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Interfering with aggregated α-synuclein in advanced melanoma leads to a major upregulation of MHC class II proteins

ABSTRACT: Interfering with aggregated α-synuclein in advanced melanoma leads to a major upregulation of MHC class II proteins

PROVIDER: PRJNA1005576 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25643452.fastq.gz	Fastqsanger.gz
	SRR25643453.fastq.gz	Fastqsanger.gz
	SRR25643454.fastq.gz	Fastqsanger.gz
	SRR25643455.fastq.gz	Fastqsanger.gz
	SRR25643456.fastq.gz	Fastqsanger.gz

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Similar Datasets

Interfering with aggregated α-synuclein in advanced melanoma leads to a major upregulation of MHC class II proteins

Project description:Melanoma is the most serious and deadly form of skin cancer and with progression to advanced melanoma, the intrinsically disordered protein α-synuclein is upregulated to high levels; and while toxic to dopaminergic neurons in Parkinson’s disease, it is highly beneficial for primary and metastatic melanoma cells. To gain detailed insights, both at the level of the proteome and the transcriptome, into this exact opposite role of α-synuclein in advanced melanoma, we performed proteome and transcriptome studies of high-level α-synuclein-expressing primary and metastatic human melanoma cell lines and metastatic human melanoma xenografts treated with the small-molecule diphenyl-pyrazole compound anle138b, which binds to and interferes with the oligomeric structure of α-synuclein. Our data demonstrate that interfering with oligomerized α-synuclein in these melanoma cells and tumor xenografts leads to a substantial upregulation of major histocompatibility complex (MHC) proteins, which are important for enhancing anti-melanoma immune responses.

2024-07-03 | PXD030615 | Pride

Interfering with aggregated α-synuclein in advanced melanoma leads to a major upregulation of MHC class II proteins

Project description:Melanoma is the most serious and deadly form of skin cancer and with progression to advanced melanoma, the intrinsically disordered protein α-synuclein is upregulated to high levels; and while toxic to dopaminergic neurons in Parkinson’s disease, it is highly beneficial for primary and metastatic melanoma cells. To gain detailed insights, both at the level of the proteome and the transcriptome, into this exact opposite role of α-synuclein in advanced melanoma, we performed proteomic studies of high-level α-synuclein-expressing primary and metastatic human melanoma cell lines and proteomic and transcriptomic studies of metastatic human melanoma xenografts treated systemically with the diphenyl-pyrazole small-molecule compound anle138b, which binds to and interferes with the oligomeric structure of α-synuclein. The results of these studies reveal that interfering with oligomerized α-synuclein in these tumor xenografts led to a substantial upregulation of expression of major histocompatibility complex proteins in the melanoma cells, the latter of which is pertinent to enhancing anti-melanoma immune responses.

2024-05-21 | GSE240854 | GEO

Interfering with aggregated α-synuclein in advanced melanoma leads to a major upregulation of MHC class II proteins.

Project description:Melanoma is the most serious and deadly form of skin cancer and with progression to advanced melanoma, the intrinsically disordered protein α-synuclein is upregulated to high levels. While toxic to dopaminergic neurons in Parkinson's disease, α-synuclein is highly beneficial for primary and metastatic melanoma cells. To gain detailed insights into this exact opposite role of α-synuclein in advanced melanoma, we performed proteomic studies of high-level α-synuclein-expressing human melanoma cell lines that were treated with the diphenyl-pyrazole small-molecule compound anle138b, which binds to and interferes with the oligomeric structure of α-synuclein. We also performed proteomic and transcriptomic studies of human melanoma xenografts that were treated systemically with the anle138b compound. The results reveal that interfering with oligomerized α-synuclein in the melanoma cells in these tumor xenografts led to a substantial upregulation and expression of major histocompatibility complex proteins, which are pertinent to enhancing anti-melanoma immune responses.

| S-EPMC11361348 | biostudies-literature

The responses of astrocytes stimulated by extracellular a-synuclein

Project description:Abnormal neuronal aggregation of a-synuclein is implicated in the development of Parkinson’s disease. Glial cells also show extensive a-synuclein pathology and are thought to contribute to disease progression. However, the mechanism that produces the glial a-synuclein pathology and the interaction between neurons and glia in the disease-inflicted microenvironment remain unknown. Here, we show that in neuronal cells misfolded a-synuclein proteins are selectively translocated into vesicles, leading to exocytosis of the aggregated forms. More importantly, our data demonstrate that astrocytes take up the neuron-derived a-synuclein aggregates and produce a-synuclein inclusions similar to the ones found in human brains. This uptake is paralleled by changes in the gene expression profile reflecting an inflammatory response. These results suggest that astroglial a-synuclein pathology is produced by cell-to-cell transmission of neuronal a-synuclein aggregates. This transmission step is thus an important mediator of pathogenic glial responses and could qualify as a new therapeutic target. To determine how astrocytes respond to extracellular a-synuclein, gene expression profiles were established and analyzed for nearly 22,000 rat genes using the Illumina RatRef-12 Expression BeadChip. Total RNA was isolated from astrocytes exposed for 6h or 24h to conditioned medium from cultures of a-synuclein or lacZ expressing cells.

2010-01-11 | E-GEOD-11574 | biostudies-arrayexpress

The responses of astrocytes stimulated by extracellular a-synuclein

2010-01-12 | GSE11574 | GEO

Epigenetic regulations in the IFNM-NM-3 signalling pathway: IFNM-NM-3-mediated MHC class I upregulation on tumour cells is associated with DNA demethylation of antigen-presenting machinery genes [TC1A9_IFN]

Project description:Reversible MHC class I deficiency on tumour cells is commonly caused by coordinated silencing of antigen-presenting machinery genes and restorable by IFNM-NM-3. Here we describe association of DNA demethylation of selected antigen-presenting machinery gene regulatory regions located in the MHC genomic locus (TAP-1, TAP-2, LMP-2, LMP-7) upon IFNM-NM-3 treatment with MHC class I upregulation on tumour cells. Our novel findings demonstrate that IFNM-NM-3 acts as an epigenetic modifier upregulating the expression of antigen-presenting machinery genes through DNA demethylation. Our data also cast more light on the role of DNA methylation in tumour cell escape from specific immunity. TC-1/A9 cultured cells treated with IFN gama or nothing. 3 biological replicates per condition.

2014-12-08 | E-GEOD-53467 | biostudies-arrayexpress

Project description:Reversible MHC class I deficiency on tumour cells is commonly caused by coordinated silencing of antigen-presenting machinery genes and restorable by IFNM-NM-3. Here we describe association of DNA demethylation of selected antigen-presenting machinery gene regulatory regions located in the MHC genomic locus (TAP-1, TAP-2, LMP-2, LMP-7) upon IFNM-NM-3 treatment with MHC class I upregulation on tumour cells. Our novel findings demonstrate that IFNM-NM-3 acts as an epigenetic modifier upregulating the expression of antigen-presenting machinery genes through DNA demethylation. Our data also cast more light on the role of DNA methylation in tumour cell escape from specific immunity. TC-1/A9 cultured cells treated with DAC/TSA or nothing. 3 biological replicates per condition.

2014-12-08 | E-GEOD-53466 | biostudies-arrayexpress

Project description:Reversible MHC class I deficiency on tumour cells is commonly caused by coordinated silencing of antigen-presenting machinery genes and restorable by IFNM-NM-3. Here we describe association of DNA demethylation of selected antigen-presenting machinery gene regulatory regions located in the MHC genomic locus (TAP-1, TAP-2, LMP-2, LMP-7) upon IFNM-NM-3 treatment with MHC class I upregulation on tumour cells. Our novel findings demonstrate that IFNM-NM-3 acts as an epigenetic modifier upregulating the expression of antigen-presenting machinery genes through DNA demethylation. Our data also cast more light on the role of DNA methylation in tumour cell escape from specific immunity. RVP3 cultured cells treated with DAC/TSA or nothing. 3 biological replicates per condition.

2014-12-08 | E-GEOD-53465 | biostudies-arrayexpress

Identification of Alpha-Synuclein Interacting Synaptosomal Proteins

Project description:α-Synuclein is an abundant presynaptic protein that when aggregated and dyslocated from the synapse is associated to Parkinson’s disease and dementia. The normal presynaptic function of α-synuclein is unclear as well as the disease triggering mechanism. In order to extend the knowledge of the α-synuclein interactome during normal function and disease, we have used porcine brain synaptosomes as a source of ligands and purified α-synuclein monomers or oligomers as bait in co-immunoprecipitation experiments. The isolated binding synaptosomal proteins were identified with LC-LTQ-orbitrap tandem mass spectrometry and quantified by peak area using the freely-available Windows client application, Skyline Targeted Proteomic Environment. To compare proteins binding to a-synuclein monomer with proteins binding to a-synuclein oligomer, quantifications were log transformed, normalized to buffer-background, and compared by students t-test. Furthermore, to specify the preferential binding an average fold increase was calculated by comparing binding to monomer and oligomer. 10 α-synuclein preferential monomer binding proteins were identified and among those, we successfully validated Abl interactor 1, and myelin proteolipid protein. 76 α-synuclein preferential oligomer binding proteins were found, including glutamate decarboxylase 2, synapsin 1, and glial fibrillary acidic protein, which were positively validated. We identified 92 proteins binding to α-synuclein, for which we were not able to detect any conformational preferences among. This study presents a catalog of proteins interacting with α-synuclein in its non-aggregated and aggregated oligomeric state, which can be used to investigate the normal and pathological roles of α-synuclein.

2015-02-09 | PXD001462 | Pride

Epigenetic regulations in the IFNγ signalling pathway: IFNγ-mediated MHC class I upregulation on tumour cells is associated with DNA demethylation of antigen-presenting machinery genes [TC1A9_IFN]

Project description:Reversible MHC class I deficiency on tumour cells is commonly caused by coordinated silencing of antigen-presenting machinery genes and restorable by IFNγ. Here we describe association of DNA demethylation of selected antigen-presenting machinery gene regulatory regions located in the MHC genomic locus (TAP-1, TAP-2, LMP-2, LMP-7) upon IFNγ treatment with MHC class I upregulation on tumour cells. Our novel findings demonstrate that IFNγ acts as an epigenetic modifier upregulating the expression of antigen-presenting machinery genes through DNA demethylation. Our data also cast more light on the role of DNA methylation in tumour cell escape from specific immunity.

2014-12-08 | GSE53467 | GEO

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