کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10770925 | 1050837 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
PrP cooperates with STI1 to regulate SOD activity in PrP-deficient neuronal cell line
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Cellular prion protein (PrPC) plays anti-apoptotic and anti-oxidative roles in apoptosis induced by serum deprivation in an immortalized prion protein gene (Prnp)-deficient neuronal cell line. The octapeptide repeat region (OR) and N-terminal half of the hydrophobic region (HR) of PrPC are indispensable for PrPC activity, but the mechanisms remain unclear. In the present study, elucidation of the mechanisms by which PrPC elicits the anti-oxidative activities was facilitated by evidence of stress-inducible protein 1 (STI1) mediating PrPC-dependent superoxide dismutase (SOD) activation. Immunoprecipitation revealed that PrPC was associated with STI1. The inhibitory peptides against PrPC-STI1 binding [STI1 pep.1 and PrPÂ (113-132)] indicated toxic activity in PrPC-expressing cells by inhibiting SOD activity but not in Prnpâ/â cells. Furthermore, OR and N-terminal half of the HR were required for the inhibitory effect of PrPÂ (113-132) but not STI1 pep.1. These data are consistent with results established with a model where OR and N-terminal half of the HR mediate the action of STI1 upon cell survival and upregulation of SOD activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 1, 4 March 2005, Pages 14-19
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 1, 4 March 2005, Pages 14-19
نویسندگان
Akikazu Sakudo, Deug-chan Lee, Shuming Li, Toyoo Nakamura, Yoshitsugu Matsumoto, Keiichi Saeki, Shigeyoshi Itohara, Kazuyoshi Ikuta, Takashi Onodera,