کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9886547 | 1537834 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The gene encoding the human ileal bile acid-binding protein (I-BABP) is regulated by peroxisome proliferator-activated receptors
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کلمات کلیدی
Direct Repeat 1EMSABareileal bile acid-binding proteinI-BABPRetinoid-X-receptorfarnesoid-x-receptorCYP8B1liver-X-receptorCYP27A1CYP7A1DR1SREBPCATPPARRXRCDCAFXRLXRAsbt - آزبستElectrophoretic mobility shift assay - آزمون تحرک تحرک الکتروفورزPPRE - ارسالsterol 12α-hydroxylase - استرول 12α-هیدروکسیلازsterol 27-hydroxylase - استرول 27-هیدروکسیلازChenodeoxycholic acid - اسید ChenodeoxycholicBile acid - اسید صفراویapical sodium-dependent bile acid transporter - اپوکسی سدیم وابسته به پروتئین اسید صفراFibrate - فیبر کردنsterol regulatory element-binding proteins - پروتئین های الزم برای تنظیم عصاره استرولchloramphenicol acetyl transferase - کلرامفنیکول استیل ترانسفرازcholesterol 7α-hydroxylase - کلسترول 7α-هیدروکسیلازPeroxisome proliferator-activated receptors - گیرنده فعال فعال پروکسیوم
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Peroxisome proliferator-activator receptors (PPAR) are involved in cholesterol homeostasis through the regulation of bile acids synthesis, composition, and reclamation. As ileal bile acid-binding protein (I-BABP) is thought to play a crucial role in the enterohepatic circulation of bile acids, we investigated whether I-BABP gene expression could also be affected by PPAR. Indeed, treatment with the PPARα-PPARβ/δ agonist bezafibrate led to the up-regulation of I-BABP mRNA levels in the human intestine-derived Caco-2 cells. Cotransfections of the reporter-linked human I-BABP promoter (hI-BABPâ2769/+44) together with PPAR and RXR expression vectors demonstrated that the fibrate-mediated induction of the I-BABP gene is dependent on PPARα or PPARβ/δ. Using progressive 5â² deletions of the hI-BABP promoter and sequence analysis, we identified a putative PPAR-binding site located at the position â198 and â186 upstream of the transcription initiation site. Electrophoretic mobility shift assays showed that the PPAR/RXR heterodimer can specifically bind to this PPRE-like motif. The deletion of the PPRE within the hI-BABP promoter abolished the PPAR-mediated transactivation in transient transfection assays. The regulation of the I-BABP promoter by PPAR appears species-specific, as the mouse I-BABP promoter, which lacks a conserved PPRE, was not responsive to exogenous PPAR expression in the presence of bezafibrate. Our findings show that the I-BABP gene may be a novel target for PPAR in humans and further emphasize the role for PPAR in the control of bile acid homeostasis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1735, Issue 1, 15 June 2005, Pages 41-49
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1735, Issue 1, 15 June 2005, Pages 41-49
نویسندگان
J.F. Landrier, C. Thomas, J. Grober, I. Zaghini, V. Petit, H. Poirier, I. Niot, P. Besnard,