Journal of Muscle Research & Cell Motility

, Volume 11, Issue 4, pp 293–301

The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle

Authors

  • Ph. Gailly
    • Département de PhysiologieUniversité Catholique de Louvain, UCL 5540
  • Th. Lejeune
    • Département de PhysiologieUniversité Catholique de Louvain, UCL 5540
  • J. P. Capony
    • Centre de Recherche de Biochimie MacromoléculaireCNRS, et INSERM U 249
  • J. M. Gillis
    • Département de PhysiologieUniversité Catholique de Louvain, UCL 5540
Papers

DOI: 10.1007/BF01766667

Cite this article as:
Gailly, P., Lejeune, T., Capony, J.P. et al. J Muscle Res Cell Motil (1990) 11: 293. doi:10.1007/BF01766667

Summary

Brevin is a protein which regulates the actin gel-sol transformation: it severs F-actin filaments into shorter ones. This action is Ca-dependent and is prevented by tropomyosin. We tested the effect of brevin on isometric contractions of skinned smooth muscle (taenia coli) and noted a dramatic loss of tension that possibly reflects some F-actin fragmentation. This effect is tentatively attributed to a partial loss of tropomyosin in the skinning procedure. We also studied the effect of brevin on unloaded shortenings of skinned preparations: thin bundles and enzymatically dissociated cells. We observed a marked increase of the velocity of shortening in the presence of brevin. This effect cannot be attributed to an increased ATPase activity as the latter is slightly reduced in the presence of brevin. We interpret this result as reflecting a decrease in internal resistance to movement, possibly by solation of an actin-filamin domain.

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Copyright information

© Chapman and Hall Ltd 1990