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Volumn 96, Issue 3, 2004, Pages 333-342

Biochemical properties of a bushmaster snake venom serine proteinase (LV-Ka), and its kinin releasing activity evaluated in rat mesenteric arterial rings

Author keywords

Bradykinin; Lachesis; Mesenteric arterial ring; Serine proteinase; Snake venom

Indexed keywords

ALPHA 2 MACROGLOBULIN; BOVINE KININOGEN; BRADYKININ; BRADYKININ B2 RECEPTOR ANTAGONIST; CASEIN; CHROMOGENIC SUBSTRATE; DEXTRO VALYLLEUCYLARGININE 4 NITROANILIDE; DEXTRO VALYLLEUCYLLYSINE 4 NITROANILIDE; DIMETHYLCASEIN; GLYCOPROTEIN; GLYCOSIDASE; ICATIBANT; INDOMETACIN; KALLIKREIN; KININ; KININOGEN; LV KA PROTEIN; N GLYCOSIDASE F; PLASMIN; POLYPEPTIDE; PROSTAGLANDIN SYNTHASE INHIBITOR; PROTEIN; PROTEINASE INHIBITOR; SERINE PROTEINASE; SNAKE VENOM; TISSUE KALLIKREIN; UNCLASSIFIED DRUG;

EID: 10944240203     PISSN: 13478613     EISSN: None     Source Type: Journal    
DOI: 10.1254/jphs.FPJ04005X     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0025851952 scopus 로고
    • Effects of snake venoms on hemostasis
    • Meier J, Stocker K. Effects of snake venoms on hemostasis. Crit Rev Toxicol. 1991;21:171-182.
    • (1991) Crit Rev Toxicol , vol.21 , pp. 171-182
    • Meier, J.1    Stocker, K.2
  • 2
    • 0033741151 scopus 로고    scopus 로고
    • Snake venom proteins acting on hemostasis
    • Braud S, Bon C, Wisner A. Snake venom proteins acting on hemostasis. Biochimie. 2000;82:851-859.
    • (2000) Biochimie , vol.82 , pp. 851-859
    • Braud, S.1    Bon, C.2    Wisner, A.3
  • 3
    • 10944229005 scopus 로고
    • Bradykininogen levels following Crotalus envenomation
    • Russell FE. Bradykininogen levels following Crotalus envenomation. Toxicon. 1965;2:277-279.
    • (1965) Toxicon , vol.2 , pp. 277-279
    • Russell, F.E.1
  • 4
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland FS. Snake venoms and the hemostatic system. Toxicon. 1998;36:1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 5
    • 0035742969 scopus 로고    scopus 로고
    • Snake venom proteinases as tools in hemostasis studies: Structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom
    • Wisner A, Braud S, Bon C. Snake venom proteinases as tools in hemostasis studies: structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom. Haemostasis. 2001;31:133-140.
    • (2001) Haemostasis , vol.31 , pp. 133-140
    • Wisner, A.1    Braud, S.2    Bon, C.3
  • 6
    • 84931128415 scopus 로고
    • Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and trypsin
    • Rocha e Silva, M, Beraldo WT, Rosenfeld G. Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and trypsin. Am J Physiol. 1949;156:261-273.
    • (1949) Am J Physiol , vol.156 , pp. 261-273
    • Rocha E Silva, M.1    Beraldo, W.T.2    Rosenfeld, G.3
  • 7
    • 0006411257 scopus 로고
    • Physiological and pharmacological effects of rattlesnake venoms
    • Tu AT, editor: New York: Marcel Decker
    • Hawgood BJ. Physiological and pharmacological effects of rattlesnake venoms. In: Tu AT, editor. Rattlesnake venoms: New York: Marcel Decker; 1982. p. 121-162.
    • (1982) Rattlesnake Venoms , pp. 121-162
    • Hawgood, B.J.1
  • 8
    • 0031754694 scopus 로고    scopus 로고
    • Chemistry and biochemistry of kallikrein-like enzyme from snake venoms
    • Komori Y, Nikai T. Chemistry and biochemistry of kallikrein-like enzyme from snake venoms. J Toxicol-Toxin Rev. 1998; 17:261-277.
    • (1998) J Toxicol-Toxin Rev , vol.17 , pp. 261-277
    • Komori, Y.1    Nikai, T.2
  • 9
    • 0034811398 scopus 로고    scopus 로고
    • Fibrinogenolytic proteases isolated from the snake venom of Taiwan habu: Serine proteases with kallikrein-like and angiotensin-degrading activities
    • Hung CC, Chiou SH. Fibrinogenolytic proteases isolated from the snake venom of Taiwan habu: serine proteases with kallikrein-like and angiotensin-degrading activities. Biochem Biophys Res Commun. 2001;281:1012-1018.
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 1012-1018
    • Hung, C.C.1    Chiou, S.H.2
  • 10
    • 0024811327 scopus 로고
    • Purification and properties of the thrombin-like enzyme from the venom of Lachesis muta muta
    • Silveira AMV, Magalhães A, Diniz CR, Oliveira EB. Purification and properties of the thrombin-like enzyme from the venom of Lachesis muta muta. Int J Biochem. 1989;21:863-871.
    • (1989) Int J Biochem , vol.21 , pp. 863-871
    • Silveira, A.M.V.1    Magalhães, A.2    Diniz, C.R.3    Oliveira, E.B.4
  • 11
    • 0026577668 scopus 로고
    • Purification and properties of a kininogenin from the venom of Lachesis muta muta (bushmaster)
    • Diniz MRV, Oliveira EB. Purification and properties of a kininogenin from the venom of Lachesis muta muta (bushmaster). Toxicon. 1992;30:247-258.
    • (1992) Toxicon , vol.30 , pp. 247-258
    • Diniz, M.R.V.1    Oliveira, E.B.2
  • 12
    • 33750605786 scopus 로고    scopus 로고
    • Mutalysins
    • Barrett AJ, Rawlings ND, Woessner FJ, editors. Elsevier Ltd; In press
    • Sanchez EF. Mutalysins. In: Barrett AJ, Rawlings ND, Woessner FJ, editors. Handbook of proteolytic enzymes. 2nd ed. Elsevier Ltd; In press. 2004.
    • (2004) Handbook of Proteolytic Enzymes. 2nd Ed.
    • Sanchez, E.F.1
  • 13
    • 0024373445 scopus 로고
    • A gyroxin analogue from the venom of the bushmaster (Lachesis muta muta)
    • Da Silva ND, Aird SD, Seebert C, Kaiser II. A gyroxin analogue from the venom of the bushmaster (Lachesis muta muta). Toxicon. 1989;27:763-771.
    • (1989) Toxicon , vol.27 , pp. 763-771
    • Da Silva, N.D.1    Aird, S.D.2    Seebert, C.3    Kaiser, I.I.4
  • 15
    • 0034213534 scopus 로고    scopus 로고
    • Isolation of a proteinase with plasminogen activating activity from Lachesis muta muta (bushmaster) snake venom
    • Sanchez EF, Santos CI, Magalhães A, Diniz CR, Figueiredo S, Gilroy J, et al. Isolation of a proteinase with plasminogen activating activity from Lachesis muta muta (bushmaster) snake venom. Arch Biochem Biophys. 2000;378:131-141.
    • (2000) Arch Biochem Biophys , vol.378 , pp. 131-141
    • Sanchez, E.F.1    Santos, C.I.2    Magalhães, A.3    Diniz, C.R.4    Figueiredo, S.5    Gilroy, J.6
  • 16
    • 0027305178 scopus 로고
    • The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta)
    • Magalhães A, Fonseca BCB, Diniz CR, Gilroy J, Richardson M. The complete amino acid sequence of a thrombin-like enzyme/gyroxin analogue from venom of the bushmaster snake (Lachesis muta muta). FEBS Lett. 1993;325:116-120.
    • (1993) FEBS Lett , vol.325 , pp. 116-120
    • Magalhães, A.1    Fonseca, B.C.B.2    Diniz, C.R.3    Gilroy, J.4    Richardson, M.5
  • 17
    • 0032005943 scopus 로고    scopus 로고
    • Purification and characterization of a kinin-releasing and fibrinogen clotting serine proteinase (KNBJ) from the venom of Bothrops jararaca, and molecular cloning and sequence analysis of its cDNA
    • Serrano SMT, Hagiwara Y, Muruyama N, Higuchi S, Mentele R, Sampaio CAM, et al. Purification and characterization of a kinin-releasing and fibrinogen clotting serine proteinase (KNBJ) from the venom of Bothrops jararaca, and molecular cloning and sequence analysis of its cDNA. Eur J Biochem. 1998;251:845-853.
    • (1998) Eur J Biochem , vol.251 , pp. 845-853
    • Serrano, S.M.T.1    Hagiwara, Y.2    Muruyama, N.3    Higuchi, S.4    Mentele, R.5    Sampaio, C.A.M.6
  • 18
    • 0019021441 scopus 로고
    • Covalent binding of proteinases in their reaction with alpha 2-macroglobulin
    • Salvesen GS, Barrett AJ. Covalent binding of proteinases in their reaction with alpha 2-macroglobulin. Biochem J. 1980; 187:695-701.
    • (1980) Biochem J , vol.187 , pp. 695-701
    • Salvesen, G.S.1    Barrett, A.J.2
  • 19
    • 0024333351 scopus 로고
    • α2-macroglobulins: Structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen L. α2-macroglobulins: structure, shape, and mechanism of proteinase complex formation. J Biol Chem. 1989;264:11539-11542.
    • (1989) J Biol Chem , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 20
    • 0342359205 scopus 로고    scopus 로고
    • Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems
    • Estevao-Costa MI, Diniz CR, Magalhaes A, Markland FS, Sanchez EF. Action of metalloproteinases mutalysin I and II on several components of the hemostatic and fibrinolytic systems. Thromb Res. 2000;99:363-376.
    • (2000) Thromb Res , vol.99 , pp. 363-376
    • Estevao-Costa, M.I.1    Diniz, C.R.2    Magalhaes, A.3    Markland, F.S.4    Sanchez, E.F.5
  • 21
    • 0031565264 scopus 로고    scopus 로고
    • Arachidonic acid products-mediated contraction induced by bradykinin in relaxed mesenteric arterial rings from Holtzman rats
    • Weinberg MLD, Moreira E, Weinberg J. Arachidonic acid products-mediated contraction induced by bradykinin in relaxed mesenteric arterial rings from Holtzman rats. Eur J Pharmacol. 1997;320:145-150.
    • (1997) Eur J Pharmacol , vol.320 , pp. 145-150
    • Weinberg, M.L.D.1    Moreira, E.2    Weinberg, J.3
  • 22
    • 10944267859 scopus 로고    scopus 로고
    • Prostanoid-mediated bradykinin-induced contraction of relaxed mesenteric arterial rings from spontaneously hypertensive rats
    • Águas de Lindóia, Brazil
    • Weinberg MLD, Weinberg J. Prostanoid-mediated bradykinin-induced contraction of relaxed mesenteric arterial rings from spontaneously hypertensive rats. Abstracts from XVI Latin-american Congress of Pharmacology, Águas de Lindóia, Brazil. 2000:292.
    • (2000) Abstracts from XVI Latin-American Congress of Pharmacology , pp. 292
    • Weinberg, M.L.D.1    Weinberg, J.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0017990368 scopus 로고
    • Isolation of pure IgGa, IgG2a immunoglobulins from mouse serum using protein A-Sepharose
    • Ey PL, Pouse SJ, Jenking CR. Isolation of pure IgGa, IgG2a immunoglobulins from mouse serum using protein A-Sepharose. Immunochemistry. 1978;15:429-436.
    • (1978) Immunochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Pouse, S.J.2    Jenking, C.R.3
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehlin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Nat Acad Sci USA. 1979;76:4350-4356.
    • (1979) Proc Nat Acad Sci USA , vol.76 , pp. 4350-4356
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 27
    • 0025620159 scopus 로고
    • A statistical treatment for solution of a family of simultaneous equations derived from enzyme inhibition studies
    • Junqueira RG, Mares-Guia M. A statistical treatment for solution of a family of simultaneous equations derived from enzyme inhibition studies. Braz J Med Biol Res. 1990;23:773-784.
    • (1990) Braz J Med Biol Res , vol.23 , pp. 773-784
    • Junqueira, R.G.1    Mares-Guia, M.2
  • 28
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schlechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commum. 1967;27:157-162.
    • (1967) Biochem Biophys Res Commum , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 30
    • 0027432428 scopus 로고
    • Complete primary structure and biochemical properties of gilatoxin, a serine protease with kallikrein-like and angiotensin-degrading activities
    • Utaisincharoen P, Mackessy SP, Miller RA, Tu AT. Complete primary structure and biochemical properties of gilatoxin, a serine protease with kallikrein-like and angiotensin-degrading activities. J Biol Chem. 1993;268:21975-21983.
    • (1993) J Biol Chem , vol.268 , pp. 21975-21983
    • Utaisincharoen, P.1    Mackessy, S.P.2    Miller, R.A.3    Tu, A.T.4
  • 31
    • 0024278701 scopus 로고
    • Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family
    • Itoh N, Tanaka N, Funakoshi I, Kawasaki T, Mihashi S, Yamashina I. Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family. J Biol Chem. 1988;263:7628-7631.
    • (1988) J Biol Chem , vol.263 , pp. 7628-7631
    • Itoh, N.1    Tanaka, N.2    Funakoshi, I.3    Kawasaki, T.4    Mihashi, S.5    Yamashina, I.6
  • 32
    • 0012009598 scopus 로고
    • Cardiovascular effects of snake venoms
    • Lee CY, editor, Berlin: Spring-Verlag
    • Lee CY, Lee S. Cardiovascular effects of snake venoms. In: Lee CY, editor. Snake venoms, Berlin: Spring-Verlag; 1979. p. 547-590.
    • (1979) Snake Venoms , pp. 547-590
    • Lee, C.Y.1    Lee, S.2
  • 36
    • 0021223962 scopus 로고
    • Further evidence for the existence of two receptor sites for bradykinin responsible for the diphasic effect in the rat isolated duodenum
    • Boschcov P, Paiva ACM, Paiva TB, Shimuta S. Further evidence for the existence of two receptor sites for bradykinin responsible for the diphasic effect in the rat isolated duodenum. Br J Pharmacol. 1984;83:591-600.
    • (1984) Br J Pharmacol , vol.83 , pp. 591-600
    • Boschcov, P.1    Paiva, A.C.M.2    Paiva, T.B.3    Shimuta, S.4
  • 38
    • 0028170434 scopus 로고
    • 2 receptors and coupling mechanisms in the smooth muscle of the guinea-pig Taenia caeci
    • 2 receptors and coupling mechanisms in the smooth muscle of the guinea-pig Taenia caeci. Br J Pharmacol. 1994;113:607-613.
    • (1994) Br J Pharmacol , vol.113 , pp. 607-613
    • Field, J.L.1    Butt, S.K.2    Morton, I.K.M.3    Hall, J.M.4
  • 40
    • 0018995127 scopus 로고
    • Pharmacology of bradykinin and related kinins
    • Regoli D, Barabé J. Pharmacology of bradykinin and related kinins. Pharmacol Rev. 1980;32:1-46.
    • (1980) Pharmacol Rev , vol.32 , pp. 1-46
    • Regoli, D.1    Barabé, J.2
  • 41
    • 0027474517 scopus 로고
    • Bradykinin: Potential for vascular constriction in the presence of endothelial injury
    • Briner VA, Tsai P, Schrier RW. Bradykinin: potential for vascular constriction in the presence of endothelial injury. Am J Physiol. 1993;264:F322-F327.
    • (1993) Am J Physiol , vol.264
    • Briner, V.A.1    Tsai, P.2    Schrier, R.W.3


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