Autolysis, Ca2+ Requirement, and Heterodimer Stability in m-Calpain
نویسندگان
چکیده
منابع مشابه
The role of autolysis in activity of the Ca2+-dependent proteinases (mu-calpain and m-calpain).
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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'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 an...
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Proteolytic activity in sheared human umbilical vein endothelial cells (HUVECs) was measured using a fluorogenic substrate and laser scanning confocal microscopy to clarify the key role of an intracellular Ca(2+)-sensitive protease, calpain, in these cells in response to shear stress. Within physiological shear range, activity in the cells was enhanced in shear-dependent fashion. Short interfer...
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15 صفحه اولmu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
mu-Calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that mu-calpain becomes proteolytically active in the presence of 2-200 microM Ca2+. Although calpain-3 is poorly understood, autolysis is thought to result in its...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1997
ISSN: 0021-9258
DOI: 10.1074/jbc.272.17.11268