5
  • 67
    • 33644512439 scopus 로고    scopus 로고
    • Lipoxygenase-derived eicosanoids are involved in the inhibitory effect of Crotalus durissus terrificus venom or crotoxin on rat macrophage pahgocytosis
    • Sampaio S.C., Alba-Loureiro T.C., Brigatte P., Landgraf R.G., dos Santos E.C., Curi R., and Cury Y. Lipoxygenase-derived eicosanoids are involved in the inhibitory effect of Crotalus durissus terrificus venom or crotoxin on rat macrophage pahgocytosis. Toxicon 47 (2006) 313-321
    • (2006) Toxicon , vol.47 , pp. 313-321
    • Sampaio, S.C.1    Alba-Loureiro, T.C.2    Brigatte, P.3    Landgraf, R.G.4    dos Santos, E.C.5    Curi, R.6    Cury, Y.7
  • 68
    • 17344384790 scopus 로고    scopus 로고
    • A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogênica activities
    • Soares A.M., Rodrigues V.M., Homsi-Brandeburgo M.I., Toyama M.H., Lombardi F.R., Arni R.K., and Giglio J.R. A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogênica activities. Toxicon 36 (1998) 503-514
    • (1998) Toxicon , vol.36 , pp. 503-514
    • Soares, A.M.1    Rodrigues, V.M.2    Homsi-Brandeburgo, M.I.3    Toyama, M.H.4    Lombardi, F.R.5    Arni, R.K.6    Giglio, J.R.7
  • 69
    • 0034918136 scopus 로고    scopus 로고
    • Effects of chemical modifications of crotoxin B, the phospholipase A(2) subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities
    • Soares A.M., Mancin A.C., Cecchini A.L., Arantes E.C., França S.C., Gutiérrez J.M., and Giglio J.R. Effects of chemical modifications of crotoxin B, the phospholipase A(2) subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities. Int. J. Biochem. Cell Biol. 33 (2001) 877-888
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 877-888
    • Soares, A.M.1    Mancin, A.C.2    Cecchini, A.L.3    Arantes, E.C.4    França, S.C.5    Gutiérrez, J.M.6    Giglio, J.R.7
  • 71
    • 0032211140 scopus 로고    scopus 로고
    • 2 in nerve growth factor-stimulated rat serosal mast cells is facilitated by independent of their enzymatic functions
    • 2 in nerve growth factor-stimulated rat serosal mast cells is facilitated by independent of their enzymatic functions. J. Immunol. 161 (1998) 5008-5015
    • (1998) J. Immunol. , vol.161 , pp. 5008-5015
    • Tada, K.1    Murakami, M.2    Kambe, T.3    Kudo, I.4
  • 73
    • 0035860823 scopus 로고    scopus 로고
    • Coupling between cyclooxygenase, terminal prostanoid synthase, and phospholipase A2
    • Ueno N., Murakami M., Tanioka T., Fujimori K., Tanabe T., Urade Y., and Kudo I. Coupling between cyclooxygenase, terminal prostanoid synthase, and phospholipase A2. J. Biol. Chem. 276 (2001) 34918-34927
    • (2001) J. Biol. Chem. , vol.276 , pp. 34918-34927
    • Ueno, N.1    Murakami, M.2    Tanioka, T.3    Fujimori, K.4    Tanabe, T.5    Urade, Y.6    Kudo, I.7


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