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TET2 guards against unchecked BATF3-induced CAR T cell expansion [RNA-seq]

ABSTRACT: Comparing transcriptional profiles of TET2 deficent hyper-proliferative CAR T cells and unedited CAR T cells

ORGANISM(S): Homo sapiens

PROVIDER: GSE220258 | GEO | 2022/12/30

REPOSITORIES: GEO

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TET2 guards against unchecked BATF3-induced CAR T cell expansion [ATAC-seq]

Project description:Comparing genome accessibility profiles (ATACseq) of TET2 deficent hyper-proliferative CAR T cells and unedited CAR T cells

2022-12-30 | GSE220257 | GEO

TET2 guards against unchecked BATF3-induced CAR T cell expansion

Project description:TET2 guards against unchecked BATF3-induced CAR T cell expansion

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TET2 guards against unchecked BATF3-induced CAR T cell expansion [ATAC-seq]

Project description:TET2 guards against unchecked BATF3-induced CAR T cell expansion [ATAC-seq]

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TET2 guards against unchecked BATF3-induced CAR T cell expansion [RNA-seq]

Project description:TET2 guards against unchecked BATF3-induced CAR T cell expansion [RNA-seq]

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TET2 guards against unchecked BATF3-induced CAR T cell expansion

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

2022-12-30 | GSE220259 | GEO

Expression data from chimeric antigen receptor transduced (CAR) human CD4+ T cells during expansion

Project description:In this data set we include expression data from human CD4+ T cells isolated on day 0, 6, 11 and 24 follow anti-CD3/anti-CD28 magnetic bead stimulation and chimeric antigen receptor transduction. 30 samples were submitted. Samples represented three biological replicates of normal donors transduced with various CARs. CARs used were a cMet 28z specific CAR comprised of the IgG4 hinge, CD28 transmembrane and CD28 and CD3zeta intracellular domains. A CD19 CD28 CAR was specific to CD19, and was comprised of a CD8a hinge, CD28 transmembrane and CD28 and CD3zeta intracellular domain. A third CAR, the CD19 BBz, was used that was specific to CD19 was comprised of a CD8a hinge, CD8a transmembrane and 4-1BB and CD3zeta intracellular domains. Expression data was analyzied on day 0, 6, 11 and 24.

2015-01-14 | E-GEOD-64914 | biostudies-arrayexpress

Genome-wide chromatin accessibility profiles of TET2-disrupted T cells from a chronic lymphocytic leukemia (CLL) patient.

Project description:Following CD19-directed chimeric antigen receptor (CAR) T cell infusion, TET2 disrupted CAR+ T cells exhibited an epigenetic profile consistent with altered differentiation.

2018-03-30 | GSE112494 | GEO

14-3-3 protects AMPK phosphorylated TET2 from dephosphorylation by PP2A

Project description:Ten-eleven translocation-2 (TET2) is a member of the methylcytosine dioxygenase family of enzymes implicated in cancer and in aging due to its role as a global epigenetic modifier. TET2 has a large N-terminal domain followed by a catalytic C-terminal. Previous reports have demonstrated that the catalytic domain remains active independent of the N-terminal domain. As such, the function of the N-terminus of this large protein remains poorly characterized. Here, we identify that several isoforms of the 14-3-3 family of proteins bind TET2. 14-3-3s bind TET2 when phosphorylated at serine 99 (S99). AMPK-mediated phosphorylation at S99 promotes TET2 stability and increases global DNA 5-hydroxymethylcytosine. 14-3-3s’ interaction with TET2 serves to protect S99 phosphorylation. Disruption of this interaction leads to both reduced TET2 phosphorylation and decreased protein stability. Furthermore, we identify that the protein phosphatase 2A (PP2A) can interact with TET2 and dephosphorylates S99. Collectively, our study provides novel insights into the role of the N-terminal domain in TET2 regulation. Moreover, they demonstrate the dynamic nature of TET2 protein regulation that could have therapeutic implications for disease states resulting from reduced TET2 levels and/or activity.

2020-01-13 | PXD016160 | Pride

Context Dependent Effects of Ascorbic Acid Treatment in TET2 Mutant Myeloid Neoplasia

Project description:Loss-of-function TET2 mutations (TET2MT) are common in myeloid neoplasia. TET2, a DNA dioxygenase, requires 2-oxoglutarate and Fe(II) to oxidize 5-methylcytosine. TET2MT thus result in hypermethylation and transcriptional repression. Ascorbic acid (AA) increases dioxygenase activity by facilitating Fe(III)/Fe(II) redox reaction and may alleviate some biological consequences of TET2MT by restoring dioxygenase activity. Here, we report the utility of AA in the prevention of TET2MT MN, clarify the mechanistic underpinning of the TET2-AA interactions, and demonstrate that the ability of AA to restore TET2 activity in cells depends on N- and C-terminal lysine acetylation and nature of TET2MT. Consequently, pharmacologic modulation of acetyltransferases and histone deacetylases may regulate TET dioxygenase-dependent AA effects. Thus, our study highlights the contribution of factors that may enhance or attenuate AA effects on TET2 and provides a rationale for novel therapeutic approaches including combinations of AA with class I/II HDAC inhibitor or sirtuin activators in TET2MT leukemia.

2020-09-09 | PXD020550 | Pride

An immunoproteomic approach to characterize the CAR interactome and signalosome

Project description:Adoptive transfer of chimeric antigen receptor (CAR)-T cells is expected to become the first line of treatment for multiple malignancies, following the enormous success of anti-CD19 therapies. However, their mechanism of action is not fully understood, and clear guidelines for the design of safe and efficient receptors are missing. We hereby describe a systematic analysis of the CAR “signalosome” in human primary T cells. Two CAR designs were compared: a second-generation (PSCA2) and a third-generation (PSCA3) anti-PSCA CAR. Phosphorylation events triggered by CAR-mediated recognition of target cells were quantified by mass spectrometry.

2019-11-07 | PXD007086 | Pride

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