کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803185 | 1055801 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Anisomycin induces COX-2 mRNA expression through p38MAPK and CREB independent of small GTPases in intestinal epithelial cells
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کلمات کلیدی
p38MAPKEGFCOXJnkGPCRERKGAPDHCREBc-Jun N-terminal kinase - C-Jun N-terminal kinaseG-protein coupled receptor - G-پروتئین همراه گیرندهMAPK - MAPKanisomycin - آنزومایسینcyclooxygenase - آنزیم سیکلواکسیژنازGene expression - بیان ژنCyclooxygenase-2 - سیکلوکوکسیژناز2epidermal growth factor - عامل رشد اپیدرمیmitogen-activated protein kinase - پروتئین کیناز فعال با mitogenprostaglandin - پروستاگلاندینهاextracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولیglyceraldehyde 3-phosphate dehydrogenase - گلیسرولیدید 3-فسفات دهیدروژناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Anisomycin induces COX-2 mRNA expression through p38MAPK and CREB independent of small GTPases in intestinal epithelial cells Anisomycin induces COX-2 mRNA expression through p38MAPK and CREB independent of small GTPases in intestinal epithelial cells](/preview/png/10803185.png)
چکیده انگلیسی
Cyclooxygenase (COX)-2 expression in intestinal epithelial cells is associated with colorectal carcinogenesis. COX-2 expression is induced by numerous growth factors and gastrointestinal hormones through multiple protein kinase cascades. Here, the role of mitogen activated protein kinases (MAPKs) and small GTPases in COX-2 expression was investigated. Anisomycin and sorbitol induced COX-2 expression in non-transformed, intestinal epithelial IEC-18 cells. Both anisomycin and sorbitol activated p38MAPK followed by phosphorylation of CREB. SB202190 and PD169316 but neither PD98059 nor U0126 blocked COX-2 expression and CREB phosphorylation by anisomycin or sorbitol. Clostridium difficile toxin B inhibition of small GTPases did not affect anisomycin-induced COX-2 mRNA expression or phosphorylation of p38MAPK and CREB but did inhibit sorbitol-dependent COX-2 expression and phosphorylation of p38MAPK and CREB. Angiotensin (Ang) II-dependent induction of COX-2 mRNA and induced phosphorylation of p38MAPK and CREB were inhibited by toxin B. Reduction of CREB protein in cells transfected with CREB siRNAs inhibited anisomycin-induced COX-2 expression. These results indicate that activation of p38MAPK signaling is sufficient for COX-2 expression in IEC-18 cells. Ang II and sorbitol require small GTPase activity for COX-2 expression via p38MAPK while anisomycin-induced COX-2 expression by p38MAPK does not require small GTPases. This places small GTPase activity down-stream of the AT1 receptor and hyperosmotic stress and up-stream of p38MAPK and CREB.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1745, Issue 3, 30 September 2005, Pages 393-400
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1745, Issue 3, 30 September 2005, Pages 393-400
نویسندگان
Lindsay M. Shafer, Lee W. Slice,