Autolysis of Calpain Large Subunit Inducing of Stoichiometric Heterodimer of Calpain Irreversible Dissociation
نویسنده
چکیده
'Department ofMolecular Biology, institute ofMolecular and Cellular Biosciences, Uhiversity of 7btvo, l-1-1 Yityoi, Buntvo-ku, 7bkyo 113-Oa32, lapan 20fice ofBrewing 71echnology, ()saka Regional 72Txation Bureau, 1-5-63, Otemae, Chuo-ku, ()saka City, Osaka 540-OOO& lapan 3DepartmentofApplied Biological Chemistny, and DE:partment ofAmptied Biological Engineering Graduate Sehool ofAgricuttural andLij e Sciencq Uitiver:sity of 7bkyo. 1-1-1 Ytryoi, Bunkyo-ku, 7bkyo 113-Oa32, .Jdpan `Laboratoryfor Proteolytic IVeuroscienee, RLKEN Brain Science Ihstitutq 2-1, Hirosawa, PVtiko, Saitama 351-Ol98. -lapan SDepartmentofLijle Sciencq 6raduate School ofArts and Science. Univensity of 7bdyo, Mleguro-ku, 7bkyo 153-89a2, lapan
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Stabilization of calpain large subunits by overexpression of truncated calpain small subunit in L8 myoblasts.
The objectives were to investigate the function of the small subunit in the calpain system by expression of the autolytic form of this subunit in L8 myoblasts. Rat post-autolysis small subunit (21 kDa) cDNA expression plasmid was transfected into L8 myoblasts and selected by G418 containing medium. The concentrations of cytosolic micro-calpain in transfected cells, SS2 and SS3, were found to be...
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A recent hypothesis suggests that proteolytic activity of the micromolar and millimolar Ca2+-requiring forms of the Ca2+-dependent proteinases (mu- and m-calpain, respectively) is regulated in vivo by their association with a phosphatidylinositol-containing site on the plasma membrane followed by autolysis of the proteinases. Phosphatidylinositol association lowers the Ca2+ concentration needed...
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