کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767033 | 1050696 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fe65 does not stabilize AICD during activation of transcription in a luciferase assay
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کلمات کلیدی
Fe65PNTAβNICDAPPCTFAICDBACEDAPTCho - برایChinese Hamster Ovary - تخمدان هامستر چینیAPP intracellular domain - دامنه داخل سلولی APPNotch intracellular domain - دامنه درون سلولی NotchTranscription - رونویسیluciferase - لوسیفرازamyloid precursor protein - پروتئین پیش ماده آمیلوئیβ-amyloid peptide - پپتید β-آمیلوئید
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The APP intracellular domain (AICD) could be involved in signaling via interaction with the adaptor protein Fe65, and with the histone acetyl transferase Tip60. However, the real function of AICD and Fe65 in regulation of transcription remains controversial. In this study, the human APPGal4 fusion protein was expressed in CHO cells and the transcriptional activity of AICDGal4 was measured in a luciferase-based reporter assay. AICDGal4 was stabilized by expression of Fe65 and levels of AICDGal4 controlled luciferase activity. On the contrary, when human APP was expressed in CHO cells, coexpression of Fe65 increased luciferase activity without affecting the amount of AICD fragment. AICD produced from APP was protected from degradation by orthophenanthroline, but not by lactacystine, indicating that AICD is not a substrate of the chymotryptic activity of the proteasome. It is concluded that Fe65 can control luciferase activity without stabilizing the labile AICD fragment.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 361, Issue 2, 21 September 2007, Pages 317-322
Journal: Biochemical and Biophysical Research Communications - Volume 361, Issue 2, 21 September 2007, Pages 317-322
نویسندگان
Sandra Huysseune, Pascal Kienlen-Campard, Jean-Noël Octave,