کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5922356 | 1165371 | 2010 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
PTTH-stimulated ERK phosphorylation in prothoracic glands of the silkworm, Bombyx mori: Role of Ca2+/calmodulin and receptor tyrosine kinase
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
phorbol 12-myristate acetatePKCTORPVDFRIAEcdysteroidogenesisTBSERKBSA - BSACa2+/calmodulin - Ca2 + / کالمدولینPMA - LDC هاMAPK - MAPKbovine serum albumin - آلبومین سرم گاوSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدsodium dodecylsulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اکریللید سدیم دودسیل سولفاتTris-buffered saline - تریس بافر شورRTK, Receptor tyrosine kinase - تیروزین کینازهای گیرنده ایPTTH - دبیرستانpolyvinylidene difluoride - دی فلوئورید پلی وینیلیدینradioimmunoassay - رادیوایمونواسیERK phosphorylation - فسفوریلاسیون ERKSignal transduction - هدایت سیگنالtarget of rapamycin - هدف از رپامایسینProthoracicotropic hormone - هورمون ProthoracicotropicMolecular weight - وزن مولکولیProtein kinase C - پروتئین کیناز سیmitogen-activated protein kinase - پروتئین کیناز فعال با mitogenBombyx mori - کرم ابریشمextracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش حشره شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: PTTH-stimulated ERK phosphorylation in prothoracic glands of the silkworm, Bombyx mori: Role of Ca2+/calmodulin and receptor tyrosine kinase PTTH-stimulated ERK phosphorylation in prothoracic glands of the silkworm, Bombyx mori: Role of Ca2+/calmodulin and receptor tyrosine kinase](/preview/png/5922356.png)
چکیده انگلیسی
Our previous studies showed that the prothoracicotropic hormone (PTTH) stimulated extracellular signal-regulated kinase (ERK) phosphorylation in prothoracic glands of Bombyx mori both in vitro and in vivo. In the present study, the signaling pathway by which PTTH activates ERK phosphorylation was further investigated using PTTH, second messenger analogs, and various inhibitors. ERK phosphorylation induced by PTTH was partially reduced in Ca2+-free medium. The calmodulin antagonist, calmidazolium, partially inhibited both PTTH-stimulated ERK phosphorylation and ecdysteroidogenesis, indicating the involvement of calmodulin. When the prothoracic glands were treated with agents that directly elevate the intracellular Ca2+ concentration [either A23187, thapsigargin, or the protein kinase C (PKC) activator, phorbol 12-myristate acetate (PMA)], a great increase in ERK phosphorylation was observed. In addition, it was found that PTTH-stimulated ecdysteroidogenesis was greatly attenuated by treatment with PKC inhibitors (either calphostin C or chelerythrine C). However, PTTH-stimulated ERK phosphorylation was not attenuated by the above PKC inhibitors, indicating that PKC is not involved in PTTH-stimulated ERK phosphorylation. A potent and specific inhibitor of insulin receptor tyrosine kinase, HNMPA-(AM)3, greatly inhibited the ability of PTTH to activate ERK phosphorylation and stimulate ecdysteroidogenesis. However, genistein, another tyrosine kinase inhibitor, did not inhibit PTTH-stimulated ERK phosphorylation, although it did markedly attenuate the ability of A23187 to activate ERK phosphorylation. From these results, it is suggested that PTTH-stimulated ERK phosphorylation is only partially Ca2+- and calmodulin-dependent and that HNMPA-(AM)3-sensitive receptor tyrosine kinase is involved in activation of ERK phosphorylation by PTTH.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Insect Physiology - Volume 56, Issue 1, January 2010, Pages 93-101
Journal: Journal of Insect Physiology - Volume 56, Issue 1, January 2010, Pages 93-101
نویسندگان
Shi-Hong Gu, Ju-Ling Lin, Pei-Ling Lin,