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GLUD1 blockade triggers glutamine production by macrophages, nourishing satellite cells and promoting muscle regeneration

ABSTRACT: GLUD1 blockade triggers glutamine production by macrophages, nourishing satellite cells and promoting muscle regeneration

PROVIDER: PRJNA509926 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8315950.fastq.gz	Fastqsanger.gz
	SRR8315960.fastq.gz	Fastqsanger.gz
	SRR8315951.fastq.gz	Fastqsanger.gz
	SRR8315952.fastq.gz	Fastqsanger.gz
	SRR8315953.fastq.gz	Fastqsanger.gz

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GLUD1 blockade triggers glutamine production by macrophages, nourishing satellite cells and promoting muscle regeneration

Project description:RNAseq was performed on Glud1-deficient macrophages vs. WT macrophages sorted at baseline and at the peak of muscle damage (1day after intramuscular injection of cardiotoxin). By analysing the clustered for M1 and M2 genes as well as for wound healing genes of Glud1-deficient macrophages vs. WT macrophages recovered from muscle damage model, our understanding of key macrophage-dependent events in the damaged muscles will be improved.

2020-07-01 | GSE123825 | GEO

The effect of Glud1 inhibition of HSCs durgin ev vivo culture

Project description:Self-renewing hematopoietic stem cells (HSCs) during hematopoietic regeneration showed lower intracellular glutamate (Glu) levels compared with dividing progenitor cells in the steady state and HSCs that attenuate stem cell features during ex vivo culture. Moreover, R162, an inhibitor of glutamine dehydrogenase (Glud1) that catabolize Glu into α-ketoglutarate, contributed to stem cell maintenance during HSC divisions. These data suggest that lower intracellular Glu levels during HSC division contributed to self-renewing divisions by suppressing Glud1-mediated reactions.

2026-07-13 | GSE279490 | GEO

GLUD1 determines murine muscle stem cell fate by controlling mitochondrial glutamate levels

Project description:Muscle stem cells (MuSCs) enable muscle growth and regeneration after exercise or injury, but how metabolism controls their regenerative potential is poorly understood. We describe that primary metabolic changes can determine murine MuSC fate decisions. We found that glutamine anaplerosis into the TCA cycle decreases during MuSC differentiation and coincides with decreased expression of the mitochondrial glutamate deaminase GLUD1. Deletion of Glud1 in proliferating MuSCs resulted in precocious differentiation and fusion combined with loss of self-renewal in vitro and in vivo. Mechanistically, deleting Glud1 caused mitochondrial glutamate accumulation and inhibited the malate-aspartate shuttle (MAS). The resulting defect in transporting NADH reducing equivalents into the mitochondria induced compartment-specific NAD+/NADH ratio shifts. MAS activity restoration or directly altering NAD+/NADH ratios normalised myogenesis. In conclusion, GLUD1 prevents deleterious mitochondrial glutamate accumulation and inactivation of the MAS in proliferating MuSCs. It thereby acts as a compartment specific metabolic brake on MuSC differentiation.

2024-07-02 | GSE243640 | GEO

MYLK-AS1 Enhances Glutamine Metabolism to Promote EGFR Inhibitor Resistance in Non-Small Cell Lung Cancer

Project description:Here we identified a role for the lncRNA MYLK-AS1 promoting acquired TKI resistance of lung cancer in vitro and in vivo. MYLK-AS1 bound and directly drove phase separation of interleukin enhancer binding factor 3 (ILF3), thus interacting with the 3’UTR of glutamate dehydrogenase 1 (GLUD1) to post-transcriptionally promote its mRNA stability, thus enhancing mitochondrial glutamine catabolism, promoting TKI resistance. The MYLK-AS1/ILF3/GLUD1 may be a target for overcoming TKI resistance in lung cancer.

2025-04-28 | GSE295807 | GEO

GeneChip expression profiling of Glud1 (glutamate dehydrogenase 1) transgenic mice

Project description:Glud1 (glutamate dehydrogenase 1) transgenic mice release more excitatory neurotransmitter glutamate to synaptic cleft throughout lifespan and show signs of accelerated aging. Here we compared transcriptomic profiles of these animals to their wild-type counterparts. The hippocampus was used for the analysis. Keywords: transgenic analysis Three Glud1 transgenic mice vs. three age-matched wide-type mice. Age: 9-month-old. Tissue: hippocampus.

2010-07-12 | E-GEOD-11419 | biostudies-arrayexpress

GeneChip expression profiling of Glud1 (glutamate dehydrogenase 1) transgenic mice across age

Project description:Glud1 (Glutamate dehydrogenase 1) transgenic mice release more excitatory neurotransmitter glutamate to synaptic cleft throughout lifespan. Here we compared transcriptomic profiles of these animals to their wild-type counterparts across 5 ages. The hippocampus was used for the analysis. Longitudinal studies of Glud1 transgenic and wide-type mice across 5 age points: 10 days post birth, 4.5 mo, 9 mo, 14.5 mo, and 20 mo.

2014-07-31 | E-GEOD-48911 | biostudies-arrayexpress

GeneChip expression profiling of Glud1 (glutamate dehydrogenase 1) transgenic mice

2010-07-12 | GSE11419 | GEO

GeneChip expression profiling of Glud1 (glutamate dehydrogenase 1) transgenic mice across age

2014-07-31 | GSE48911 | GEO

Combined with Gefitinib Overcomes Immunosuppression Induced by long-term Glutamine blockade in Bladder Cancer

Project description:Glutamine is a major energy source for tumor cells and blocking glutamine metabolism is being investigated as a promising strategy for cancer therapy. However, the antitumor effect of glutamine blockade in bladder cancer remains unclear, necessitating further investigation. Here, we demonstrated that glutamine metabolism was involved in the malignant progression of bladder cancer. Treatment with the glutamine antagonist 6-Diazo-5-oxo-L-norleucine (DON) inhibited bladder cancer cells in vitro in several ways. In addition, we observed a remarkable inhibition of tumor growth in bladder cancer-bearing mice using JHU083, a prodrug that was designed to prevent DON-induced toxicity. However, the antitumor immune effect of T cells changed from activation to inhibition as the administrated time extended. We found that both in vitro treatment with DON and in vivo prolonged administration of JHU083 led to the upregulation of PD-L1 in bladder cancer cells. Mechanistically, glutamine blockade up-regulates PD-L1 expression in bladder cancer cells by accumulating ROS, subsequently activating the EGFR/ERK/C-Jun signaling pathway. Combinatorial treatment with JHU083 and gefitinib reversed the up-regulation of PD-L1 in bladder cancer cells induced by prolonged glutamine blockade. This reversal resulted in the alleviation of T-cell immunosuppression and a significant improvement in therapeutic outcome. These preclinical findings suggested that broad targeting of glutamine metabolism could represent a viable therapeutic strategy for bladder cancer, with the potential for further enhancement through combined treatment with gefitinib.

2024-08-08 | GSE269520 | GEO

The unique catalytic properties of PSAT1 mediate metabolic adaptation to glutamine blockade

Project description:Cultured cancer cells frequently rely on the consumption of glutamine and its subsequent hydrolysis to glutamate by the mitochondrial enzyme glutaminase (GLS). However, this metabolic addiction can be lost in the tumor microenvironment (TME), rendering GLS inhibitors ineffective in the clinic. Here, we show that seemingly glutamine-addicted breast cancer cells ultimately adapt to chronic glutamine starvation, or targeted GLS inhibition, via the AMPK-mediated upregulation of the serine synthesis pathway (SSP). In this context, the key product of the SSP is not serine itself, but a-ketoglutarate (a-KG). Mechanistically, we find that the phylogenetically distinct transaminase phosphoserine aminotransferase 1 (PSAT1) has a unique capacity for sustained a-KG production when glutamate is severely depleted. Breast cancer cells with intrinsic or acquired resistance to glutamine starvation or GLS inhibition are highly dependent on SSP-supplied a-KG. Accordingly, pharmacological disruption of the SSP prevents adaptation to glutamine blockade, yielding a potent drug synergism that abolishes breast tumor growth in vivo. These findings highlight how metabolic redundancy can be context dependent, with the catalytic properties of different metabolic enzymes that act on the same substrate determining which pathways can support tumor growth in a particular nutrient environment. This in turn has practical consequences for therapies targeting cancer metabolism.

2024-07-05 | GSE263696 | GEO

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