Stimulation of Tissue Transglutaminase Activity by Clostridium botulinum Neurotoxin Type B

  • Moon, Yu-Seok (Department of Biological Science, Korea advanced institute of Science and Technology) ;
  • Gi-Hyeok (Microbial Toxin Research Institute, Medy-Tox Inc.) ;
  • Rhee, Sang-Dal (Department of Biological Science, Korea advanced institute of Science and Technology) ;
  • Jung, Hyun-Ho (Microbial Toxin Research Institute, Medy-Tox Inc.,Division of Applied Biological Sciences, Sunmoon University)
  • Published : 2003.06.01

Abstract

Recombinant light chain of Clostridium botulinum neurotoxin type B stimulated transglutaminase activity in a dose dependent manner, Compared to native toxin, recombinant light chain showed av greater stimulatory effect on transglutaminase activity. Zn-chelating agents, inhibiting the proteolytic activity of the clostridial toxins, did not interfere with this stimulation. These results suggest that the light chain plays a major stimulatory role, which is not due to its metallopeptidase activity, but is possibly due to specific interaction with transglutaminase. More importantly, this report provides a new insight into the intracellular action of C. botulinum neurotoxins.

Keywords

References

  1. Botulinum, tetanus neurotoxins: neurotransmission and biomedical aspects Factors underlying the characteristic inhibition of the euronal release of transmitters by tetanus and various botulinum toxins Ashton,A.C.;A.de Pavia;B.Poulain;L.Tauc;J.O.Dolly;B.R.DasGupta(ed.)
  2. J. Neurochem. v.68 Microtubules and microfilaments participate in the inhibition of synaptosomal noradrenaline release by tetanus toxin Ashton,A.C.;J.O.Dolly https://doi.org/10.1046/j.1471-4159.1997.68020649.x
  3. J. Biol. Chem. v.270 Tetanus toxin inhibits neuroexocytosis even when its Zn($2^ +$)-dependent protease activity is removed Ashton,A.C.;Y.Li;F.Doussau;U.Weller;G.Dougan;B.Poulain;J.O.Dolly https://doi.org/10.1074/jbc.270.52.31386
  4. J. Biol. Chem. v.269 The role of transglutaminase in the mechanism of action of tetanus toxin Coffield,J.A.;R.V.Considine;J.Jeyapaul;A.B.Maksymowych;R.Zhang;L.L.Simpson
  5. Eur. J. Biochem. v.154 Botulinum neurotoxin type B. Its purification, radioiodination and interaction with rat-brain synaptosomal membranes Evans,D.M.;R.S.Williams;C.C.Shone;P.Hambleton;J.Melling;J.O.Dolly https://doi.org/10.1111/j.1432-1033.1986.tb09413.x
  6. J. Biol. Chem. v.267 Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity Facchiano,F.;A.Luini
  7. J. Biol. Chem. v.268 Covalent modification of synapsin Ⅰ by a tetanus toxin-activated transglutaminase Facchiano,F.;F.Benfenati;F.Valtorta;A.Luini
  8. Trends Biochem. Sci. v.18 The transglutaminase hypothesis for the action of tetanus toxin Facchiano,F.;F.Valtorta;F.Benfenati;A.Luini https://doi.org/10.1016/0968-0004(93)90066-V
  9. FASEB J. v.5 Transglutaminase: multifunctional cross-linking enzymes that stabilize tissues Greenberg,C.S.;P.J.Birkbichler;R.H.Rice
  10. Biochimie v.82 How botulinum and tetanus neurotoxins block neurotransmitter release Humeau,Y.;F.Dousaur;N.J.Grant;B.Poulain https://doi.org/10.1016/S0300-9084(00)00216-9
  11. Trends Biochem. Sci. v.18 Tetanus and botulism neurotoxins: a new group of zinc proteases Montecucco,C.;G.Schiavo https://doi.org/10.1016/0968-0004(93)90065-U
  12. Mol. Microbiol. v.13 Mechanism of action of tetanus and botulinum neurotoxins Montecucco,C.;G.Schiavo https://doi.org/10.1111/j.1365-2958.1994.tb00396.x
  13. A sourcebook of bacterial protein toxins Molecular biology of clostridial neurotoxins Niemann,H.;J.Alouf(ed.);J.Freer(ed.)
  14. J. Neurochem. v.46 A role for transglutaminase in neurotransmitter release by rat brain synaptosomes Pastuszko,A.;D.F.Wilson;M.Erecinska https://doi.org/10.1111/j.1471-4159.1986.tb12996.x
  15. FEMS Microbiol. Lett. v.150 Cleavage of the synaptobrevin/vesicle-associated membrane protein (VAMP) of the mouse brain by the recombinant light chain of Clostridium botulinum type B toxin Rhee,S.D.;H.H.Jung;G.H.Yang;Y.S.Moon;K.H.Yang https://doi.org/10.1016/S0378-1097(97)00114-6
  16. Nature v.359 Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin Schiavo,G.;F.Benfenati;B.Poulain;O.Rossetto;P.Polverino de Laureto;B.R.DasGupta;C.Montecucco https://doi.org/10.1038/359832a0
  17. Anal. Biochem. v.153 Modification of transglutaminase assay: use of ammonium sulfate to stop the reaction Takagi,J.;Y.Saito;T.Kikuchi;Y.Inada https://doi.org/10.1016/0003-2697(86)90095-3
  18. Proc. Natl. Acad. Sci. U.S.A. v.91 Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F Yamasaki,S.;Y.G.Hu;T.Binz;A.Kalkuhl;H.Kurazono;T.Tamura;R.Jahn;E.Kandel;H.Niemann https://doi.org/10.1073/pnas.91.11.4688