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S-adenosylmethionine treatment affects histone methylation in prostate cancer cells

ABSTRACT: S-adenosylmethionine represents a potent inhibitor of cancer cell proliferation, migration and invasion in vitro. The reason remains unclear. Here, we examined if treatment with exogenous SAM is capable of causing alterations in the methylation of the histone markers H3K4me3 and H3K27me3, which are both known to be important in the initiation and progression of prostate cancer.

ORGANISM(S): Homo sapiens

PROVIDER: GSE235629 | GEO | 2023/10/26

REPOSITORIES: GEO

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S-adenosylmethionine (SAM) treatment attenuates breast cancer growth, invasion, metastasis

Project description:This study examines the therapeutic plausibility of using universal methyl group donor S-adenosylmethionine (SAM) to block breast cancer development, growth, and metastasis. cancer. Anti-tumor and anti-metastatic activity of SAM was evaluated through a series of studies in vitro using two different human breast cancer cell lines and in vivo using a MDA-MB-231 xenograft model of breast cancer. The data shown in this array is obtained from control and SAM-treated MDA-MB-231 cell lines.

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Formaldehyde regulates S-adenosylmethionine biosynthesis and one-carbon metabolism

Project description:One-carbon metabolism is an essential branch of cellular metabolism that intersects with epigenetic regulation. Here, we show formaldehyde, a one-carbon unit derived from both endogenous sources and environmental exposure, regulates one-carbon metabolism by inhibiting the biosynthesis of S-adenosylmethionine (SAM), the major methyl donor in cells. Formaldehyde reacts with privileged, hyperreactive cysteine sites in the proteome, including Cys120 in S-adenosylmethionine synthase isoform type-1 (MAT1A). Formaldehyde exposure inhibited MAT1A activity and decreased SAM production with MAT-isoform specificity. A genetic mouse model of chronic formaldehyde overload showed a decrease in SAM and in methylation on selected histones and genes. Epigenetic and transcriptional regulation of Mat1a and related genes function as compensatory mechanisms for formaldehyde-dependent SAM depletion, revealing a biochemical feedback cycle between formaldehyde and SAM one-carbon units.

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S-adenosylmethionine (SAM) changes DNA methylation patterns in prostate cancer cells

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2015-03-01 | E-GEOD-62053 | biostudies-arrayexpress

S-adenosylmethionine (SAM) changes DNA methylation patterns in prostate cancer cells

2015-03-01 | GSE62053 | GEO

Transcriptome change caused by lowered intracellular S-adenosylmethionine level in the X63/0 mouse plasma cell line.

Project description:We aimed to examine the gene expression changes responding to a depletion of intracellular S-adenosylmethionine (SAM). The mouse plasma cell line X63/0 was treated with the SAM-synthetase inhibitor cycloleucine (cLEU), and the total RNA was isolated and analyzed by RNA-sequencing. As a result, we idntified 27 genes, including the ubiquitous SAM-synthetase MAT2A, whose expssions were up-regulated by two-fold or more.

2017-11-09 | GSE106674 | GEO

S-adenosylmethionine modifies cocaine-induced DNA methylation and increases locomotor sensitization in mice

Project description:The aim of the study was to investigate whether environmental factors like S-adenosylmethionine (SAM) via affecting epigenome could alter cocaine-induced gene expression and locomotor sensitization in mice. Using mouse nucleus accumbens (NAc) tissue, whole-genome gene expression profiling revealed that repeated SAM treatment affected a limited number of genes, but significantly modified cocaine-induced gene expression by blunting nonspecifically the cocaine response. At the gene level, we discovered that SAM modulated cocaine-induced DNA methylation by inhibiting both promoter-associated CpG-island hyper- and hypomethylation in the NAc but not in the reference tissue cerebellum.

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Formaldehyde regulates one-carbon metabolism through S-adenosylmethionine biosynthesis

Project description:One-carbon metabolism is a universal hub for cellular metabolism and epigenetic regulation.1–3 Here, we report that formaldehyde (FA), a one-carbon unit that organisms produce in substantial quantities through folate metabolism,4 is a regulator of the one-carbon cycle via the biosynthesis of S-adenosyl-L-methionine (SAM), an essential one-carbon building block for synthesis of nucleotides, amino acids, and methylated nucleic acids and proteins.5 Activity-based protein profiling (ABPP) in mouse liver tissue identifies FA-sensitive cysteine sites across the proteome, revealing several one-carbon cycle targets including S-adenosylmethionine synthetase isoform 1 (MAT1A), the terminal enzyme in SAM biosynthesis. Biochemical studies of the formaldehyde-MAT1A interaction establish FA-dependent inhibition of MAT1A activity through a conserved C120 site, as the MAT2A isoform lacking this cysteine is not FA-sensitive. CRISPR knockout-generated HepG2 cell models that predominantly express either MAT1A or MAT2A show that MAT1A-positive cells respond to FA treatment in a dose-dependent manner by decreasing their SAM levels and downstream RNA methylation, whereas the MAT2A-positive cells are not affected by FA. Our findings reveal an unexpected interplay between SAM and FA, two central one-carbon units to influence the overall methylation potential of the cell.

2023-11-02 | PXD018251 | Pride

S-adenosylmethionine modifies cocaine-induced DNA methylation and increases locomotor sensitization in mice

2013-06-27 | E-GEOD-48365 | biostudies-arrayexpress

mTORC1-independent translation control in mammalian cells by methionine adenosyltransferase 2A and S-adenosylmethionine

Project description:Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (SAM). As the sole methyl-donor of methylation of DNA, RNA and proteins, SAM amount affects gene expression by changing their methylation. Expression of MAT2A, the catalytic subunit of isozyme MAT2, is positively correlated with proliferation of cancer cells. However, how MAT2A promotes cell proliferation is largely unknown. Given that the protein synthesis is induced in proliferating cells and that RNA and protein components of translation machinery are methylated, we tested whether MAT2 and SAM are coupled with protein synthesis. By measuring ongoing protein translation with puromycin labeling in HeLa and Hepa1 cells, we revealed that MAT2A depletion by siRNA or chemical inhibition by cycloleucine reduced protein synthesis in mammalian cells. Overexpression of MAT2A enhanced protein synthesis, indicating that SAM is limiting under normal culture conditions. MAT2 inhibition did not accompany a reduction in the mTORC1 activity but reduced polysome formation. Polysome-bound RNA sequencing revealed that MAT2 inhibition decreased translation efficiency of a fraction of mRNAs. MAT2A was also found to interact with the proteins involved in rRNA processing and ribosome biogenesis. Depletion or inhibition of MAT2 reduced 18S rRNA processing. In addition, by quantitative mass spectrometry, we observed that some translation factors were dynamically methylated in response to the activity of MAT2A or the availability of SAM. These observations suggest that cells possess an mTOR-independent regulatory mechanism that tunes translation in response to the amount of SAM. Such a system may acclimate cells for survival when SAM synthesis is reduced whereas it may support proliferation when SAM is sufficient.

2022-12-21 | GSE201299 | GEO

C. elegans methionine/S-adenosylmethionine cycle activity is sensed and adjusted by a nuclear hormone receptor: RNA-seq dataset 2

Project description:Vitamin B12 is an essential micronutrient that functions in two metabolic pathways: the canonical propionate breakdown pathway and the methionine/S-adenosylmethionine (Met/SAM) cycle. In Caenorhabditis elegans, low vitamin B12, or genetic perturbation of the canonical propionate breakdown pathway results in propionate accumulation and the transcriptional activation of a propionate shunt pathway. This propionate-dependent mechanism requires nhr-10 and is referred to as “B12-mechanism-I”. Here, we report that vitamin B12 represses the expression of Met/SAM cycle genes by a propionate-independent mechanism we refer to as “B12-mechanism-II”. This mechanism is activated by perturbations in the Met/SAM cycle, genetically or due to low dietary vitamin B12. B12-mechanism-II requires nhr-114 to activate Met/SAM cycle gene expression, the vitamin B12 transporter, pmp-5, and adjust influx and efflux of the cycle by activating msra-1 and repressing cbs-1, respectively. Taken together, Met/SAM cycle activity is sensed and transcriptionally adjusted to be in a tight metabolic regime.

2020-06-05 | GSE151847 | GEO

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