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热心网友 时间：2024-10-31 08:19

Fibronectin induces endothelial cell migration through β1 integrin and Src-dependent phosphorylation of fibroblast growth factor receptor-1 at tyrosines 653/654 and 766.Zou L, Cao S, Kang N, Huebert RC, Shah VH.SourceGastroenterology Research Unit and Cancer Cell Biology Program, Mayo Clinic, Rochester, Minnesota 55905, USA.
Abstract
The extracellular matrix microenvironment regulates cell phenotype and function. One mechanism by which this is achieved is the transactivation of receptor tyrosine kinases by specific matrix molecules. Here, we demonstrate that the provisional matrix protein, fibronectin (FN), activates fibroblast growth factor (FGF) receptor-1 (FGFR1) independent of FGF ligand in liver endothelial cells. FN activation of FGFR1 requires β1 integrin, as evidenced by neutralizing antibody and siRNA-based studies. Complementary genetic and pharmacologic approaches identify that the non-receptor tyrosine kinase Src is required for FN transactivation of FGFR1. Whereas FGF ligand-induced phosphorylation of FGFR1 preferentially activates ERK, FN-induced phosphorylation of FGFR1 preferentially activates AKT, indicating differential downstream signaling of FGFR1 in response to alternate stimuli. Mutation analysis of known tyrosine residues of FGFR1 reveals that tyrosine 653/654 and 766 residues are required for FN-FGFR1 activation of AKT and chemotaxis. Thus, our study mechanistically dissects a new signaling pathway by which FN achieves endothelial cell chemotaxis, demonstrates how differential phosphorylation profiles of FGFR1 can achieve alternate downstream signals, and, more broadly, highlights the diversity of mechanisms by which the extracellular matrix microenvironment regulates cell behavior through transactivation of receptor tyrosine kinases.是这个吗
纤连蛋白通过β1整合素和Src的依赖性磷酸化的成纤维细胞生长因子受体酪氨酸653／654和766在诱导内皮细胞迁移。

邹莉，曹雪芹，康N，Huebert RC，沙阿VH。

sourcegastroenterology研究单位和癌细胞生物学程序，梅奥诊所，罗切斯特，明尼苏达55905，美国。

摘要

细胞外基质的微环境调节细胞的表型和功能。一个机制，这是实现由特定的基质分子的受体酪氨酸激酶的激活作用。在这里，我们表明，临时基质蛋白，纤连蛋白（FN），激活成纤维细胞生长因子（FGF）受体（FGFR1）独立的FGF配体在肝脏内皮细胞。FGFR1蛋白的激活需要β1整合素，作为证明的中和抗体和siRNA为基础的研究。互补基因和药物的方法确定非受体酪氨酸激酶Src是FN激活FGFR1的要求。而FGF配体诱导的磷酸化FGFR1优先激活ERK，FN诱导磷酸化FGFR1优先激活Akt，指示响应FGFR1交替刺激下游信号微分。已知的FGFR1酪氨酸残基的突变分析表明，酪氨酸653／654和766残基是需要激活Akt和趋化fn-fgfr1。因此，我们的研究机理剖析一个新的信号转导通路的FN获得血管内皮细胞的趋化性，论证了FGFR1微分磷酸化配置可以实现备用的下游信号，和，更广泛地说，集锦机制的多样性，细胞外基质微环境通过酪氨酸激酶受体的转录调节细胞的行为。
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热心网友 时间：2024-10-31 08:17

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热心网友 时间：2024-10-31 08:20

Fibronectin induces endothelial cell migration through β1 integrin and Src-dependent phosphorylation of fibroblast growth factor receptor-1 at tyrosines 653/654 and 766.Zou L, Cao S, Kang N, Huebert RC, Shah VH.SourceGastroenterology Research Unit and Cancer Cell Biology Program, Mayo Clinic, Rochester, Minnesota 55905, USA.
Abstract
The extracellular matrix microenvironment regulates cell phenotype and function. One mechanism by which this is achieved is the transactivation of receptor tyrosine kinases by specific matrix molecules. Here, we demonstrate that the provisional matrix protein, fibronectin (FN), activates fibroblast growth factor (FGF) receptor-1 (FGFR1) independent of FGF ligand in liver endothelial cells. FN activation of FGFR1 requires β1 integrin, as evidenced by neutralizing antibody and siRNA-based studies. Complementary genetic and pharmacologic approaches identify that the non-receptor tyrosine kinase Src is required for FN transactivation of FGFR1. Whereas FGF ligand-induced phosphorylation of FGFR1 preferentially activates ERK, FN-induced phosphorylation of FGFR1 preferentially activates AKT, indicating differential downstream signaling of FGFR1 in response to alternate stimuli. Mutation analysis of known tyrosine residues of FGFR1 reveals that tyrosine 653/654 and 766 residues are required for FN-FGFR1 activation of AKT and chemotaxis. Thus, our study mechanistically dissects a new signaling pathway by which FN achieves endothelial cell chemotaxis, demonstrates how differential phosphorylation profiles of FGFR1 can achieve alternate downstream signals, and, more broadly, highlights the diversity of mechanisms by which the extracellular matrix microenvironment regulates cell behavior through transactivation of receptor tyrosine kinases.是这个吗
纤连蛋白通过β1整合素和Src的依赖性磷酸化的成纤维细胞生长因子受体酪氨酸653／654和766在诱导内皮细胞迁移。

邹莉，曹雪芹，康N，Huebert RC，沙阿VH。

sourcegastroenterology研究单位和癌细胞生物学程序，梅奥诊所，罗切斯特，明尼苏达55905，美国。

摘要

细胞外基质的微环境调节细胞的表型和功能。一个机制，这是实现由特定的基质分子的受体酪氨酸激酶的激活作用。在这里，我们表明，临时基质蛋白，纤连蛋白（FN），激活成纤维细胞生长因子（FGF）受体（FGFR1）独立的FGF配体在肝脏内皮细胞。FGFR1蛋白的激活需要β1整合素，作为证明的中和抗体和siRNA为基础的研究。互补基因和药物的方法确定非受体酪氨酸激酶Src是FN激活FGFR1的要求。而FGF配体诱导的磷酸化FGFR1优先激活ERK，FN诱导磷酸化FGFR1优先激活Akt，指示响应FGFR1交替刺激下游信号微分。已知的FGFR1酪氨酸残基的突变分析表明，酪氨酸653／654和766残基是需要激活Akt和趋化fn-fgfr1。因此，我们的研究机理剖析一个新的信号转导通路的FN获得血管内皮细胞的趋化性，论证了FGFR1微分磷酸化配置可以实现备用的下游信号，和，更广泛地说，集锦机制的多样性，细胞外基质微环境通过酪氨酸激酶受体的转录调节细胞的行为。
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热心网友 时间：2024-10-31 08:21

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