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

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

PROVIDER: PRJNA814616 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18290033_1.fastq.gz	Fastqsanger.gz
	SRR18290033_2.fastq.gz	Fastqsanger.gz
	SRR18290034_1.fastq.gz	Fastqsanger.gz
	SRR18290034_2.fastq.gz	Fastqsanger.gz
	SRR18290035_1.fastq.gz	Fastqsanger.gz

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

2022-10-31 | GSE198317 | GEO

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 pyruvate carboxylase (PcxL-/-) to understand the role of Pcx in hepatic mitochondrial metabolism under disparate physiological states. PcxL-/- mice exhibited a deficit in hepatic gluconeogenesis as expected but were able to maintain systemic euglycemia following a 24hr fast and enhanced ketogenesis. Feeding a high fat diet to PcxL-/- mice resulted in animals that were resistant to glucose intolerance without affecting body weight. However, PcxL-/- mice fed a ketogenic diet for 1 week became severely hypoglycemic, demonstrating a requirement for hepatic Pcx for long term glycemia under carbohydrate limited diets. Loss of Pcx was associated with an induction of protein acetylation in PcxL-/- mice regardless of physiologic state. Furthermore, liver acetyl-proteomics revealed a biased induction in mitochondrial lysine acetylation. These data show that Pcx is important for maintaining the proper balance of pyruvate metabolism between oxidative and anaplerotic pathways.

2022-10-31 | PXD032028 | Pride

suppression of Pyruvate carboxylase

Project description:suppression of Pyruvate carboxylase

| PRJNA821599 | 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 via the pyruvate decarboxylase complex or the biotin-dependent carboxylation to oxaloacetate via pyruvate carboxylase (Pcx). Here, we have generated mice with a liver-specific KO of pyruvate carboxylase (PcxL-/-) to understand the role of Pcx in hepatic mitochondrial metabolism under disparate physiological states. PcxL-/- mice exhibited a deficit in hepatic gluconeogenesis and enhanced ketogenesis as expected but were able to maintain systemic euglycemia following a 24 h fast. Feeding a high-fat diet to PcxL-/- mice resulted in animals that were resistant to glucose intolerance without affecting body weight. However, we found that PcxL-/- mice fed a ketogenic diet for 1 week became severely hypoglycemic, demonstrating a requirement for hepatic Pcx for long-term glycemia under carbohydrate-limited diets. Additionally, we determined that loss of Pcx was associated with an induction in the abundance of lysine-acetylated proteins in PcxL-/- mice regardless of physiologic state. Furthermore, liver acetyl-proteomics revealed a biased induction in mitochondrial lysine-acetylated proteins. These data show that Pcx is important for maintaining the proper balance of pyruvate metabolism between oxidative and anaplerotic pathways.

| S-EPMC9694104 | biostudies-literature

suppression of Pyruvate carboxylase in M-wnt tumors

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

| PRJNA821609 | ENA

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 tumors [in vivo]

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

| PRJNA821608 | ENA

suppression of Pyruvate carboxylase in E0771 cells [in vitro]

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

| PRJNA821607 | ENA

Pyruvate carboxylase and carbon metabolism in Listeria monocytogenes

2010-02-10 | GSE19014 | 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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