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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [single-cell RNA-seq]

ABSTRACT: Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [single-cell RNA-seq]

PROVIDER: PRJNA773406 | ENA |

REPOSITORIES: ENA

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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells

Project description:Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells

| PRJNA773400 | ENA

Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [Human KC]

Project description:Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [Human KC]

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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [mouse KC]

Project description:Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [mouse KC]

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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [Human KC]

Project description:To investigate the human primary Kupffer cells from NAFLD patients response to DPI in vitro.

2021-10-23 | GSE186326 | GEO

Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [mouse KC]

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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells [single-cell RNA-seq]

Project description:Single-cell RNAseq analysis of liver cells from NASH and cirrhosis patients has identified the presence of TREM2+ disease-associated macrophages (DAMs) in the liver that display lower expression of metabolic genes. To determine whether the DAMs are also present in patient with mild NFALD, we performed scRNAseq of freshly isolated immune cells from liver biopsies of 3 healthy donors and 3 mild NFALD patients. Kupffer cells were specifically focused.

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Activation of GPR3-b-Arrestin2-PKM2 by DPI enhanced glycolysis in kupffer cells

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

2021-10-23 | GSE186329 | GEO

PKM2 functions as a histidine kinase to phosphorylate PGAM1 to increase glycolysis shunts in cancer

Project description:Phosphoglycerate mutase 1 (PGAM1) is a key-node enzyme that diverts the metabolic intermediates from glycolysis into its shunts to support macromolecule biosynthesis for rapid and sustainable cell proliferation. It is prevalent that PGAM1 activity is upregulated in various tumors; however, the underlying mechanism remains unclear. Here, we unveil that pyruvate kinase M2 (PKM2) moonlights as a histidine kinase in a phosphoenolpyruvate (PEP)-dependent manner to catalyze PGAM1 H11 phosphorylation, that is essential for PGAM1 activity. Moreover, the dimeric or monomeric PKM2 in tumor cells phosphorylates PGAM1 more efficiently than the tetrameric one. In response to epidermal growth factor (EGF), Src signaling triggered PGAM1 Y119 phosphorylation is a prerequisite for PKM2 binding and the subsequent H11 phosphorylation of PGAM1, which constitutes the discrepancy between tumor cells and normal ones. A PGAM1-derived pY119-containing cell-permeable peptide or Y119 mutation disrupts the interaction of PGAM1 with PKM2 and its H11 phosphorylation, and eventually dampens the glycolysis shunts and tumor growth. We not only identifes a histidine kinase function of PKM2, but also illustrates an enzymes-cross-talk regulatory mode during metabolic reprogramming.

2024-03-21 | PXD049235 | Pride

Pharmacological activation of pyruvate kinase M2 (PKM2) inhibits CD4+ T cell pathogenicity and suppresses autoimmunity

Project description:Pyruvate kinase (PK) catalyzes the conversion of phosphoenolpyruvate to pyruvate during glycolysis. The PK isoform PKM2 has additional roles in regulation of gene transcription and protein phosphorylation. PKM2 controls macrophage metabolic remodeling in inflammation, but its role in T cell biology is poorly understood. These results show that TEPP-46, an activator of PKM2, reduces CD4+ T cell activation, proliferation, and cytokine production by inhibiting essential signaling pathways and preventing glycolysis.

2019-11-26 | GSE139378 | GEO

PKM2 functions as a histidine kinase to phosphorylate PGAM1 to increase glycolysis shunts in cancer-Cellular lipid level assessment

Project description:Phosphoglycerate mutase 1 (PGAM1) is a key node enzyme that diverts the metabolic reactions from glycolysis into its shunts to support macromolecule biosynthesis for rapid and sustainable cell proliferation. It is prevalent that PGAM1 activity is upregulated in various tumors; however, the underlying mechanism remains unclear. Here, we unveil that pyruvate kinase M2 (PKM2) moonlights as a histidine kinase in a phosphoenolpyruvate (PEP)-dependent manner to catalyze PGAM1 H11 phosphorylation, that is essential for PGAM1 activity. Moreover, monomeric and dimeric PKM2 are efficient to phosphorylate and activate PGAM1, while the tetrameric PKM2 is not. In response to epidermal growth factor (EGF) signaling, Src-catalyzed PGAM1 Y119 phosphorylation is a prerequisite for PKM2 binding and the subsequent PGAM1 H11 phosphorylation, which constitutes the discrepancy between tumor cells and normal ones. A PGAM1-derived pY119-containing cell-permeable peptide or Y119 mutation disrupted the interaction of PGAM1 with PKM2 and its H11 phosphorylation, and eventually dampened the glycolysis shunts and tumor growth. We not only identified a function of PKM2 as a histidine kinase, but also illustrated an enzymes-cross-talk regulatory mode during metabolic reprogramming.

2024-03-21 | PXD049310 | Pride

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