Dataset Information

Tripartite Motif-Containing Protein 59 (TRIM59) Promotes Epithelial Ovarian Cancer Progression via the Focal Adhesion Kinase(FAK)/AKT/Matrix Metalloproteinase (MMP) Pathway.

ABSTRACT: BACKGROUND The tripartite motif-containing protein 59 (TRIM59) is an important member of the TRIM family, which regulates biological processes. However, the relationship between TRIM59 and epithelial ovarian cancer (EOC) is not clear. MATERIAL AND METHODS The TRIM59 expression level was detected in EOC tissues and cell lines. CCK-8 assay, Transwell assay, and wound healing assay were performed to determine the effects of TRIM59 on EOC cell proliferation, invasion, and migration. Silencing of the expression of TRIM59 in EOC cells and expression of FAK/AKT/MMP pathway-related protein were detected by Western blot analysis. RESULTS Through bioinformatics analysis, TRIM59 was found to be highly expressed in EOC and was correlated with prognosis of patients. TRIM59 was upregulated in EOC tissues and cells. Silencing TRIM59 significantly suppressed EOC cell proliferation, migration, and invasion. In terms of molecular mechanism, silencing TRIM59 inhibited the FAK/AKT/MMP pathway. CONCLUSIONS TRIM59 is a biomarker for the prognosis of EOC. It is also oncogenic and a potential target for EOC therapy.

SUBMITTER: Zhang P

PROVIDER: S-EPMC6519306 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Tripartite Motif-Containing Protein 59 (TRIM59) Promotes Epithelial Ovarian Cancer Progression via the Focal Adhesion Kinase(FAK)/AKT/Matrix Metalloproteinase (MMP) Pathway.

Zhang Pei P Zhang Hengliang H Wang Yan Y Zhang Pan P Qi Yan Y

Medical science monitor : international medical journal of experimental and clinical research 20190507

BACKGROUND The tripartite motif-containing protein 59 (TRIM59) is an important member of the TRIM family, which regulates biological processes. However, the relationship between TRIM59 and epithelial ovarian cancer (EOC) is not clear. MATERIAL AND METHODS The TRIM59 expression level was detected in EOC tissues and cell lines. CCK-8 assay, Transwell assay, and wound healing assay were performed to determine the effects of TRIM59 on EOC cell proliferation, invasion, and migration. Silencing of the ...[more]

PMID: 31062766

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Project description:PURPOSE: Regulation of lens development involves an intricate interplay between growth factor (e.g. FGF and TGFbeta) and extracellular matrix (ECM) signaling pathways. Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase that plays key roles in transmitting ECM signals by integrins. In this study, we delineated patterns of FAK expression and tyrosine phosphorylation (Y397) in the developing lens and investigated its regulation by FGF2. We also examined FAK expression and activation during disrupted fiber differentiation in mice expressing a dominant-negative TGFbeta receptor. METHODS: FAK expression and activation (phosphorylation on Y397) was studied in embryonic and postnatal rodent lenses by in situ hybridization, immunofluorescence, and western blotting. Rat lens explants were used to investigate the effects of FGF2 on FAK expression and activation. Immunofluorescence and western blotting were used to examine FAK expression and phosphorylation in transgenic mice that express a dominant-negative TGFbeta receptor. RESULTS: FAK is widely expressed and phosphorylated during embryonic stages of lens morphogenesis and differentiation. However, in postnatal lenses its expression and activation becomes restricted to the posterior germinative zone and the transitional zone at the lens equator. While both NH2- and COOH-terminal antibodies revealed cytoplasmic and membrane-associated staining in lens cells, the NH2-terminal antibody also showed FAK was present in fiber cell nuclei. In vitro, FAK expression and phosphorylation on Y397 were increased by concentrations of FGF2 that initiate lens epithelial cell migration (10 ng/ml) and differentiation (50 ng/ml) but not proliferation (5 ng/ml). Moreover, reactivity for Y397 phosphorylated FAK is prominent in the nuclei of differentiating fibers both in vivo and in vitro. Disruption of TGFbeta-like signals by ectopic expression of a dominant-negative TGFbeta receptor (TbetaRII(D/N)) results in abnormal lens fiber differentiation in transgenic mice. While FAK expression is initiated normally in the posterior germinative zone of TbetaRII(D/N) transgenic lenses, as fiber differentiation proceeds, FAK becomes localized to a perinuclear compartment, decreases its association with the cytoskeleton and is poorly phosphorylated on Y(397). CONCLUSIONS: FAK is widely expressed and activated during early lens morphogenesis. During secondary lens fiber differentiation, FAK is expressed and phosphorylated on Y397 as epithelial cells exit the cell cycle, initiate migration at the equator, and undergo differentiation in the transitional zone. During terminal fiber differentiation an NH2-terminal fragment of FAK, including Y397, is translocated to the nucleus. The expression, activation, and nuclear localization of FAK are regulated, at least partly, by FGF2. FAK activity and subcellular localization are also modulated by TGFbeta-like signals. In fiber cells of TbetaRII(D/N) transgenic lenses, FAK is abnormally retained in a perinuclear compartment, loses its association with the cytoskeleton, and is poorly phosphorylated. These data suggest that integrin signaling via FAK plays important roles during lens differentiation, mediated by FGFs and TGFbeta-superfamily signals.

Dataset Information

Tripartite Motif-Containing Protein 59 (TRIM59) Promotes Epithelial Ovarian Cancer Progression via the Focal Adhesion Kinase(FAK)/AKT/Matrix Metalloproteinase (MMP) Pathway.

Publications

Tripartite Motif-Containing Protein 59 (TRIM59) Promotes Epithelial Ovarian Cancer Progression via the Focal Adhesion Kinase(FAK)/AKT/Matrix Metalloproteinase (MMP) Pathway.

Similar Datasets

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