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磷脂酰肌醇3激酶/蛋白激酶B信号通路增强了Smad3刺激的系膜细胞I型胶原蛋白表达,以响应转化生长因子-β1。

The phosphatidylinositol 3-kinase/Akt pathway enhances Smad3-stimulated mesangial cell collagen I expression in response to transforming growth factor-beta1.

作者信息

Runyan Constance E, Schnaper H William, Poncelet Anne-Christine

机构信息

Department of Pediatrics, Northwestern University, Chicago, Illinois 60611, USA.

出版信息

J Biol Chem. 2004 Jan 23;279(4):2632-9. doi: 10.1074/jbc.M310412200. Epub 2003 Nov 10.

Abstract

Transforming growth factor (TGF)-beta has been associated with renal glomerular matrix accumulation. We previously showed that Smad3 promotes COL1A2 gene activation by TGF-beta1 in human glomerular mesangial cells. Here, we report that the PI3K/Akt pathway also plays a role in TGF-beta1-increased collagen I expression. TGF-beta1 stimulates the activity of phosphoinositide-dependent kinase (PDK)-1, a downstream target of PI3K, starting at 1 min. Akt, a kinase downstream of PDK-1, is phosphorylated and concentrates in the membrane fraction within 5 min of TGF-beta1 treatment. The PI3K inhibitor LY294002 decreases TGF-beta1-stimulated alpha1(I) and alpha2(I) collagen mRNA expression. Similarly, LY294002 or an Akt dominant negative construct blocks TGF-beta1 induction of COL1A2 promoter activity. However, PI3K stimulation alone is not sufficient to increase collagen I expression, since neither a constitutively active p110 PI3K construct nor PDGF, which induces Akt phosphorylation, is able to stimulate COL1A2 promoter activity or mRNA expression, respectively. LY294002 inhibits stimulation of COL1A2 promoter activity by Smad3. In a Gal4-LUC assay system, blockade of the PI3K pathway significantly decreases TGF-beta1-induced transcriptional activity of Gal4-Smad3. Activity of SBE-LUC, a Smad3/4-responsive construct, is stimulated by over-expression of Smad3 or Smad3D, in which the three C-terminal serine phospho-acceptor residues are mutated. This induction is blocked by LY294002, suggesting that inhibition of the PI3K pathway decreases Smad3 transcriptional activity independently of C-terminal serine phosphorylation. However, TGF-beta1-induced total serine phosphorylation of Smad3 is decreased by LY294002, suggesting that Smad3 is phosphorylated by the PI3K pathway at serine residues other than the direct TGF-beta receptor I target site. Thus, although the PI3K-PDK1-Akt pathway alone is insufficient to stimulate COL1A2 gene transcription, its activation by TGF-beta1 enhances Smad3 transcriptional activity leading to increased collagen I expression in human mesangial cells. This cross-talk between the Smad and PI3K pathways likely contributes to TGF-beta1 induction of glomerular scarring.

摘要

转化生长因子(TGF)-β与肾小球基质积聚有关。我们先前表明,Smad3在人肾小球系膜细胞中促进TGF-β1介导的COL1A2基因激活。在此,我们报告PI3K/Akt信号通路在TGF-β1诱导的I型胶原蛋白表达中也发挥作用。TGF-β1在1分钟时开始刺激磷酸肌醇依赖性激酶(PDK)-1的活性,PDK-1是PI3K的下游靶点。PDK-1下游的激酶Akt在TGF-β1处理5分钟内发生磷酸化并集中在膜组分中。PI3K抑制剂LY294002可降低TGF-β1刺激的α1(I)和α2(I)胶原蛋白mRNA表达。同样,LY294002或Akt显性负性构建体可阻断TGF-β1诱导的COL1A2启动子活性。然而,单独的PI3K刺激不足以增加I型胶原蛋白表达,因为组成型活性p110 PI3K构建体或诱导Akt磷酸化的血小板衍生生长因子(PDGF)均不能分别刺激COL1A2启动子活性或mRNA表达。LY294002可抑制Smad3对COL1A2启动子活性的刺激。在Gal4-LUC检测系统中,PI3K信号通路的阻断显著降低TGF-β1诱导的Gal4-Smad3转录活性。Smad3/4反应性构建体SBE-LUC的活性可被Smad3或Smad3D(其中三个C末端丝氨酸磷酸化受体残基发生突变)的过表达所刺激。LY294002可阻断这种诱导,这表明PI3K信号通路的抑制可独立于C末端丝氨酸磷酸化降低Smad3转录活性。然而,LY294002可降低TGF-β1诱导的Smad3总丝氨酸磷酸化,这表明Smad3在直接的TGF-β受体I靶点以外的丝氨酸残基上被PI3K信号通路磷酸化。因此,尽管单独的PI3K-PDK1-Akt信号通路不足以刺激COL1A2基因转录,但其被TGF-β1激活可增强Smad3转录活性,导致人系膜细胞中I型胶原蛋白表达增加。Smad和PI3K信号通路之间的这种相互作用可能有助于TGF-β1诱导肾小球瘢痕形成。

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