PKB in real terms,这个里的PKB dnf连发是什么么

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miR-200a和上皮-间质转化在结直肠癌中的研究.pdf98页
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硕士学位论文 miR．200a和上皮．间质转化在 结直肠癌中的研究 硕士研究生：吴共发 指导教师：韩慧霞教授 摘要
研究背景： 结直肠癌是我国最常见的恶性肿瘤之一，由于早期发现和治疗方法的进步，
结直肠癌的死亡率在过去三十年有一定程度下降，但随着人们生活水平的提高 以及生活方式的改变，近年来我国的结直肠癌发病率却有所上升。侵袭转移是
结直肠癌治疗失败导致患者死亡的最主要原因。因此，探讨与结直肠癌侵袭转
移密切相关的因素势在必行。 恶性肿瘤的发生和发展是一个多因素、多步骤的复杂生物学行为过程。对
恶性肿瘤发生、发展、浸润及转移机制和寻求新的特效治疗方法与手段一直是
瘤研究的热点。miRNA是真核生物细胞中一类长度约为18．24核苷酸的内源性
非编码小分子RNA。它由DNA转录产生，但并不翻译蛋白质，而是在蛋白质
合成中起调节其他基因的功能，是调控其他蛋白质编码基因的基因。miRNA通 7．untranslated
过与靶基因mRNA的37．非编码区 3 region，3’-UTR 以完全
或不完全互补配对的方式结合，降解或者抑制靶基因mRNA。miRNA与基因之
间的作用是错综复杂的，一个miRNA可调控多个基因的mRNAs，一个基因的
mRNAs也可由多个miRNAs调控，此外，基因也可参与对miRNAs的调控。 摘要
miR．200a,miR一200b，miR．200c，miR．114，miR．429 的一员在多种肿瘤中表达下 transition，EMT 过程，
调，主要通过调控上皮．间质转化 epithelial．mesenchymal
对肿瘤的侵袭转移起到关键作用。肿瘤细胞EMT的发生包括诸多因素，主要有
转录因子表达上调以及各种信号通路激活。大量研究表明AKT和ERK信号通
路的激活在结直肠癌EMT的发生中起到重要作用，另外有报道称在人肝癌细
正在加载中，请稍后...Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding.
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2000 Oct 6;275(40):30901-6.Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding.1, , .1Department of Cell Biology & Anatomy, New York Medical College, Valhalla, New York 10595, USA.AbstractThe mechanism of outside-in signaling by integrins parallels that for growth factor receptors. In both pathways, phosphorylation of a cytoplasmic segment on tyrosine generates a docking site for proteins containing Src homology 2 (SH2) and phosphotyrosine binding domains. We recently observed that phosphorylation of a threonine (Thr-753), six amino acids proximal to tyrosine 759 in beta(3) of the platelet specific integrin alpha(IIb)beta(3), inhibits outside-in signaling through this receptor. We hypothesized that the presence of phosphothreonine 753 either renders beta(3) a poor substrate for tyrosine kinases or inhibits the docking capabilities of the tyrosyl-phosphorylated form of beta(3.) The first alternative was tested by comparing the phosphorylation of beta(3) model peptides by the tyrosine kinase pp60(c-src) and we found that the presence of a phosphate group on a residue corresponding to Thr-753 did not detectably alter the kinetics of tyrosine phosphorylation. However, the presence of phosphate on this threonine inhibited the binding of Shc to tyrosyl-phosphorylated beta(3) peptide. The inhibitory effect of the phosphate group could be mimicked by substituting an aspartic acid for Thr-753, suggesting that a negative charge at this position modulates the binding of Shc and possibly other phosphotyrosine binding domain- and SH2-containing proteins. A survey of several protein kinases revealed that Thr-753 was avidly phosphorylated by PDK1 and Akt/PKB in vitro. These observations suggest that activation of PDK1 and/or Akt/PKB in platelets may modulate the binding activity and/or specificity of beta(3) for signaling molecules.PMID:
[PubMed - indexed for MEDLINE]
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