Snake venom cardiotoxin induces G-actin polymerization

Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl 2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl 2 was present in the buffe...

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Published inBiochimica et biophysica acta Vol. 966; no. 2; pp. 266 - 268
Main Authors Chen, Yee-Hsiung, Chu, Sin-Tak
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 11.08.1988
Elsevier
North-Holland
Subjects
Actin polymerization
Actins - metabolism
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biopolymers - metabolism
Cardiotoxin
Cobra Cardiotoxin Proteins - pharmacology
Contractile proteins
Elapid Venoms - pharmacology
Fundamental and applied biological sciences. Psychology
Holoproteins
In Vitro Techniques
Muscles - drug effects
Muscles - metabolism
Proteins
Rabbit skeletal muscle
Rabbits
Snake venom
Cardiotoxin
Snake venom
Actin polymerization
Rabbit skeletal muscle
Vertebrata
Mammalia
Basic protein
Venom
Actins
Rabbit
Polymerization
Molecular interaction
Reptilia
Lagomorpha
Striated muscle
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Abstract Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl 2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl 2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
AbstractList Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl 2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl 2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.Snake venom cardiotoxin showed the ability to induce polymerization of G-actin from rabbit skeletal muscle in a low ionic strength buffer composed of 0.2 mM CaCl2/0.2 mM ATP/0.5 mM mercaptoethanol/2.0 mM Tris-HCl, pH 8.0. The activity was enhanced greatly when 0.4 mM MgCl2 was present in the buffer and could be inhibited if G-actin was preincubated with deoxyribonuclease I. Furthermore, the DNAase could also partially depolymerize actin polymer previously formed by the interaction of G-actin with the toxin.
Author Chen, Yee-Hsiung
Chu, Sin-Tak
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Issue 2
Keywords Cardiotoxin
Snake venom
Actin polymerization
Rabbit skeletal muscle
Vertebrata
Mammalia
Basic protein
Venom
Actins
Rabbit
Polymerization
Molecular interaction
Reptilia
Lagomorpha
Striated muscle
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References Spudich, Cooke (BIB7) 1971; 246
Chang (BIB2) 1979; Vol. 52
Chen, Pan, Lee (BIB1) 1982; 702
Chen, Liou, Hu, Juan, Yang (BIB3) 1987; 73
Tu (BIB5) 1977
Bray, Thomas (BIB6) 1976; 105
Condrea (BIB4) 1979; Vol. 52
Lazarides, Lindberg (BIB11) 1974; 71
Higashi, Oosawa (BIB8) 1965; 12
Lo, Chen, Lee (BIB10) 1966; 13
Spudich, Cooke (BIB9) 1975; 250
Lin, Lin (BIB12) 1979; 76
Chen (10.1016/0304-4165(88)90120-1_BIB3) 1987; 73
Spudich (10.1016/0304-4165(88)90120-1_BIB7) 1971; 246
Tu (10.1016/0304-4165(88)90120-1_BIB5) 1977
Lazarides (10.1016/0304-4165(88)90120-1_BIB11) 1974; 71
Condrea (10.1016/0304-4165(88)90120-1_BIB4) 1979; Vol. 52
Lin (10.1016/0304-4165(88)90120-1_BIB12) 1979; 76
Chen (10.1016/0304-4165(88)90120-1_BIB1) 1982; 702
Lo (10.1016/0304-4165(88)90120-1_BIB10) 1966; 13
Bray (10.1016/0304-4165(88)90120-1_BIB6) 1976; 105
Spudich (10.1016/0304-4165(88)90120-1_BIB9) 1975; 250
Higashi (10.1016/0304-4165(88)90120-1_BIB8) 1965; 12
Chang (10.1016/0304-4165(88)90120-1_BIB2) 1979; Vol. 52
References_xml – volume: 250
  start-page: 7485
  year: 1975
  end-page: 7491
  ident: BIB9
  publication-title: J. Biol. Chem.
– volume: 73
  start-page: 69
  year: 1987
  end-page: 76
  ident: BIB3
  publication-title: Mol. Cell. Biochem.
– volume: Vol. 52
  start-page: 448
  year: 1979
  end-page: 472
  ident: BIB4
  publication-title: Handbook of Experimental Pharmacology
– start-page: 301
  year: 1977
  end-page: 320
  ident: BIB5
  article-title: Venom: Chemistry and Molecular Biology
– volume: 12
  start-page: 843
  year: 1965
  end-page: 865
  ident: BIB8
  publication-title: J. Mol. Biol.
– volume: 13
  start-page: 25
  year: 1966
  end-page: 37
  ident: BIB10
  publication-title: J. Chin. Chem. Soc.
– volume: 76
  start-page: 2345
  year: 1979
  end-page: 2349
  ident: BIB12
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: Vol. 52
  start-page: 309
  year: 1979
  end-page: 376
  ident: BIB2
  publication-title: Handbook of Experimental Pharmacology
– volume: 702
  start-page: 193
  year: 1982
  end-page: 196
  ident: BIB1
  publication-title: Biochim. Biophys. Acta
– volume: 105
  start-page: 527
  year: 1976
  end-page: 544
  ident: BIB6
  publication-title: J. Mol. Biol.
– volume: 246
  start-page: 4866
  year: 1971
  end-page: 4871
  ident: BIB7
  publication-title: J. Biol. Chem.
– volume: 71
  start-page: 4742
  year: 1974
  end-page: 4746
  ident: BIB11
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 246
  start-page: 4866
  year: 1971
  ident: 10.1016/0304-4165(88)90120-1_BIB7
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)62016-2
– start-page: 301
  year: 1977
  ident: 10.1016/0304-4165(88)90120-1_BIB5
  article-title: Venom: Chemistry and Molecular Biology
– volume: 76
  start-page: 2345
  year: 1979
  ident: 10.1016/0304-4165(88)90120-1_BIB12
– volume: 105
  start-page: 527
  year: 1976
  ident: 10.1016/0304-4165(88)90120-1_BIB6
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(76)90233-3
– volume: 12
  start-page: 843
  year: 1965
  ident: 10.1016/0304-4165(88)90120-1_BIB8
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(65)80332-1
– volume: 702
  start-page: 193
  year: 1982
  ident: 10.1016/0304-4165(88)90120-1_BIB1
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0167-4838(82)90502-7
– volume: Vol. 52
  start-page: 309
  year: 1979
  ident: 10.1016/0304-4165(88)90120-1_BIB2
– volume: Vol. 52
  start-page: 448
  year: 1979
  ident: 10.1016/0304-4165(88)90120-1_BIB4
– volume: 73
  start-page: 69
  year: 1987
  ident: 10.1016/0304-4165(88)90120-1_BIB3
  publication-title: Mol. Cell. Biochem.
  doi: 10.1007/BF00229378
– volume: 250
  start-page: 7485
  year: 1975
  ident: 10.1016/0304-4165(88)90120-1_BIB9
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)40970-8
– volume: 13
  start-page: 25
  year: 1966
  ident: 10.1016/0304-4165(88)90120-1_BIB10
  publication-title: J. Chin. Chem. Soc.
  doi: 10.1002/jccs.196600004
– volume: 71
  start-page: 4742
  year: 1974
  ident: 10.1016/0304-4165(88)90120-1_BIB11
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SubjectTerms Actin polymerization
Actins - metabolism
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biopolymers - metabolism
Cardiotoxin
Cobra Cardiotoxin Proteins - pharmacology
Contractile proteins
Elapid Venoms - pharmacology
Fundamental and applied biological sciences. Psychology
Holoproteins
In Vitro Techniques
Muscles - drug effects
Muscles - metabolism
Proteins
Rabbit skeletal muscle
Rabbits
Snake venom
Title Snake venom cardiotoxin induces G-actin polymerization
URI https://dx.doi.org/10.1016/0304-4165(88)90120-1
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