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Fibromodulin FMOD promotes oral squamous cell carcinoma via activating EGFR signaling axis

ABSTRACT: Fibromodulin FMOD promotes oral squamous cell carcinoma via activating EGFR signaling axis

PROVIDER: PRJNA946151 | ENA |

REPOSITORIES: ENA

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Fibromodulin FMOD promotes oral squamous cell carcinoma via activating EGFR signaling axis

Project description:As a Class II small leucine-rich proteoglycan, fibromodulin (FMOD) plays critical roles in collagen fibrillogenesis and angiogenesis. However, the biological function of FMOD in oral squamous cell carcinoma remains unknown to date. In this study, immunohistochemistry and immunofluorescence assays identified that FMOD protein was located in cytoplasm and nucleus and was overexpressed in OSCC tissues and cell lines. Clinical analysis confirmed that FMOD overexpression showed a significant association with malignant progression (P=0.011) and lymph node metastasis (P=0.032) in OSCC patients. Moreover, loss-of-function studies verified that knockdown of FMOD significantly inhibited OSCC growth and metastasis in vitro and in vivo. Mechanismly, RNA sequencing studies further confirmed that. Knockdown of FMOD expression inhibited OSCC cell proliferation, migration, invasion, and tumor growth probably through altering transcriptome leading to active cell cycle, down-regulating Cell adhesion molecules and ECM-receptor interaction and through inhibiting EGFR-ERK and EGFR-AKT pathways.

2023-08-31 | GSE227643 | GEO

AXL mediates resistance to PI3Kα inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas.

Project description:Phosphoinositide-3-kinase (PI3K)-α inhibitors are clinically active in squamous carcinoma (SCC) of the head and neck (H&N) bearing mutations or amplification of PIK3CA. We aimed to identify potential mechanism of resistance and have observed that SCCs cells overcome the antitumor effects of the PI3Kα inhibitor BYL719 by maintaining PI3K-independent activation of the mammalian target of rapamycin (mTOR). The persistent mTOR activation is mediated by the tyrosine kinase receptor AXL. We found that AXL is overexpressed in resistant tumors, dimerizes with the epidermal growth factor receptor (EGFR), phosphorylates EGFR tyrosine 1173, resulting in activation of phospholipase Cγ (PLCγ)- protein kinase C (PKC) that, in turn, activates mTOR. Finally, simultaneous treatment with PI3Kα and either EGFR, AXL or PKC inhibitors reverts this resistance. RNAseq from acquired resistant cells CAL33B, K180B were compared to their parental counterpart CAL33 and K180, respectively. K180 is a shortcut of KYSE180, and B stands for BYL719. Duplicate of parental sensitive cells and K180B, and triplicate for CAL33B.

2015-04-12 | E-GEOD-61515 | biostudies-arrayexpress

N-Glycosylation of the Epidermal Growth Factor Receptor (EGFR) Derived from Human Oral Squamous Carcinoma Cells with beta-Catenin/CREB-Binding Protein (CBP) Inhibition

Project description:Head and neck squamous cell carcinoma (HNSCC) is the sixth most common malignancy in the world; oral squamous cell carcinomas (OSCC) account for the majority of HNSCC cases. A major driver of OSCC is the epidermal growth factor receptor (EGFR), a receptor tyrosine kinase (RTK) with 12 N-glycosylation sites whose activity is aberrantly upregulated in 80-90% of tumors. EGFR antennary-fucosylated glycans have been shown to suppress EGFR dimerization and signaling in lung adenocarcinoma. High levels of fucosylated glycan epitopes have also been observed in OSCC, but invasive regions lose expression of linkage-specific fucosylated epitopes, suggesting that certain fucosylated glycans are involved in the suppression of cell growth and invasion. We found that EGFR from metastatic HSC-3 cells has low levels of fucosylated N-glycans, while EGFR from non-metastatic CAL27 cells shows higher levels of fucosylation at multiple EGFR glycosylation sites including sites N420 and N579, via nUPLC-MS/MS. In cell culture and in mouse tumor xenografts, treatment with ICG-001, a small molecule inhibitor of the interaction between nuclear -catenin and CREB-binding protein (CBP) resulted in higher expression of FUT2 and FUT3, higher fucosylation of EGFR at sites N420 and N579, and decreased EGFR abundance. In addition, we have performed in-depth characterization of multiply-fucosylated N-glycans via glycopeptide tandem mass spectrometry to understand which fucosylated glycan epitopes are involved in the observed effect.

2020-03-26 | PXD017060 | Pride

DLEU1 promotes oral squamous cell carcinoma progression through activating interferon-stimulated genes

Project description:DLEU1 promotes oral squamous cell carcinoma progression through activating interferon-stimulated genes

| PRJNA739720 | ENA

AXL mediates resistance to PI3Kα inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas.

2015-04-12 | GSE61515 | GEO

Canine oral squamous cell carcinoma

Project description:An investigation of canine oral squamous cell carcinomas

2024-06-30 | PRJEB77007 | EVA

EGFR activity addiction facilitates anti-ERBB based combination treatment of squamous bladder cancer

Project description:Recent findings suggested a benefit of anti-EGFR therapy for basal-like muscle invasive bladder cancer (MIBC). However, impact on bladder cancer with substantial squamous differentiated (Sq-BLCA) and especially pure squamous cell carcinoma (SCC) remains unknown. Therefore, we comprehensively characterized pure and mixed Sq-BLCA (n=125) on genetic and protein expression level, and performed functional pathway and drug-response analyses with cell line models and isolated primary SCC (p-SCC) cells of the human urinary bladder. We identified abundant EGFR expression in 95% of Sq-BLCA without evidence for activating EGFR mutations. Both SCaBER and p-SCC cells were sensitive to EGFR tyrosine kinase inhibitors (TKIs: erlotinib and gefitinib). Combined treatment with anti-EGFR TKIs and varying chemotherapeutics led to a concentration-dependent synergism in SCC cells according to the Chou-Talalay method. In addition, siRNA knockdown of EGFR impaired SCaBER viability suggesting a putative ‘‘Achilles heel’’ of Sq-BLCA. The observed effects seem Sq-BLCA-specific since non-basal urothelial cancer cells were characterized by poor TKI sensitivity associated with a short-term feedback response by upregulating EGFR and ERBB3 expression. Hence, our findings give novel insights into a crucial, Sq-BLCA-specific role of the ERBB signaling pathway proposing improved effectiveness of combined anti-EGFR and chemotherapeutic regimens in squamous bladder cancers with wild-type EGFR-overexpression.

2023-03-12 | GSE146975 | GEO

DLEU1 promotes oral squamous cell carcinoma progression through activating interferon-stimulated genes [microarray]

Project description:DLEU1 promotes oral squamous cell carcinoma progression through activating interferon-stimulated genes [microarray]

| PRJNA739714 | ENA

Gene expression signatures in EGFR-deleted oral squamous cell carcinoma (OSCC) cell lines

Project description:Gene expression signatures in EGFR-deleted oral squamous cell carcinoma (OSCC) cell lines

| PRJNA922911 | ENA

Expression data from fibroblasts derived from human normal oral mucosa, oral dysplasia and oral squamous cell carcinoma

Project description:Identification of genes that are differentially regulated in fibroblasts derived from dysplastic oral mucosa and oral squamous cell carcinoma compared to fibroblasts derived from normal oral mucosa. Affymetrix microarrays were used to define differential gene expression. Populations of fibroblasts were isolated from human normal oral mucosa, oral dysplasia and oral squamous cell carcinoma, maintained in 3D collagen I biomatrices, RNA extracted and processed for Affymetrix arrays. Fibroblasts maintained as monolayers were also included as comparators.

2013-12-01 | E-GEOD-38517 | biostudies-arrayexpress

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