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High Expression of SRSF1 Facilitates Osteosarcoma Progression and Unveilsits Potential Mechanisms

ABSTRACT: High Expression of SRSF1 Facilitates Osteosarcoma Progression and Unveilsits Potential Mechanisms

PROVIDER: PRJNA1018930 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26113458_1.fastq.gz	Fastqsanger.gz
	SRR26113458_2.fastq.gz	Fastqsanger.gz
	SRR26113459_1.fastq.gz	Fastqsanger.gz
	SRR26113459_2.fastq.gz	Fastqsanger.gz
	SRR26113460_1.fastq.gz	Fastqsanger.gz

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High Expression of SRSF1 Facilitates Osteosarcoma Progression and Unveilsits Potential Mechanisms

Project description:SRSF1, a member of Serine/Arginine-Rich Splicing Factors (SRSFs), has been observed to significantly influence cancer progression. However, the precise role of SRSF1 in osteosarcoma (OS) remains unclear. In this study, we aimed to investigate the functions of SRSF1 and its underlying mechanism in OS.SRSF1 expression level in OS was obtained from the TCGA dataset, TAGET-OS database. qRT-PCR and Western blotting were employed to assess SRSF1 expression in human OS cell lines and human bone marrow mesenchymal stem cells (BMSC), as well as the interfered ectopic expression states. The effect of SRSF1 on cell migration, invasion, proliferation, and apoptosis of OS cells were measured by transwell assay and flow cytometry. RNA sequence and bioinformatic analyses were conducted to elucidate the relevant biological pathways regulated by SRSF1. Subsequently, Alternative Splicing (AS) events mediated by SRSF1 were identified through RNA-seq and summarized briefly.Our results highlight the oncogenic role of high SRSF1 expression in promoting OS progression, and further explore the potential mechanisms of action. The significant involvement of SRSF1 in OS development suggests its potential utility as a therapeutic target in OS.

2024-04-14 | GSE243561 | GEO

Splicing factor SRSF1 promotes breast cancer progression via regulating alternative splicing

Project description:Purpose:Intensive evidence have highlighted the effect of aberrant alternative splicing (AS) events triggered by dysregulation of SR protein family on cancer progression. Nonetheless, the underlying mechanism in breast cancer (BRCA) remains elusive. Here we sought to explore the molecular function of SRSF1 and identify the key AS events regulated by SRSF1 in BRCA. Methods:We conducted comprehensive analysis for the expression and the clinical correlation of SRSF1 in BRCA based on TCGA, Metabric database, clinical tissue samples and BRCA cell lines. Functional analysis of SRSF1 in BRCA was conducted in vitro and in vivo. SRSF1-mediated AS events and its binding motif were identified by RNA-seq, RNA immunoprecipitation-PCR (RIP-PCR) and in vivo crosslinking followed by immunoprecipitation (CLIP), which was further validated by the minigene reporter assay. Finally, the expression and their clinical significance were validated in clinical samples and TCGA database. Results:SRSF1 was upregulated in BRCA samples, associated positively with tumor grade and Ki-67 index, and correlated with poor prognosis in hormone receptor positive (HR+) cohort, which facilitated tumor progression in vitro and in vivo. We identified SRSF1-mediated AS events and discovered the SRSF1 binding motif in the regulation of PTPMT1. Furthermore, PTPMT1 splice switching regulated by SRSF1 partially mediated the oncogenic role of SRSF1 via the AKT/C-MYC axis. Additionally, PTPMT1 splice switching was validated in tissue samples of BRCA patients. Conclusions:Collectively, SRSF1 exerts the oncogenic roles in BRCA partially through regulating AS of PTPMT1, which could be a candidate prognostic factor and therapeutic target in HR+ BRCA cohort.

2021-05-25 | GSE163025 | GEO

CNTNAP4 signaling regulates osteosarcoma disease progression

Project description:CNTNAP4 signaling regulates osteosarcoma disease progression

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METTL1/WDR4-mediated tRNA m7G modification and mRNA translation control promotes oncogenesis and doxorubicin resistance in osteosarcoma

Project description:Osteosarcoma is the most common bone tumor that leads to high mortality in adolescents and children. The tRNA N7-methylguanosine methyltransferase METTL1 is located in chromosome 12q14.1, a region that is frequently amplified in osteosarcoma patients, while its functions and underlying mechanisms in regulation of osteosarcoma remain unknown. Herein we show that METTL1 and WDR4 are overexpressed in osteosarcoma and associated with poor patient prognosis. Knockdown of METTL1 or WDR4 causes decreased tRNA m7G modification level and impairs osteosarcoma progression in vitro and in vivo. Conversely, METTL1/WDR4 overexpression promotes osteosarcoma proliferation, migration and invasion capacities. tRNA methylation and mRNA translation profiling indicated that METTL1/WDR4 modified tRNAs enhance translation of mRNAs with more m7G tRNA-decoded codons, including extracellular matrix (ECM) remodeling effectors, which facilitates osteosarcoma progression and chemoresistance to doxorubicin.Our study demonstrates METTL1/WDR4 mediated tRNA m7G modification plays crucial oncogenic functions to enhance osteosarcoma progression and chemoresistance to doxorubicin via alteration of oncogenic mRNA translation, suggesting METTL1 inhibition combined with chemotherapy is a promising strategy for treatment of osteosarcoma patients.

2024-02-01 | GSE225515 | GEO

Phosphorylation of SRSF1 at Tyr-19 promotes cell proliferation in pediatric acute lymphoblastic leukemia

Project description:we identified for the first time that the phosphorylation state of SRSF1 is linked to different phases in ALL. Our results underscore the phosphorylation of SRSF1 at the Tyr-19 residue disrupts subcellular localization of SRSF1 and promotes cell proliferation in leukemic cells by accelerating cell-cycle progression. Targeting Tie2 kinase is able to catalyze Tyr-19 phosphorylation of SRSF1, and offer a promising therapeutic target for the treatment of pediatric ALL. These findings undoubtedly add a new layer in understanding of how post-translational mechanism supports leukemia progression.

2018-12-11 | GSE118727 | GEO

Splicing Factor SRSF1 Promotes Tumorigenesis via Oncogenic Splice-Switching and Predicts Poor Prognosis in Multiple Myeloma

Project description:Alternative splicing (AS) and its regulation play critical roles in cancer, yet the dysregulation of AS and its molecular bases in multiple myeloma (MM) development have not yet been elucidated. We identified SRSF1 as a key splicing factor in tumor progression, SRSF1 expression was frequently upregulated in MM and correlated with poor survival.We conducted transcriptome comparison of SRSF1-knockdown and control cells highlighted the functional importance of SRSF1 in mediating MM progression through regulating AS, and revealed the upstream and downstream molecular regulation mechanism of SRSF1. Further investigation to clarify molecular mechanisms and to replicate our findings is necessary. Thus, our findings are of high translational relevance and are expected to have a substantial impact on the development of a promising epigenetic approach for investigating targeted therapies for MM with high SRSF1 expression.

2022-09-04 | GSE160724 | GEO

Splicing factor SRSF1 promotes breast cancer progression via regulating alternative splicing

Project description:Splicing factor SRSF1 promotes breast cancer progression via regulating alternative splicing

| PRJNA684349 | ENA

Chip-chip from Mouse MEFs cells for H3K36me3, Srsf1, Psip1(A300-847 antibody).

Project description:The p52 isoform of Psip1/Ledgf links histone H3K36 methylation and the regulation of alternative splicing. Chromatin immunoprecipitation (ChIP) of Psip1 together with H3K36me3 and Srsf1 and by ChIP-on-chip analysis demonstrated that H3K36me3, Psip1 and SRSF1 enrichment correlates on the gene bodies Array design includes 2 dye swap replicates for Srsf1 and Psip1-/- samples, and single arrays for PSIP and H3K36me3 samples

2012-01-01 | E-GEOD-31520 | biostudies-arrayexpress

Next Generation Sequencing Analysis of SRSF1 flox/flox and SRSF1-KO pancreatic islet Transcriptome

Project description:we report insulin secretion defects in SRSF1 Ins2-Cre mice, in which SRSF1 is ablated in pancreatic β cells.

2023-04-17 | GSE173455 | GEO

SRSF1 HITS-CLIP

Project description:SRSF1 HITS-CLIP

| PRJNA541847 | ENA