Autolysis of Calpain Large Subunit Inducing Irreversible Dissociation of Stoichiometric Heterodimer of Calpain.

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  • KITAGAKI Hiroshi
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo Office of Brewing Technology, Osaka Regional Taxation Bureau
  • TOMIOKA Shigeo
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo
  • YOSHIZAWA Toshio
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo
  • SORIMACHI Hiroyuki
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo Department of Applied Biological Chemistry, and Department of Applied Biological Engineering, Graduate School of Agricultural and Life Science, University of Tokyo
  • SAIDO Takaomi C.
    Laboratory for Proteolytic Neuroscience, RIKEN Brain Science Institute
  • ISHIURA Shoichi
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo Department of Life Science, Graduate School of Arts and Science, University of Tokyo
  • SUZUKI Koichi
    Department of Molecular Biology, Institute of Molecular and Cellular Biosciences, University of Tokyo

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  Calpain, a calcium dependent cysteine protease, consists of a catalytic large subunit and a regulatory small subunit. Two models have been proposed to explain calpain activation: an autolysis model and a dissociation model. In the autolysis model, the autolyzed form is the active species, which is sensitized to Ca2+. In the dissociation model, dissociated large subunit is the active species. We have reported that the Ca2+ concentration regulates reversible dissociation of subunits. We found further that in chicken μ/m-calpain autolysis of the large subunit induces irreversible dissociation from the small subunit as well as activation. So we could propose a new mechanism for activation of the calpain by combining our findings. Our model insists that autolyzed large subunit remains dissociated from the small subunit even after the removal of Ca2+ to keep it sensitized to Ca2+. This model could be expanded to other calpains and give a new perspective on calpain activation.<br>

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