메뉴 건너뛰기




Volumn 17, Issue 4, 2011, Pages 430-441

Effect of Bothrops alternatus snake venom on macrophage phagocytosis and superoxide production: Participation of protein kinase C

Author keywords

Bothrops; Inflammation; Macrophages; Phagocytosis; Protein kinase C; Snake venom; Superoxide

Indexed keywords

COMPLEMENT RECEPTOR; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; SNAKE VENOM; SUPEROXIDE; THIOGLYCOLIC ACID; ZYMOSAN;

EID: 83255185635     PISSN: 16789180     EISSN: 16789199     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (80)
  • 1
    • 73649105717 scopus 로고    scopus 로고
    • Epidemiologia dos acidentes por animais peçonhentos
    • In: Cardoso JL, Haddad-Jr V, França FOS, Wen FH, Malaque CMS, editors, 2nd ed. São Paulo: Sarvier
    • Oliveira RC, Wen FH, Sifuentes DN. Epidemiologia dos acidentes por animais peçonhentos. In: Cardoso JL, Haddad-Jr V, França FOS, Wen FH, Malaque CMS, editors. Animais peçonhentos do Brasil: biologia, clínica e terapêutica. 2nd ed. São Paulo: Sarvier; 2009. p. 6-21.
    • (2009) Animais Peçonhentos Do Brasil: Biologia, Clínica E Terapêutica , pp. 6-21
    • Oliveira, R.C.1    Wen, F.H.2    Sifuentes, D.N.3
  • 4
    • 0025307909 scopus 로고
    • Acidentes por serpentes do gênero Crotalus
    • Barraviera B. Acidentes por serpentes do gênero Crotalus. Arq Bras Med. 1990;64:14-20.
    • (1990) Arq Bras Med , vol.64 , pp. 14-20
    • Barraviera, B.1
  • 5
    • 3142546284 scopus 로고
    • Estudo clínico dos acidentes ofídicos
    • Barraviera B. Estudo clínico dos acidentes ofídicos. J Bras Med. 1993;65(4):209-50.
    • (1993) J Bras Med , vol.65 , Issue.4 , pp. 209-250
    • Barraviera, B.1
  • 7
    • 68149178423 scopus 로고    scopus 로고
    • Morphological and molecular evidence for phylogeny and classification of South American pitvipers, genera Bothrops, Bothriopsis, and Bothrocophias (Serpentes: Viperidae)
    • Fenwick AM, Gutberlet RL Jr, Evans JA, Christopher LP. Morphological and molecular evidence for phylogeny and classification of South American pitvipers, genera Bothrops, Bothriopsis, and Bothrocophias (Serpentes: Viperidae). Zool J Linn Soc. 2009;156(3):617-40.
    • (2009) Zool J Linn Soc , vol.156 , Issue.3 , pp. 617-640
    • Fenwick, A.M.1    Gutberlet Jr, R.L.2    Evans, J.A.3    Christopher, L.P.4
  • 8
    • 0001495821 scopus 로고
    • Symptomatology, pathology and treatment of snakes bites in South America
    • Burchel, W, Buckley, EE, editors, New York: Academic Press
    • Rosenfeld G. Symptomatology, pathology and treatment of snakes bites in South America. In: Burchel, W, Buckley, EE, editors. Venomous animals and their venoms. New York: Academic Press; 1971. p. 345-403.
    • (1971) Venomous Animals and Their Venoms , pp. 345-403
    • Rosenfeld, G.1
  • 9
    • 0026085650 scopus 로고
    • Comparative study of nine Bothrops snake venoms from adult female snakes and their offspring
    • Furtado MF, Maruyama M, Kamiguti AS, Antonio LC. Comparative study of nine Bothrops snake venoms from adult female snakes and their offspring. Toxicon. 1991;29(2):219-26.
    • (1991) Toxicon , vol.29 , Issue.2 , pp. 219-226
    • Furtado, M.F.1    Maruyama, M.2    Kamiguti, A.S.3    Antonio, L.C.4
  • 11
    • 0000857506 scopus 로고
    • A comparative study of enzyme activities in snake venoms
    • Mebs D. A comparative study of enzyme activities in snake venoms. Int J Biochem. 1970;1(3):335-42.
    • (1970) Int J Biochem , vol.1 , Issue.3 , pp. 335-342
    • Mebs, D.1
  • 12
    • 0026042486 scopus 로고
    • A comparative study of the biological properties of some venoms of snacks of the genus Bothrops (American lance-headed viper)
    • Tan NH, Ponnudurai G. A comparative study of the biological properties of some venoms of snacks of the genus Bothrops (American lance-headed viper). Comp Biochem Physiol. 1991;100(2):361-5.
    • (1991) Comp Biochem Physiol , vol.100 , Issue.2 , pp. 361-365
    • Tan, N.H.1    Ponnudurai, G.2
  • 13
    • 18244428621 scopus 로고    scopus 로고
    • Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Brothops alternatus snake venom
    • Stábeli RG, Marcussi S, Carlos GB, Pietro RC, Selistre-de-Araújo HS, Giglio JR, et al. Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Brothops alternatus snake venom. Bioorg Med Chem. 2004;12(11):2881-6.
    • (2004) Bioorg Med Chem , vol.12 , Issue.11 , pp. 2881-2886
    • Stábeli, R.G.1    Marcussi, S.2    Carlos, G.B.3    Pietro, R.C.4    Selistre-de-Araújo, H.S.5    Giglio, J.R.6
  • 14
    • 0022556252 scopus 로고
    • Phospholipase A2 from Bothrops alternatus (víbora de la cruz) venom. Purification and some characteristic properties
    • Nisenbom HE, Seki C, Vidal JC. Phospholipase A2 from Bothrops alternatus (víbora de la cruz) venom. Purification and some characteristic properties. Toxicon. 1986;24(3):259-72.
    • (1986) Toxicon , vol.24 , Issue.3 , pp. 259-272
    • Nisenbom, H.E.1    Seki, C.2    Vidal, J.C.3
  • 15
    • 0032125141 scopus 로고    scopus 로고
    • Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus
    • Smolka MB, Marangoni S, Oliveira B, Novello JC. Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus. Toxicon. 1998;36(7):1059-63.
    • (1998) Toxicon , vol.36 , Issue.7 , pp. 1059-1063
    • Smolka, M.B.1    Marangoni, S.2    Oliveira, B.3    Novello, J.C.4
  • 16
    • 0032400791 scopus 로고    scopus 로고
    • Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus
    • Castro HC, Dutra DL, Oliveira-Carvalho AL, Zingali RB. Bothroalternin, a thrombin inhibitor from the venom of Bothrops alternatus. Toxicon. 1998;36(12):1903-12.
    • (1998) Toxicon , vol.36 , Issue.12 , pp. 1903-1912
    • Castro, H.C.1    Dutra, D.L.2    Oliveira-Carvalho, A.L.3    Zingali, R.B.4
  • 17
    • 0034671998 scopus 로고    scopus 로고
    • The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha2beta1 integrin-mediated cell adhesion
    • Souza DH, Iemma MR, Ferreira LL, Faria JP, Oliva ML, Zingali RB, et AL. The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits alpha2beta1 integrin-mediated cell adhesion. Arch Biochem Biophys. 2000;384(2):341-50.
    • (2000) Arch Biochem Biophys , vol.384 , Issue.2 , pp. 341-350
    • Souza, D.H.1    Iemma, M.R.2    Ferreira, L.L.3    Faria, J.P.4    Oliva, M.L.5    Zingali, R.B.6
  • 19
    • 0043171125 scopus 로고    scopus 로고
    • BaG, a new dimeric metalloproteinase/disintegrin from the Bothrops alternatus snake venom, that interacts with alpha5beta1 integrin
    • Cominetti MR, Ribeiro JU, Fox JW, Selistre-de-Araujo, HS. BaG, a new dimeric metalloproteinase/disintegrin from the Bothrops alternatus snake venom, that interacts with alpha5beta1 integrin. Arch Biochem Biophys. 2003;416(2):171-9.
    • (2003) Arch Biochem Biophys , vol.416 , Issue.2 , pp. 171-179
    • Cominetti, M.R.1    Ribeiro, J.U.2    Fox, J.W.3    Selistre-de-Araujo, H.S.4
  • 20
    • 2442498537 scopus 로고    scopus 로고
    • Alternagin-C, a disintegrin like protein, induces vascular endothelial cell growth factor (VEGF) expression and endothelial cell proliferation in vitro
    • Cominetti MR, Terrugi CHB, Ramos OHP, Fox JW, Figueiredo CC, Mariano-Oliveira A, et al. Alternagin-C, a disintegrin like protein, induces vascular endothelial cell growth factor (VEGF) expression and endothelial cell proliferation in vitro. J Biol Chem. 2004;279(18):18247-55.
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 18247-18255
    • Cominetti, M.R.1    Terrugi, C.H.B.2    Ramos, O.H.P.3    Fox, J.W.4    Figueiredo, C.C.5    Mariano-Oliveira, A.6
  • 21
    • 24344481759 scopus 로고    scopus 로고
    • Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom
    • Gay CC, Leiva IC, Maruñak S, Teibler P, Acosta de Pérez O. Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom. Toxicon. 2005;46(5):546-54.
    • (2005) Toxicon , vol.46 , Issue.5 , pp. 546-554
    • Gay, C.C.1    Leiva, I.C.2    Maruñak, S.3    Teibler, P.4    Acosta de Pérez, O.5
  • 22
    • 26644458809 scopus 로고    scopus 로고
    • Alternagin-C, a disintegrin-like protein from the venom of Bothrops alternatus, modulates alpha2beta1 integrin-mediated cell adhesion, migration and proliferation
    • Selistre-de-Araújo HS, Cominetti MR, Terruggi CH, Mariano-Oliveira A, De Freitas MS, Crepin M, et al. Alternagin-C, a disintegrin-like protein from the venom of Bothrops alternatus, modulates alpha2beta1 integrin-mediated cell adhesion, migration and proliferation. Braz J Med Biol Res. 2005;38(10):1505-11.
    • (2005) Braz J Med Biol Res , vol.38 , Issue.10 , pp. 1505-1511
    • Selistre-de-Araújo, H.S.1    Cominetti, M.R.2    Terruggi, C.H.3    Mariano-Oliveira, A.4    de Freitas, M.S.5    Crepin, M.6
  • 23
    • 52649171365 scopus 로고    scopus 로고
    • Purification and characterization of a phosphodiesterase from Bothrops alternatus snake venom
    • Valério AA, Corradini AC, Panunto PC, Mello SM, Hyslop S. Purification and characterization of a phosphodiesterase from Bothrops alternatus snake venom. J Protein Chem. 2002;21(8):495-503.
    • (2002) J Protein Chem , vol.21 , Issue.8 , pp. 495-503
    • Valério, A.A.1    Corradini, A.C.2    Panunto, P.C.3    Mello, S.M.4    Hyslop, S.5
  • 24
    • 0028019098 scopus 로고
    • Clinical and epidemiological aspects of the 'urutu' lance-headed viper (Bothrops alternatus) bite in a Brazilian hospital
    • Bauab FA, Junqueira GR, Corradini MC, Silveira PV, Nishioka S de A. Clinical and epidemiological aspects of the 'urutu' lance-headed viper (Bothrops alternatus) bite in a Brazilian hospital. Trop Med Parasitol. 1994;45(3):243-5.
    • (1994) Trop Med Parasitol , vol.45 , Issue.3 , pp. 243-245
    • Bauab, F.A.1    Junqueira, G.R.2    Corradini, M.C.3    Silveira, P.V.4    de Nishioka, S.A.5
  • 25
    • 0033288010 scopus 로고    scopus 로고
    • Hemorrhagic, edema-forming, proteolytic and myonecrotic activities of viper venoms of Bothrops alternatus (Vibora de la Cruz)
    • Maruñak SL, Acosta De Pérez O, Ruíz De Torrent RM, Teibler GP. Hemorrhagic, edema-forming, proteolytic and myonecrotic activities of viper venoms of Bothrops alternatus (Vibora de la Cruz). Acta Physiol Pharmacol Ther Latinoam. 1999;49(3):149-54.
    • (1999) Acta Physiol Pharmacol Ther Latinoam , vol.49 , Issue.3 , pp. 149-154
    • Maruñak, S.L.1    Acosta de Pérez, O.2    Ruíz de Torrent, R.M.3    Teibler, G.P.4
  • 26
    • 0033979438 scopus 로고    scopus 로고
    • A comparison of different methods to assess the hemorrhagic activity of Bothrops venoms
    • de Roodt AR, Dolab JA, Dokmetjian JC, Litwin S, Segre L, Vidal JCA. A comparison of different methods to assess the hemorrhagic activity of Bothrops venoms. Toxicon. 2000;38(6):865-73.
    • (2000) Toxicon , vol.38 , Issue.6 , pp. 865-873
    • de Roodt, A.R.1    Dolab, J.A.2    Dokmetjian, J.C.3    Litwin, S.4    Segre, L.5    Vidal, J.C.A.6
  • 27
    • 0021217885 scopus 로고
    • Muscle necrosis regeneration after envenomation by Bothrops jararacussu snake venom
    • Queiroz LS, Santo-Neto H, Rodrigues-Simioni L, Prado-Franceschi J. Muscle necrosis regeneration after envenomation by Bothrops jararacussu snake venom. Toxicon. 1984;22(3):339-46.
    • (1984) Toxicon , vol.22 , Issue.3 , pp. 339-346
    • Queiroz, L.S.1    Santo-Neto, H.2    Rodrigues-Simioni, L.3    Prado-Franceschi, J.4
  • 29
    • 0021134680 scopus 로고
    • Skeletal muscle regeneration after myonecrosis induced by crude venom and a myotoxin from the snake Bothrops asper (Fer-de-Lance)
    • Gutiérrez JM, Ownby CL, Odell GV. Skeletal muscle regeneration after myonecrosis induced by crude venom and a myotoxin from the snake Bothrops asper (Fer-de-Lance). Toxicon. 1984;22(5):719-31
    • (1984) Toxicon , vol.22 , Issue.5 , pp. 719-731
    • Gutiérrez, J.M.1    Ownby, C.L.2    Odell, G.V.3
  • 30
    • 0022804888 scopus 로고
    • Inflammatory infiltrate in skeletal muscle injected with Bothrops asper venom
    • Gutiérrez JM, Chaves F, Cerdas L. Inflammatory infiltrate in skeletal muscle injected with Bothrops asper venom. Rev Biol Trop. 1986;34(2):209-19.
    • (1986) Rev Biol Trop , vol.34 , Issue.2 , pp. 209-219
    • Gutiérrez, J.M.1    Chaves, F.2    Cerdas, L.3
  • 31
    • 0024504960 scopus 로고
    • Pharmacological evaluation of rat paw oedema induced by Bothrops jararaca venom
    • Trebien HA, Calixto JB. Pharmacological evaluation of rat paw oedema induced by Bothrops jararaca venom. Agents Actions.1989;26(3-4):292-300.
    • (1989) Agents Actions , vol.26 , Issue.3-4 , pp. 292-300
    • Trebien, H.A.1    Calixto, J.B.2
  • 32
    • 0027715949 scopus 로고
    • Lypoxygenase-derived mediators may be involved in in vivo neutrophil migration induced by Bothrops erythromelas and Bothrops alternatus venom
    • Flores CA, Zappellini A, Prado-Franceschi J. Lypoxygenase-derived mediators may be involved in in vivo neutrophil migration induced by Bothrops erythromelas and Bothrops alternatus venom. Toxicon. 1993;31(12):1551-9.
    • (1993) Toxicon , vol.31 , Issue.12 , pp. 1551-1559
    • Flores, C.A.1    Zappellini, A.2    Prado-Franceschi, J.3
  • 33
    • 0034894386 scopus 로고    scopus 로고
    • Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo
    • Zamuner SR, Gutiérrez JM, Muscará MN, Teixeira SA, Teixeira CF. Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo. Toxicon.2001;39(10):1505-13.
    • (2001) Toxicon , vol.39 , Issue.10 , pp. 1505-1513
    • Zamuner, S.R.1    Gutiérrez, J.M.2    Muscará, M.N.3    Teixeira, S.A.4    Teixeira, C.F.5
  • 35
    • 0031081512 scopus 로고    scopus 로고
    • Leukocyte response induced by Bothrops jararaca crude venom. In vivo and in vitro studies
    • Farsky SH, Walber J, Costa-Cruz JW, Cury Y, Teixeira CF. Leukocyte response induced by Bothrops jararaca crude venom. In vivo and in vitro studies. Toxicon. 1997;35(2):185-93.
    • (1997) Toxicon , vol.35 , Issue.2 , pp. 185-193
    • Farsky, S.H.1    Walber, J.2    Costa-Cruz, J.W.3    Cury, Y.4    Teixeira, C.F.5
  • 36
    • 0027752746 scopus 로고
    • Macrophage heterogeneity in development and differentiation
    • Naito M. Macrophage heterogeneity in development and differentiation. Arch Histol Cytol. 1993;56(4):331-51.
    • (1993) Arch Histol Cytol , vol.56 , Issue.4 , pp. 331-351
    • Naito, M.1
  • 37
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • Aderem A, Underhill DM. Mechanisms of phagocytosis in macrophages. Annu Rev Immunol. 1999;17:593-23.
    • (1999) Annu Rev Immunol , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 38
    • 0035817818 scopus 로고    scopus 로고
    • Immune recognition. A new receptor for beta-glucans
    • Brown GD, Gordon S. Immune recognition. A new receptor for beta-glucans. Nature. 2001; 413: 36-7.
    • (2001) Nature , vol.413 , pp. 36-37
    • Brown, G.D.1    Gordon, S.2
  • 39
    • 0037605881 scopus 로고    scopus 로고
    • Phospholipase A2 (PLA2) enzymes in membrane trafficking: Mediators of membrane shape and function
    • Brown WJ, Chambers K, Doody A. Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function. Traffic. 2003;4(4):214-21.
    • (2003) Traffic , vol.4 , Issue.4 , pp. 214-221
    • Brown, W.J.1    Chambers, K.2    Doody, A.3
  • 40
    • 0346787827 scopus 로고    scopus 로고
    • Dectin-1 and its role in the recognition of beta-glucans by macrophages
    • Herre J, Gordon S, Brown GD. Dectin-1 and its role in the recognition of beta-glucans by macrophages. Mol Immunol. 2004;40(12):869-76.
    • (2004) Mol Immunol , vol.40 , Issue.12 , pp. 869-876
    • Herre, J.1    Gordon, S.2    Brown, G.D.3
  • 42
    • 0019971133 scopus 로고
    • Tumor-promoting phorbol esters stimulate C3b and C3b' receptor-mediated phagocytosis in cultured human monocytes
    • Wright SD, Silverstein SC. Tumor-promoting phorbol esters stimulate C3b and C3b' receptor-mediated phagocytosis in cultured human monocytes. J Exp Med. 1982;156(4):1149-64.
    • (1982) J Exp Med , vol.156 , Issue.4 , pp. 1149-1164
    • Wright, S.D.1    Silverstein, S.C.2
  • 43
    • 0022243367 scopus 로고
    • Effects of differentiation in vivo and of lymphokine treatment in vitro on the mobility of C3 receptors of human and mouse mononuclear phagocytes
    • Griffin FM Jr, Mullinax PJ. Effects of differentiation in vivo and of lymphokine treatment in vitro on the mobility of C3 receptors of human and mouse mononuclear phagocytes. J Immunol. 1985;135(5):3394-7.
    • (1985) J Immunol , vol.135 , Issue.5 , pp. 3394-3397
    • Griffin Jr, F.M.1    Mullinax, P.J.2
  • 44
    • 0027160034 scopus 로고
    • CR3 (CD11b, CD18): A phagocyte and NK cell membrane receptor with multiple ligand specificities and functions
    • Ross GD, Vetvicka V. CR3 (CD11b, CD18): a phagocyte and NK cell membrane receptor with multiple ligand specificities and functions. Clin Exp Immunol. 1993;92(2):181-4.
    • (1993) Clin Exp Immunol , vol.92 , Issue.2 , pp. 181-184
    • Ross, G.D.1    Vetvicka, V.2
  • 45
    • 0033066881 scopus 로고    scopus 로고
    • Integrin-mediated signaling in human neutrophil functioning
    • Williams MA, Solomkin JS. Integrin-mediated signaling in human neutrophil functioning. J Leukoc Biol. 1999;65(6):725-36.
    • (1999) J Leukoc Biol , vol.65 , Issue.6 , pp. 725-736
    • Williams, M.A.1    Solomkin, J.S.2
  • 46
    • 0035159327 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced activation of beta2-integrin function in macrophages requires Irak kinase activity, p38 mitogen-activated protein kinase, and the Rap1 GTPase
    • Schmidt A, Caron E, Hall A. Lipopolysaccharide-induced activation of beta2-integrin function in macrophages requires Irak kinase activity, p38 mitogen-activated protein kinase, and the Rap1 GTPase. Mol Cell Biol. 2001;21(2):438-48.
    • (2001) Mol Cell Biol , vol.21 , Issue.2 , pp. 438-448
    • Schmidt, A.1    Caron, E.2    Hall, A.3
  • 47
    • 0037329747 scopus 로고    scopus 로고
    • Cellular functions of the Rap 1 GTP-binding protein: A pattern emerges
    • Pt 3
    • Caron E. Cellular functions of the Rap 1 GTP-binding protein: a pattern emerges. J Cell Sci. 2003;116(Pt 3)435-40.
    • (2003) J Cell Sci , vol.116 , pp. 435-440
    • Caron, E.1
  • 49
    • 0021984750 scopus 로고
    • Activation of phagocytic cells' C3 receptors for phagocytosis
    • Wright SD, Griffin FM Jr. Activation of phagocytic cells' C3 receptors for phagocytosis. J Leukoc Biol. 1985;38(2):327-39.
    • (1985) J Leukoc Biol , vol.38 , Issue.2 , pp. 327-339
    • Wright, S.D.1    Griffin Jr, F.M.2
  • 50
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • Van Kooyk Y, Figdor CG. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol. 2000;12(5):542-7.
    • (2000) Curr Opin Cell Biol , vol.12 , Issue.5 , pp. 542-547
    • van Kooyk, Y.1    Figdor, C.G.2
  • 51
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior BM. NADPH oxidase: an update. Blood. 1999;93(4):1464-76.
    • (1999) Blood , vol.93 , Issue.4 , pp. 1464-1476
    • Babior, B.M.1
  • 54
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • 12 Pt 2
    • Forman HJ, Torres M. Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling. Am J Respir Crit Care Med. 2002;166(12 Pt 2):S4-8.
    • (2002) Am J Respir Crit Care Med , vol.166
    • Forman, H.J.1    Torres, M.2
  • 55
    • 24344440254 scopus 로고    scopus 로고
    • Activation of cellular functions in macrophages by venom secretory Asp-49 and Lys-49 Phospholipases A2
    • Zuliani JP, Gutiérrez JM, Casais e Silva LL, Sampaio SC, Teixeira CFP. Activation of cellular functions in macrophages by venom secretory Asp-49 and Lys-49 Phospholipases A2. Toxicon. 2005;46(3):523-32.
    • (2005) Toxicon , vol.46 , Issue.3 , pp. 523-532
    • Zuliani, J.P.1    Gutiérrez, J.M.2    Casais e Silva, L.L.3    Sampaio, S.C.4    Teixeira, C.F.P.5
  • 56
    • 0023515528 scopus 로고
    • Monoclonal antibody to the murine type 3 complement receptor inhibits adhesion of myelomonocytic cells in vitro and anflamatory cell recruitment in vivo
    • Rosen H, Gordon S. Monoclonal antibody to the murine type 3 complement receptor inhibits adhesion of myelomonocytic cells in vitro and anflamatory cell recruitment in vivo. J Exp Med. 1987;166:1685-701.
    • (1987) J Exp Med , vol.166 , pp. 1685-1701
    • Rosen, H.1    Gordon, S.2
  • 57
    • 0028141595 scopus 로고
    • Effect of thioglycollate and BCG stimuli on glucose and glutamine metabolism in rat macrophages
    • Costa Rosa LF, Safi DA, Curi R. Effect of thioglycollate and BCG stimuli on glucose and glutamine metabolism in rat macrophages. J Leukoc Biol. 1994; 56(1):10-4.
    • (1994) J Leukoc Biol , vol.56 , Issue.1 , pp. 10-14
    • Costa Rosa, L.F.1    Safi, D.A.2    Curi, R.3
  • 58
    • 0027937537 scopus 로고
    • Effects os n-6 and n-3 fatty acids on the survival of vincristine sensitive and resistant human cervical carcinoma cells, in vitro
    • Madhavi N, Das VN. Effects os n-6 and n-3 fatty acids on the survival of vincristine sensitive and resistant human cervical carcinoma cells, in vitro. Cancer Lett. 1994;84(1):31-41.
    • (1994) Cancer Lett , vol.84 , Issue.1 , pp. 31-41
    • Madhavi, N.1    Das, V.N.2
  • 59
    • 0034756636 scopus 로고    scopus 로고
    • Toxicity of South American snake venoms measured by an in vitro cell culture assay
    • Oliveira JC, de Oca HM, Duarte MM, Diniz CR, Fortes-Dias CL. Toxicity of South American snake venoms measured by an in vitro cell culture assay. Toxicon. 2002. 40(3):321-5.
    • (2002) Toxicon , vol.40 , Issue.3 , pp. 321-325
    • Oliveira, J.C.1    de Oca, H.M.2    Duarte, M.M.3    Diniz, C.R.4    Fortes-Dias, C.L.5
  • 60
    • 61849179292 scopus 로고    scopus 로고
    • Effects of Bothrops asper snake venom on the expression of cyclooxygenases and production of prostaglandins by peritoneal leukocytes in vivo, and by isolated neutrophils and macrophages in vitro
    • Moreira V, Gutiérrez JM, Amaral RB, Zamunér SR, Teixeira C de F. Effects of Bothrops asper snake venom on the expression of cyclooxygenases and production of prostaglandins by peritoneal leukocytes in vivo, and by isolated neutrophils and macrophages in vitro. Prostaglandins Leukot Essent Fatty Acids. 2009. 80(2-3):107-14.
    • (2009) Prostaglandins Leukot Essent Fatty Acids , vol.80 , Issue.2-3 , pp. 107-114
    • Moreira, V.1    Gutiérrez, J.M.2    Amaral, R.B.3    Zamunér, S.R.4    de Teixeira, C.F.5
  • 61
    • 50549181376 scopus 로고
    • Attachment and spreading of cells in culture
    • Taylor AC. Attachment and spreading of cells in culture. Exp Cell Res. 1961; 8:154-73.
    • (1961) Exp Cell Res , vol.8 , pp. 154-173
    • Taylor, A.C.1
  • 62
    • 0027170207 scopus 로고
    • The role of macrophages in skeletal muscle regeneration with particular reference to chemotaxis
    • Robertson TA, Maley MA, Grounds MD, Papadimitriou JM. The role of macrophages in skeletal muscle regeneration with particular reference to chemotaxis. Exp Cell Res. 1993;207(2):321-31.
    • (1993) Exp Cell Res , vol.207 , Issue.2 , pp. 321-331
    • Robertson, T.A.1    Maley, M.A.2    Grounds, M.D.3    Papadimitriou, J.M.4
  • 63
    • 0036773777 scopus 로고    scopus 로고
    • Protein kinase C isotypes and their specific functions: Prologue
    • Ohno S, Nishizuka Y. Protein kinase C isotypes and their specific functions: prologue. J Biochem. 2002;132(4):509-11.
    • (2002) J Biochem , vol.132 , Issue.4 , pp. 509-511
    • Ohno, S.1    Nishizuka, Y.2
  • 64
    • 0029829896 scopus 로고    scopus 로고
    • Molecular definition of distinct cytoesqueletal structures involved in complement-and Fc receptor-mediated phagocytosis in macrophages
    • Allen LA, Aderem A. Molecular definition of distinct cytoesqueletal structures involved in complement-and Fc receptor-mediated phagocytosis in macrophages. J Exp Med. 1996;184(2):627-37.
    • (1996) J Exp Med , vol.184 , Issue.2 , pp. 627-637
    • Allen, L.A.1    Aderem, A.2
  • 65
    • 0034283687 scopus 로고    scopus 로고
    • Differential requirement for classic and novel PKC isoforms in respiratory burst and phagocytosis in RAW 264.7 cells
    • Larsen EC, Di Gennaro JA, Saito N, Metha S, Loegering, DJ, Mazurkiewicz JM, et al. Differential requirement for classic and novel PKC isoforms in respiratory burst and phagocytosis in RAW 264.7 cells. J Immunol. 2000;165(5):2809-17.
    • (2000) J Immunol , vol.165 , Issue.5 , pp. 2809-2817
    • Larsen, E.C.1    di Gennaro, J.A.2    Saito, N.3    Metha, S.4    Loegering, D.J.5    Mazurkiewicz, J.M.6
  • 66
  • 67
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 1995;9(7):484-96.
    • (1995) FASEB J , vol.9 , Issue.7 , pp. 484-496
    • Nishizuka, Y.1
  • 68
    • 0037124093 scopus 로고    scopus 로고
    • Importance of C1B domain for lipid messenger-induced targeting of protein kinase C
    • Kashiwagi K, Shirai Y, Kuriyama M, Sakai N, Saito N. Importance of C1B domain for lipid messenger-induced targeting of protein kinase C. J Biol Chem. 2002;277(20):18037-45.
    • (2002) J Biol Chem , vol.277 , Issue.20 , pp. 18037-18045
    • Kashiwagi, K.1    Shirai, Y.2    Kuriyama, M.3    Sakai, N.4    Saito, N.5
  • 69
    • 0035413601 scopus 로고    scopus 로고
    • Protein Kinase C: Structural and spatial regulation by phosphorilatyon, cofactors, and macromolecular interactions
    • Newton AC. Protein Kinase C: structural and spatial regulation by phosphorilatyon, cofactors, and macromolecular interactions. Chem Rev. 2001;101(8):2353-64.
    • (2001) Chem Rev , vol.101 , Issue.8 , pp. 2353-2364
    • Newton, A.C.1
  • 70
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • Pt 2
    • Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J. 2003;370(Pt 2):361-71.
    • (2003) Biochem J , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 71
    • 0015596284 scopus 로고
    • Biological defense mechanism. The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior BM, Kipnes RS, Curcnutte JT. Biological defense mechanism. The production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest.1973;52(3):741-4.
    • (1973) J Clin Invest , vol.52 , Issue.3 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curcnutte, J.T.3
  • 73
    • 0031896343 scopus 로고    scopus 로고
    • The molecular basis of chronic granulomatous disease
    • Meischl C, Roos D. The molecular basis of chronic granulomatous disease. Springer Semin Immunopathol. 1998;19(4):417-34.
    • (1998) Springer Semin Immunopathol , vol.19 , Issue.4 , pp. 417-434
    • Meischl, C.1    Roos, D.2
  • 74
    • 62349140657 scopus 로고    scopus 로고
    • Molecular epidemiology of chronic granulomatous disease in a series of 80 kindreds: Identification of 31 novel mutations
    • Kannengiesser C, Gérard B, El Benna J, Henri D, Kroviarski Y, Chollet-Martin S, et al. Molecular epidemiology of chronic granulomatous disease in a series of 80 kindreds: identification of 31 novel mutations. Hum Mutat. 2008;29(9):132-49.
    • (2008) Hum Mutat , vol.29 , Issue.9 , pp. 132-149
    • Kannengiesser, C.1    Gérard, B.2    El Benna, J.3    Henri, D.4    Kroviarski, Y.5    Chollet-Martin, S.6
  • 75
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci. 2002;59(9):1428-59.
    • (2002) Cell Mol Life Sci , vol.59 , Issue.9 , pp. 1428-1459
    • Vignais, P.V.1
  • 76
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH-oxidase: A structural perspective
    • Pt 3
    • Groemping Y, Rittinger K. Activation and assembly of the NADPH-oxidase: a structural perspective. Biochem J. 2005;386(Pt 3):401-16.
    • (2005) Biochem J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 77
    • 0028142461 scopus 로고
    • The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline directed kinases
    • el Benna J, Faust LP, Babior BM. The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline directed kinases. J Biol Chem.1994;269(38):23431-6.
    • (1994) J Biol Chem , vol.269 , Issue.38 , pp. 23431-23436
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 78
    • 0028978633 scopus 로고
    • The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis
    • Faust LR, el Benna J, Babior BM., Chanock SJ. The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis. J Clin Invest. 1995;96(3):1499-505.
    • (1995) J Clin Invest , vol.96 , Issue.3 , pp. 1499-1505
    • Faust, L.R.1    El Benna, J.2    Babior, B.M.3    Chanock, S.J.4
  • 79
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn MT, Gauss KA. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J Leukoc Biol. 2004;76(4):760-81.
    • (2004) J Leukoc Biol , vol.76 , Issue.4 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 80
    • 33751224777 scopus 로고    scopus 로고
    • SK channels mediate NADPH oxidase-independent reactive oxygen species production and apoptosis in granulocytes
    • Fay AJ, Qian X, Jan YN, Jan LY. SK channels mediate NADPH oxidase-independent reactive oxygen species production and apoptosis in granulocytes. Proc Natl Acad Sci USA. 2006; 103(46):17548-53.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.46 , pp. 17548-17553
    • Fay, A.J.1    Qian, X.2    Jan, Y.N.3    Jan, L.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.