کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9001482 | 1557917 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Role of protein turnover in the activation of p38 mitogen-activated protein kinase in rat pinealocytes
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کلمات کلیدی
Jnkc-jun amino terminal kinaseAA-NATarylalkylamine-N-acetyltransferaseCycloMG132MAPK phosphatase 1MKP-1p38MAPKpKaGAPDHDMEMMAPK - MAPKMAPK kinase - MAPK کینازMKK - MCCDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده DulbeccoActinomycin - آتیینومایسینactin - اکتین cycloheximide - سیکلوهایسیمیدnorepinephrine - نوراپی نفرینProteasome - پروتئازومprotein kinase A - پروتئین کیناز Amitogen-activated protein kinase - پروتئین کیناز فعال با mitogenPineal - پنالتیglyceraldehyde-3-phosphate-dehydrogenase - گلیسرولیدید 3-فسفات دهیدروژناز
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Role of protein turnover in the activation of p38 mitogen-activated protein kinase in rat pinealocytes Role of protein turnover in the activation of p38 mitogen-activated protein kinase in rat pinealocytes](/preview/png/9001482.png)
چکیده انگلیسی
Differences in the time profiles of activation between p38MAPK and p42/44MAPK by norepinephrine (NE) in rat pinealocytes suggest involvement of mechanisms other than the phosphorylation cascades in their activation. In the present study we investigated whether protein turnover played a role in regulating p38MAPK activation in the rat pineal gland. NE stimulation caused an increase in MAPK kinase3/6 (MKK 3/6) and p38MAPK phosphorylation that occurred in the absence of changes in the mRNA or protein levels of p38MAPK or MKK3/6. The stimulatory effect of NE on phosphorylated MKK3/6 and p38MAPK, but not phosphorylated p42/44MAPK, was blocked by treatment with actinomycin or cycloheximide, indicating a requirement of transcription and translation in activation of the p38MAPK but not the p42/44MAPK pathway. Moreover, inhibition of proteasomes by clasto-lactacystin β-lactone or Z-Leu-Leu-Leu-CHO (MG132) selectively increased basal and NE-stimulated phosphorylated MKK3/6 and p38MAPK levels without affecting the mRNA or protein levels of MKK3 or p38MAPK. In contrast, the effect of proteasomal inhibition on NE-stimulated p42/44MAPK phosphorylation was inhibitory. Treatment with MG132 also reduced the decline in the phosphorylated levels of NE-stimulated MKK3/6 and p38MAPK that normally follows β-adrenergic blockade. Together, our results indicate that p38MAPK but not p42/44MAPK activation in the rat pineal gland is tightly coupled to protein synthesis and degradation. The synthesis of an activator upstream of MKK3/6 is required for the NE-activation of p38MAPK.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical Pharmacology - Volume 70, Issue 12, 5 December 2005, Pages 1840-1850
Journal: Biochemical Pharmacology - Volume 70, Issue 12, 5 December 2005, Pages 1840-1850
نویسندگان
A.K. Ho, L. McNeil, D. Terriff, D.M. Price, C.L. Chik,