کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767949 | 1050801 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mitochondrial localization of μ-calpain
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Calcium-dependent cysteine proteases, calpains, have physiological roles in cell motility and differentiation but also play a pathological role following insult or disease. The ubiquitous calpains are widely considered to be cytosolic enzymes, although there has been speculation of a mitochondrial calpain. Within a highly enriched fraction of mitochondria obtained from rat cortex and SH-SY5Y human neuroblastoma cells, immunoblotting demonstrated enrichment of the 80 kDa μ-calpain large subunit and 28 kDa small subunit. In rat cortex, antibodies against domains II and III of the large μ-calpain subunit also detected a 40 kDa fragment, similar to the autolytic fragment generated following incubation of human erythrocyte μ-calpain with Ca2+. Mitochondrial proteins including apoptosis inducing factor and mitochondrial Bax are calpain substrates, but the mechanism by which calpains gain access to these proteins is uncertain. Mitochondrial localization of μ-calpain places the enzyme in proximity to its mitochondrial substrates and to Ca2+ released from mitochondrial stores.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 2, 16 December 2005, Pages 1241-1247
Journal: Biochemical and Biophysical Research Communications - Volume 338, Issue 2, 16 December 2005, Pages 1241-1247
نویسندگان
Matthew Garcia, Vimala Bondada, James W. Geddes,