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The mitochondrial enzyme pyruvate carboxylase restricts pancreatic β-cell senescence by blocking p53 activation

ABSTRACT: The mitochondrial enzyme pyruvate carboxylase restricts pancreatic β-cell senescence by blocking p53 activation

PROVIDER: PRJNA1169324 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30892955_1.fastq.gz	Fastqsanger.gz
	SRR30892955_2.fastq.gz	Fastqsanger.gz
	SRR30892956_1.fastq.gz	Fastqsanger.gz
	SRR30892956_2.fastq.gz	Fastqsanger.gz
	SRR30892957_1.fastq.gz	Fastqsanger.gz

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The mitochondrial enzyme pyruvate carboxylase restricts pancreatic β-cell senescence by blocking p53 activation

Project description:Defective glucose-stimulated insulin secretion (GSIS) and β-cell senescence are hallmarks in diabetes. The mitochondrial enzyme pyruvate carboxylase (PC) has been shown to promote GSIS and β-cell proliferation in the clonal β-cell lines, yet its physiological relevance remains unknown. Here, we provide animal and human data showing a role of PC in protecting β-cells against senescence and maintaining GSIS under different physiological and pathological conditions. β-cell-specific deletion of PC impaired GSIS and induced β-cell senescence in the mouse models under either a standard chow diet or prolonged high-fat diet feeding. Transcriptomic analysis indicated that p53-related senescence and cell cycle arrest are activated in PC-deficient islets. Overexpression of PC inhibited hyperglycemia- and aging-induced p53-related senescence in human and mouse islets as well as INS-1E β-cells, whereas knockdown of PC provoked senescence. Mechanistically, PC interacted with MDM2 to prevent its degradation via the MDM2 binding motif, which in turn restricts the p53-dependent senescent program in β-cells. On the contrary, the regulatory effects of PC on GSIS and the tricarboxylic acid (TCA) anaplerotic flux are p53-independent. We illuminate a function of PC in controlling β-cell senescence through the MDM2–p53 axis.

2024-10-10 | GSE278865 | GEO

suppression of Pyruvate carboxylase

Project description:suppression of Pyruvate carboxylase

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suppression of Pyruvate carboxylase in M-wnt tumors

Project description:suppression of Pyruvate carboxylase in M-wnt tumors

| PRJNA821609 | ENA

Requirement of hepatic pyruvate carboxylase during fasting, high fat and ketogenic diet

Project description:Pyruvate has two major fates upon entry into mitochondria, the oxidative decarboxylation to acetyl-CoA or the biotin-dependent carboxylation to oxaloacetate via pyruvate carboxylase (Pcx). Here we have generated mice with a liver specific knockout of Pcx to understand its role in hepatic mitochondrial metabolism under disparate physiological states including a 24 hour fast, as well as ketogenic and high fat diets. These data ultimately show the requirement of Pcx-mediated anapleorsis in the liver under disparate metabolic conditions.

2022-10-31 | GSE198317 | GEO

Pyruvate carboxylase and carbon metabolism in Listeria monocytogenes

Project description:Transcriptional profile of wild type L. monocytogenes (EGDe) and a pycA mutant strain was compared on growth in BHI. The human pathogen L. monocytogenes is a facultatively intracellular bacterium that survives and replicates in the cytosol of many mammalian cells. The listerial metabolism, especially under intracellular conditions , is still poorly understood. Recent studies analyzed the carbon metabolism of L. monocytogenes by the 13C-isotopologue perturbation method in a defined minimal medium containing [U-13C6]glucose. It was shown that these bacteria produce oxaloacetate mainly by carboxylation of pyruvate due to an incomplete tricarboxylic acid cycle. Here we report that a pycA insertion mutant defective in pyruvate carboxylase (PYC) still grows, albeit at a reduced rate, in BHI medium, but is unable to multiply in a defined minimal medium with glucose or glycerol 36 as carbon source. Transcriptional profiling was performed on the pycA mutant and the wild type strain grown in BHI to get a closer insight into the effect of the pycA mutation in Listeria monocytogenes. RNA from the two strains were isolated after growth in BHI and and compared using whole genome oligonucleotide microarrays

2010-02-09 | E-GEOD-19014 | biostudies-arrayexpress

suppression of Pyruvate carboxylase in E0771 cells [in vitro]

Project description:suppression of Pyruvate carboxylase in E0771 cells [in vitro]

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suppression of Pyruvate carboxylase in E0771 tumors [in vivo]

Project description:suppression of Pyruvate carboxylase in E0771 tumors [in vivo]

| PRJNA821608 | ENA

Pyruvate carboxylase and carbon metabolism in Listeria monocytogenes

2010-02-10 | GSE19014 | GEO

The long noncoding RNA ADIPINT is a gatekeeper of pyruvate carboxylase function regulating human fat cell metabolism

Project description:The pleiotropic function of long noncoding RNAs (lncRNAs) is well recognized, but their direct role in governing metabolic homeostasis is less understood. Here, we describe a human adipocyte-specific lncRNA, ADIPINT, that regulates pyruvate carboxylase (PC), a pivotal enzyme in energy metabolism. With a novel approach, Targeted RNA-protein identification using Orthogonal Organic Phase Separation (TROOPS), and validation with electron microscopy, we show that ADIPINT binds to PC. ADIPINT knockdown alters the interactome and decreases the abundance and enzymatic activty of PC in the mitochondria. Reduced ADIPINT or PC expression lowers adipocyte lipid synthesis, breakdown, and lipid content.

2022-04-28 | GSE199076 | GEO

Fibroblast pyruvate carboxylase is required for collagen production in the tumor microenvironment

Project description:The aberrant production of collagen by fibroblasts is a hallmark of many solid tumors and can influence cancer progression. How fibroblasts produce collagen within tumor microenvironments which are nutrient-poor is not understood. Here, we show that pyruvate carboxylase (PC) activity increases in fibroblasts cultured in a low glutamine environment, and that PC is required for collagen production by tumor-associated fibroblasts in vivo.

2021-09-03 | GSE169588 | GEO

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