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Novel microRNAs modulating ecto-5′-nucleotidase expression [MaMel]

ABSTRACT: the effect of NT5E enhancing miRNAs was studied by gene expression profiling to unterstand mechanism of observed NT5E upregulation.

ORGANISM(S): Homo sapiens

PROVIDER: GSE228640 | GEO | 2023/05/31

REPOSITORIES: GEO

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Novel microRNAs modulating ecto-5′-nucleotidase expression [SK-Mel-28]

Project description:the effect of NT5E enhancing miRNAs was studied by gene expression profiling to unterstand mechanism of observed NT5E upregulation.

2023-05-31 | GSE228641 | GEO

Novel microRNAs modulating ecto-5′-nucleotidase expression [MDA-MB-231]

Project description:the effect of NT5E enhancing miRNAs was studied by gene expression profiling to unterstand mechanism of observed NT5E upregulation.

2023-05-31 | GSE228639 | GEO

Novel microRNAs modulating ecto-5'-nucleotidase expression.

Project description:IntroductionThe expression of immune checkpoint molecules (ICMs) by cancer cells is known to counteract tumor-reactive immune responses, thereby promoting tumor immune escape. For example, upregulated expression of ecto-5'-nucleotidase (NT5E), also designated as CD73, increases extracellular levels of immunosuppressive adenosine, which inhibits tumor attack by activated T cells. MicroRNAs (miRNAs) are small non-coding RNAs that regulate gene expression at the post-transcriptional level. Thus, the binding of miRNAs to the 3'-untranslated region of target mRNAs either blocks translation or induces degradation of the targeted mRNA. Cancer cells often exhibit aberrant miRNA expression profiles; hence, tumor-derived miRNAs have been used as biomarkers for early tumor detection.MethodsIn this study, we screened a human miRNA library and identified miRNAs affecting the expression of ICMs NT5E, ENTPD1, and CD274 in the human tumor cell lines SK-Mel-28 (melanoma) and MDA-MB-231 (breast cancer). Thereby, a set of potential tumor-suppressor miRNAs that decreased ICM expression in these cell lines was defined. Notably, this study also introduces a group of potential oncogenic miRNAs that cause increased ICM expression and presents the possible underlying mechanisms. The results of high-throughput screening of miRNAs affecting NT5E expression were validated in vitro in 12 cell lines of various tumor entities.ResultsAs result, miR-1285-5p, miR-155-5p, and miR-3134 were found to be the most potent inhibitors of NT5E expression, while miR-134-3p, miR-6859-3p, miR-6514-3p, and miR-224-3p were identified as miRNAs that strongly enhanced NT5E expression levels.DiscussionThe miRNAs identified might have clinical relevance as potential therapeutic agents and biomarkers or therapeutic targets, respectively.

| S-EPMC10318900 | biostudies-literature

Novel microRNAs modulating ecto-5′-nucleotidase expression

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-05-31 | GSE228642 | GEO

Novel microRNAs modulating ecto-5′-nucleotidase expression

Project description:Novel microRNAs modulating ecto-5′-nucleotidase expression

| PRJNA950915 | ENA

Novel microRNAs modulating ecto-5′-nucleotidase expression [MaMel]

Project description:Novel microRNAs modulating ecto-5′-nucleotidase expression [MaMel]

| PRJNA950919 | ENA

Novel microRNAs modulating ecto-5′-nucleotidase expression [MDA-MB-231]

Project description:Novel microRNAs modulating ecto-5′-nucleotidase expression [MDA-MB-231]

| PRJNA950921 | ENA

Novel microRNAs modulating ecto-5′-nucleotidase expression [SK-Mel-28]

Project description:Novel microRNAs modulating ecto-5′-nucleotidase expression [SK-Mel-28]

| PRJNA950920 | ENA

Ecto-5’-Nucleotidase (Nt5e/CD73)-Mediated Adenosine Signaling Attenuates TGFβ-2 Induced Elastin and Cellular Contraction

Project description:To investigate the broad transcriptional consequences of Nt5e knock-out on mice vascular smooth cells in culture at baseline.

2022-11-01 | GSE216727 | GEO

Ecto-5'-nucleotidase: Structure function relationships.

Project description:Ecto-5'-nucleotidase (ecto-5'-NT) is attached via a GPI anchor to the extracellular membrane, where it hydrolyses AMP to adenosine and phosphate. Related 5'-nucleotidases exist in bacteria, where they are exported into the periplasmic space. X-ray structures of the 5'-nucleotidase from E. coli showed that the enzyme consists of two domains. The N-terminal domain coordinates two catalytic divalent metal ions, whereas the C-terminal domain provides the substrate specificity pocket for the nucleotides. Thus, the substrate binds at the interface of the two domains. Here, the currently available structural information on ecto-5'-NT is reviewed in relation to the catalytic properties and enzyme function.

| S-EPMC2254484 | biostudies-literature

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