Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Defective N-Glycosylation of IL6 Induces Metastasis and Tyrosine Kinase Inhibitor Resistance in Lung Cancer

ABSTRACT: Defective N-Glycosylation of IL6 Induces Metastasis and Tyrosine Kinase Inhibitor Resistance in Lung Cancer

PROVIDER: PRJNA1123684 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

Defective N-Glycosylation of IL6 Induces Metastasis and Tyrosine Kinase Inhibitor Resistance in Lung Cancer

Project description:The biological consequences of various IL-6 glycoforms are unknown. To uncover the function of N-glycosylation of IL-6 in lung cancer, we compare the gene expression profiles in NSCLC cells induced by conditioned medium containing IL-6 with complete N-glycosylation (NG-IL6) or defective N-glycosylation (deNG-IL6).

2024-07-16 | GSE269782 | GEO

N-Glycosylation-Defective IL6 Alternatively Activates the SRC-YAP-SOX2 Axis to Drive Metastasis and EGFR TKI Resistance

Project description:The IL6-GP130-STAT3 pathway facilitates lung cancer progression and resistance to tyrosine kinase inhibitors. Although glycosylation alters the stability of GP130, its effect on the ligand IL6 remains unclear. We herein found that N-glycosylated IL6, especially at Asn73, primarily stimulates JAK-STAT3 signaling and prolongs STAT3 phosphorylation, whereas N-glycosylation-defective IL6 (deNG-IL6) induces shortened STAT3 activation and alters the downstream signaling preference for the SRC-YAP-SOX2 axis. This signaling shift induced EMT and migration in vitro and metastasis in vivo, which were suppressed by targeted inhibitors and shRNAs against SRC, YAP, and SOX2. Osimertinib-resistant lung cancer cells secreted a large amount of deNG-IL6 through reduced N-glycosyltransferase gene expression, leading to clear SRC-YAP activation. deNG-IL6 contributes to drug resistance, as confirmed by in silico analysis of cellular and clinical transcriptomes and signal expression in patient specimens. Therefore, the N-glycosylation status of IL6 not only affects cell behaviors but also shows promise in monitoring the dynamics of lung cancer evolution.

2025-01-18 | PXD051771 | Pride

Tyrosine Kinase Inhibitor Cardiotoxicity

Project description:Tyrosine Kinase Inhibitor Cardiotoxicity

| PRJNA352077 | ENA

Fms-like tyrosine kinase 3 (Flt3) contributes to a receptor tyrosine kinase signature regulating the cardiac side population

Project description:Fms-like tyrosine kinase 3 (Flt3) contributes to a receptor tyrosine kinase signature regulating the cardiac side population

| PRJNA706448 | ENA

Fms-like tyrosine kinase 3 (Flt3) contributes to a receptor tyrosine kinase signature regulating the cardiac side population

Project description:Fms-like tyrosine kinase 3 (Flt3) is a regulator of hematopoietic progenitor cells. It is a target of tyrosine kinase inhibitors (TKIs) used for acute myeloid leukemia treatment. Flt3 and its ligand (Flt3L) are expressed in the heart and cardiac side effects occur under Flt3-targeting TKIs. Whether Flt3/Flt3L also regulate cardiac progenitor cells (CPCs), however, is not known. The cardiac side population (SP) is a pool of heterogenous CPCs that can give rise to all cardiac lineages, hence contributing to cardiovascular homeostasis. Here we show that SP-CPCs produce and are responsive to Flt3L. Compared to wild-type, SP-CPCs from flt3L-/- mice are less abundant, with less contribution of CD45-CD34+ cells, and lower expression of gene sets related to epithelial-to-mesenchymal transition, cardiovascular development and stem cell differentiation. Upon culturing and compared to wild-type, flt3L-/- Sca1+CD31- SP-CPCs show increased proliferation and less vasculogenic commitment, but differentiation can be induced in the presence of receptor tyrosine kinase-activating growth factors. The observed differences are associated with decreased microvascularisation and global systolic function of flt3L-/- hearts. Thus, Flt3 contributes to a receptor tyrosine kinase signature necessary for the maintenance and functionality of SP-CPCs. These findings have potential implications regarding cardiovascular side effects observed under TKI therapy.

2021-11-30 | GSE168207 | GEO

Yes tyrosine kinase signaling promotes liver cancer development

Project description:Yes tyrosine kinase signaling promotes liver cancer development

| PRJNA744904 | ENA

Histologic transformation induced by EGFR tyrosine kinase inhibitors

Project description:Histologic transformation induced by EGFR tyrosine kinase inhibitors

| PRJNA1145888 | ENA

Proteomic profiling by array of tyrosine kinase activity in metastatic malignant melanoma from human tissue specimens

Project description:Tyrosine kinase activity profiling of metatstatic malignant melanoma and normal skin tissue samples was performed using peptide kinase arrays. All samples were run in triplicates with and withouth inhbitor PLX4032 and Sutent Malate in order to identify how tyrosine kinases responds to kinase inhibitor treatment, ex vivo.

2013-01-17 | E-MTAB-1245 | biostudies-arrayexpress

Host-dependent Phenotypic Resistance to EGFR Tyrosine Kinase Inhibitors

Project description:Host-dependent Phenotypic Resistance to EGFR Tyrosine Kinase Inhibitors

| PRJNA705946 | ENA

Yes tyrosine kinase signaling promotes liver cancer development [DSP294_SNU449]

Project description:Yes tyrosine kinase signaling promotes liver cancer development [DSP294_SNU449]

| PRJNA745028 | ENA