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Volumn 38, Issue 2, 2000, Pages 199-208

Effect of crotapotin and heparin on the rat paw oedema induced by different secretory phospholipases A2

Author keywords

[No Author keywords available]

Indexed keywords

HEPARIN; PHOSPHOLIPASE A2; POLYPEPTIDE;

EID: 0033991677     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(99)00143-9     Document Type: Article
Times cited : (58)

References (34)
  • 1
    • 0029860316 scopus 로고    scopus 로고
    • A heparin-sensitive phospholipase A2 and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase of prostaglandin D2 generation in mouse bone marrow-derived mast cells
    • Bingham C.O. 3rd, Murakami M., Fujishima H., Hunt J.E., Austen K.F., Arm J.P. A heparin-sensitive phospholipase A2 and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase of prostaglandin D2 generation in mouse bone marrow-derived mast cells. J. Biol. Chem. 271:1996;25936-25944.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25936-25944
    • Bingham C.O. III1    Murakami, M.2    Fujishima, H.3    Hunt, J.E.4    Austen, K.F.5    Arm, J.P.6
  • 2
    • 0017905777 scopus 로고
    • Phospholipase A2 activity of guinea-pig isolated perfused lungs: Stimulation and inhibition by anti-inflammatory steroids
    • Blackwell G.J., Flower R.J., Nijkamp F.P., Vane J.R. Phospholipase A2 activity of guinea-pig isolated perfused lungs: stimulation and inhibition by anti-inflammatory steroids. Br. J. Pharmacol. 62:1978;79-89.
    • (1978) Br. J. Pharmacol. , vol.62 , pp. 79-89
    • Blackwell, G.J.1    Flower, R.J.2    Nijkamp, F.P.3    Vane, J.R.4
  • 3
    • 0020030764 scopus 로고
    • Synergism of the two subunits of crotoxin
    • Bon C. Synergism of the two subunits of crotoxin. Toxicon. 2:1982;105-109.
    • (1982) Toxicon , vol.2 , pp. 105-109
    • Bon, C.1
  • 4
    • 0018522325 scopus 로고
    • Postsynaptic effects of crotoxin and of its isolated subunits
    • Bon C., Changeux J., Jeng T., Fraenkel-Conrat H. Postsynaptic effects of crotoxin and of its isolated subunits. Eur. J. Biochem. 99:1979;471-481.
    • (1979) Eur. J. Biochem. , vol.99 , pp. 471-481
    • Bon, C.1    Changeux, J.2    Jeng, T.3    Fraenkel-Conrat, H.4
  • 5
    • 0346296665 scopus 로고
    • Neurotoxic and myotoxic effects of Crotalus phospholipase A and its complex with crotapotin
    • Breithaupt H. Neurotoxic and myotoxic effects of Crotalus phospholipase A and its complex with crotapotin. Naunyn-Schmiedeberg's Arch. Pharmacol. 292:1976;271-278.
    • (1976) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.292 , pp. 271-278
    • Breithaupt, H.1
  • 6
    • 0025822798 scopus 로고
    • Chromogenic substrates and assay of phospholipase A2
    • Cho W., Kézdy F.J. Chromogenic substrates and assay of phospholipase A2. Meth. Enzymol. 197:1991;75-79.
    • (1991) Meth. Enzymol. , vol.197 , pp. 75-79
    • Cho, W.1    Kézdy, F.J.2
  • 7
    • 0027339013 scopus 로고
    • Snake-venom phospholipase A2 neurotoxins. Potentiation of a single-chain crotoxin by the chaperon subunit of a two-component neurotoxin
    • Choumet V., Saliou B., Fideler L., Chen Y.C., Gubensek F., Bon C., Delot E. Snake-venom phospholipase A2 neurotoxins. Potentiation of a single-chain crotoxin by the chaperon subunit of a two-component neurotoxin. Eur. J. Biochem. 211:1993;57-62.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 57-62
    • Choumet, V.1    Saliou, B.2    Fideler, L.3    Chen, Y.C.4    Gubensek, F.5    Bon, C.6    Delot, E.7
  • 8
    • 0011930724 scopus 로고
    • Human recombinant lipocortin 1 has acute local anti-inflammatory properties in the rat paw oedema test
    • Cirino G., Peers S.H., Flower R.J., Pepinsky R.B. Human recombinant lipocortin 1 has acute local anti-inflammatory properties in the rat paw oedema test. Proc. Natl. Acad. Sci. USA. 86:1989;3428-3432.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 3428-3432
    • Cirino, G.1    Peers, S.H.2    Flower, R.J.3    Pepinsky, R.B.4
  • 9
    • 0342539648 scopus 로고
    • Histamine release, formation of prostaglandin-like activity (SRS-C) and mast cell degranulation by the direct lytic factor (DLF) and phospholipase A of cobra venom
    • Damerau B., Lege L., Oldigs H.D., Vogt W. Histamine release, formation of prostaglandin-like activity (SRS-C) and mast cell degranulation by the direct lytic factor (DLF) and phospholipase A of cobra venom. Naunyn Schmiedebergs Arch. Pharmac. 287:1975;141-156.
    • (1975) Naunyn Schmiedebergs Arch. Pharmac. , vol.287 , pp. 141-156
    • Damerau, B.1    Lege, L.2    Oldigs, H.D.3    Vogt, W.4
  • 10
    • 0028338536 scopus 로고
    • Diversity of group types, regulation, and function of phospholipase A2
    • Dennis E.A. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem. 269:1994;13057-13060.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 11
    • 0028255937 scopus 로고
    • Inhibition of human secretory class II phospholipase A2 by heparin
    • Dua R., Cho W. Inhibition of human secretory class II phospholipase A2 by heparin. Eur. J. Biochem. 221:1994;481-490.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 481-490
    • Dua, R.1    Cho, W.2
  • 13
    • 0028260952 scopus 로고
    • Evidence that secretory phospholipase A2 plays a role in arachidonic acid release and eicosanoid biosynthesis by mast cell.
    • Fonteh A.N., Bass D.A., Marshall L.A., Seeds M., Samet J.M., Chilton F.H. Evidence that secretory phospholipase A2 plays a role in arachidonic acid release and eicosanoid biosynthesis by mast cell. J. Immunol. 152:1994;5438-5446.
    • (1994) J. Immunol. , vol.152 , pp. 5438-5446
    • Fonteh, A.N.1    Bass, D.A.2    Marshall, L.A.3    Seeds, M.4    Samet, J.M.5    Chilton, F.H.6
  • 14
    • 0021347822 scopus 로고
    • Cellular and mithocondrial changes induced in the structure of murine skeletal muscle by crotoxin, a neurotoxic phospholipase A2 complex
    • Gopalakrishnakone P., Dempster D.W., Hawgood B.J., Elder H Y. Cellular and mithocondrial changes induced in the structure of murine skeletal muscle by crotoxin, a neurotoxic phospholipase A2 complex. Toxicon. 22:1984;85-98.
    • (1984) Toxicon , vol.22 , pp. 85-98
    • Gopalakrishnakone, P.1    Dempster, D.W.2    Hawgood, B.J.3    Elder, H.Y.4
  • 15
    • 0017919089 scopus 로고
    • The crotoxin complex- an example of biochemical and paharmacological protein complementation
    • Habermann E., Breithaupt H. The crotoxin complex- an example of biochemical and paharmacological protein complementation. Toxicon. 16:1978;19-30.
    • (1978) Toxicon , vol.16 , pp. 19-30
    • Habermann, E.1    Breithaupt, H.2
  • 16
    • 77956938631 scopus 로고
    • Boyer New York: Academic Press
    • Hanahan D.N. Boyer. The enzymes. vol 4:1971;71-84 Academic Press, New York.
    • (1971) The Enzymes , vol.4 , pp. 71-84
    • Hanahan, D.N.1
  • 17
    • 0017376906 scopus 로고
    • Amino acid sequence of phospholipase A2-α From the venom of Crotalus adamanteus. A new classification of phospholipase A2 based upon structural determinants
    • Heinrikson R.L., Krueger E.T., Keim P.S. Amino acid sequence of phospholipase A2-α from the venom of Crotalus adamanteus. A new classification of phospholipase A2 based upon structural determinants. J. Biol. Chem. 252:1977;4913-4977.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4913-4977
    • Heinrikson, R.L.1    Krueger, E.T.2    Keim, P.S.3
  • 19
    • 0028084979 scopus 로고
    • Cloning and expression of a membrane receptor for secretory phospholipase A2
    • Lambeau G., Ancian P., Barhanin J., Lazdunski M. Cloning and expression of a membrane receptor for secretory phospholipase A2. J. Biol. Chem. 269:1994;1575-1578.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1575-1578
    • Lambeau, G.1    Ancian, P.2    Barhanin, J.3    Lazdunski, M.4
  • 23
    • 0028277990 scopus 로고
    • Neutralization of the cytosolic and myotoxic activities of phospholipase A2 from Bothrops asper snake venom by glycosaminoglycans of heparin/heparan sulfate family Biochem
    • Lomonte B., Tarkowski A., Bagge U., Harson L.A. Neutralization of the cytosolic and myotoxic activities of phospholipase A2 from Bothrops asper snake venom by glycosaminoglycans of heparin/heparan sulfate family Biochem. Pharmacol. 47:1994;1509-1518.
    • (1994) Pharmacol. , vol.47 , pp. 1509-1518
    • Lomonte, B.1    Tarkowski, A.2    Bagge, U.3    Harson, L.A.4
  • 24
    • 0027409655 scopus 로고
    • Antagonism of the myotoxic effects of Bothrops jararacussu venom and bothropstoxin by polyanions
    • Melo P.A., Homsi-Brandenburgo M.I., Giglio J.R., Suarez-Kurtz G. Antagonism of the myotoxic effects of Bothrops jararacussu venom and bothropstoxin by polyanions. Toxicon. 31:1993;285-291.
    • (1993) Toxicon , vol.31 , pp. 285-291
    • Melo, P.A.1    Homsi-Brandenburgo, M.I.2    Giglio, J.R.3    Suarez-Kurtz, G.4
  • 25
    • 0026611698 scopus 로고
    • PLA2 induced oedema in rat skin and histamine release in rat mast cells. Evidence for involvement of lysophospholipids in the mechanism of action
    • Moreno J.J., Ferrer X., Ortega E., Carganico G. PLA2 induced oedema in rat skin and histamine release in rat mast cells. Evidence for involvement of lysophospholipids in the mechanism of action. Agents Actions. 36:1992;258-263.
    • (1992) Agents Actions , vol.36 , pp. 258-263
    • Moreno, J.J.1    Ferrer, X.2    Ortega, E.3    Carganico, G.4
  • 26
    • 0027501885 scopus 로고
    • Triggering of degranulation in mast cells by exogenous type II phospholipase A2
    • Murakami M., Hara N., Kudo I., Inoue K. Triggering of degranulation in mast cells by exogenous type II phospholipase A2. J. Immunol. 151:1993;5675-5684.
    • (1993) J. Immunol. , vol.151 , pp. 5675-5684
    • Murakami, M.1    Hara, N.2    Kudo, I.3    Inoue, K.4
  • 27
    • 0026780031 scopus 로고
    • Release of 14-kDa group II phospholipase A2 from activated mast cells and its possible involvement in the regulation of the degranulation process
    • Murakami M., Kudo I., Suwa Y., Inoue K. Release of 14-kDa group II phospholipase A2 from activated mast cells and its possible involvement in the regulation of the degranulation process. Eur. J. Biochem. 209:1992;257-263.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 257-263
    • Murakami, M.1    Kudo, I.2    Suwa, Y.3    Inoue, K.4
  • 29
    • 0014998859 scopus 로고
    • Biochemistry and pharmacology of the crotoxin complex. I. Subfractionation and recombination of the crotoxin complex
    • Rubsamen K., Breihaupt H., Habermann E. Biochemistry and pharmacology of the crotoxin complex. I. Subfractionation and recombination of the crotoxin complex. Naunyn-Schmiedeberg's Arch. Pharmacol. 270:1971;274-288.
    • (1971) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.270 , pp. 274-288
    • Rubsamen, K.1    Breihaupt, H.2    Habermann, E.3
  • 30
    • 0029860085 scopus 로고    scopus 로고
    • Binding of human phospholipase A2 type II to proteoglycans. Differential effect of glycosaminoglycans on enzyme activity
    • Sartipy P., Johansen B., Camejo G., Rosengren B., Bondjers G., Hurt-Camejo E. Binding of human phospholipase A2 type II to proteoglycans. Differential effect of glycosaminoglycans on enzyme activity. J. Biol. Chem. 271:1996;26307-26314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26307-26314
    • Sartipy, P.1    Johansen, B.2    Camejo, G.3    Rosengren, B.4    Bondjers, G.5    Hurt-Camejo, E.6
  • 31
  • 33
    • 0004188937 scopus 로고
    • Hanahan D.J. New York: Plenum Press
    • Wait M. Hanahan D.J. The Phospholipases. vol. 5:1987;155 Plenum Press, New York.
    • (1987) The Phospholipases , vol.5 , pp. 155
    • Wait, M.1
  • 34
    • 0028092860 scopus 로고
    • Structure-function relationship of phospholipase A2 from snake venoms.
    • Yang C.C. Structure-function relationship of phospholipase A2 from snake venoms. J. Toxicol. 13:1994;125-177.
    • (1994) J. Toxicol. , vol.13 , pp. 125-177
    • Yang, C.C.1


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