کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803100 | 1055772 | 2012 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cytosolic prion protein is the predominant anti-Bax prion protein form: Exclusion of transmembrane and secreted prion protein forms in the anti-Bax function
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کلمات کلیدی
PNGaseFOPNBcl-2 associated protein XTMDF-valueGPiPrPPRLpeptide: N-glycosidase FrPrPSTErecombinant PrPeGFPOsteopontin - استئوپنتینEndo H - اندو هendoglycosidase H - اندوگلیکوزیداز HBax - باکسApoptosis - خزان یاختهایtransmembrane domain - دامنه فرابنفشdegrees of freedom - درجه آزادیcytomegalovirus - سیتومگالوویروسCMV - سیتومگالوویروسNeuroprotection - محافظت نورونی یا محافظت از عصبwild type - نوع وحشیenhanced green fluorescence protein - پروتئین فلورسانس سبز افزایش یافته استPrion protein - پروتئین پریونProlactin - پرولاکتین Prion - پریونglycosylphosphatidylinositol - گلیکوزیل فسفاتیدیلینوزیتول
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Prion protein (PrP) prevents Bax-mediated cell death by inhibiting the initial Bax conformational change that converts cytosolic Bax into a pro-apoptotic protein. PrP is mostly a glycophosphatidylinositol-anchored cell surface protein but it is also retrotranslocated into cytosolic PrP (CyPrP) or can become a type 1 or type 2 transmembrane protein. To determine the form and subcellular location of the PrP that has anti-Bax function, we co-expressed various Syrian hamster PrP (SHaPrP) mutants that favour specific PrP topologies and subcellular localization with N-terminally green fluorescent protein tagged pro-apoptotic Bax (EGFP-Bax) in MCF-7 cells and primary human neurons. Mutants that generate both CyPrP and secreted PrP (SecPrP) or only CyPrP have anti-Bax activity. Mutants that produce CtmPrP or NtmPrP lose the anti-Bax activity, despite their ability to also make SecPrP. Transmembrane-generating mutants do not produce CyPrP and both normal and cognate mutant forms of CyPrP rescue against the loss of anti-Bax activity. SecPrP-generating constructs also produce non-membrane attached SecPrP. However, this form of PrP has minimal anti-Bax activity. We conclude that CyPrP is the predominant form of PrP with anti-Bax function. These results imply that the retrotranslocation of PrP encompasses a survival function and is not merely a pathway for the proteasomal degradation of misfolded protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 2001-2012
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1783, Issue 10, October 2008, Pages 2001-2012
نویسندگان
David T.S. Lin, Julie Jodoin, Michaël Baril, Cynthia G. Goodyer, Andréa C. LeBlanc,