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Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Mus musculus

PROVIDER: GSE122863 | GEO | 2018/11/30

REPOSITORIES: GEO

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Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [microarray]

Project description:Immunological memory is central to adaptive immunity and protection from disease. Changing metabolic demands as antigen-specific T cells transition from effector to memory have been well documented, but the cell-specific pathways and molecules that govern this transition are poorly defined. ACC1 is a rate-limiting enzym in fatty acid biosynthesis. We show that genetic deletion of ACC1 enhanced the formation of CD4+ T cell memory, and that inhibition of ACC1 function enhanced memory T cell formation during parasite infection in mice. ACC1-deficient effector Th cells had similar metabolic signatures to wild-type memory Th cells, and Acaca expression was inversely correlated with a memory gene signature in individual cells. Single cell analysis allowed us to identify a memory precursor-enriched population (CCR7hiCD137lo) present during early differentiation of effector CD4+ T cells. Thus, fatty acid metabolism directs cell fate determination during the generation of memory CD4+ T cells.

2018-11-30 | GSE122861 | GEO

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RNA-seq]

2018-11-30 | GSE120667 | GEO

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RT-PCR]

2018-11-30 | GSE122862 | GEO

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis

Project description:Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis

| PRJNA506713 | ENA

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [microarray]

Project description:Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [microarray]

| PRJNA506715 | ENA

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RNA-seq]

Project description:Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RNA-seq]

| PRJNA494052 | ENA

Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RT-PCR]

Project description:Acc1 determines memory potential of individual CD4+ T cells by regulating de novo fatty acid biosynthesis [RT-PCR]

| PRJNA506717 | ENA

Hepatic de novo lipogenesis is present in liver-specific ACC1-deficient mice.

Project description:Acetyl coenzyme A (acetyl-CoA) carboxylase (ACC) catalyzes carboxylation of acetyl-CoA to form malonyl-CoA. In mammals, two isozymes exist with distinct physiological roles: cytosolic ACC1 participates in de novo lipogenesis (DNL), and mitochondrial ACC2 is involved in negative regulation of mitochondrial beta-oxidation. Since systemic ACC1 null mice were embryonic lethal, to clarify the physiological role of ACC1 in hepatic DNL, we generated the liver-specific ACC1 null mouse by crossbreeding of an Acc1(lox(ex46)) mouse, in which exon 46 of Acc1 was flanked by two loxP sequences and the liver-specific Cre transgenic mouse. In liver-specific ACC1 null mice, neither hepatic Acc1 mRNA nor protein was detected. However, to compensate for ACC1 function, hepatic ACC2 protein and activity were induced 1.4 and 2.2 times, respectively. Surprisingly, hepatic DNL and malonyl-CoA were maintained at the same physiological levels as in wild-type mice. Furthermore, hepatic DNL was completely inhibited by an ACC1/2 dual inhibitor, 5-tetradecyloxyl-2-furancarboxylic acid. These results strongly demonstrate that malonyl-CoA from ACC2 can access fatty acid synthase and become the substrate for the DNL pathway under the unphysiological circumstances that result with ACC1 disruption. Therefore, there does not appear to be strict compartmentalization of malonyl-CoA from either of the ACC isozymes in the liver.

| S-EPMC1820479 | biostudies-literature

Mitochondrial protein import determines lifespan through metabolic reprogramming and de novo serine biosynthesis.

Project description:Sustained mitochondrial fitness relies on coordinated biogenesis and clearance. Both processes are regulated by constant targeting of proteins into the organelle. Thus, mitochondrial protein import sets the pace for mitochondrial abundance and function. However, our understanding of mitochondrial protein translocation as a regulator of longevity remains enigmatic. Here, we targeted the main protein import translocases and assessed their contribution to mitochondrial abundance and organismal physiology. We find that reduction in cellular mitochondrial load through mitochondrial protein import system suppression, referred to as MitoMISS, elicits a distinct longevity paradigm. We show that MitoMISS triggers the mitochondrial unfolded protein response, orchestrating an adaptive reprogramming of metabolism. Glycolysis and de novo serine biosynthesis are causatively linked to longevity, whilst mitochondrial chaperone induction is dispensable for lifespan extension. Our findings extent the pro-longevity role of UPRmt and provide insight, relevant to the metabolic alterations that promote or undermine survival and longevity.

| S-EPMC8814026 | biostudies-literature

Pseudomonas aeruginosa directly shunts ?-oxidation degradation intermediates into de novo fatty acid biosynthesis.

Project description:We identified the fatty acid synthesis (FAS) initiation enzyme in Pseudomonas aeruginosa as FabY, a ?-ketoacyl synthase KASI/II domain-containing enzyme that condenses acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the FAS primer ?-acetoacetyl-ACP in the accompanying article (Y. Yuan, M. Sachdeva, J. A. Leeds, and T. C. Meredith, J. Bacteriol. 194:5171-5184, 2012). Herein, we show that growth defects stemming from deletion of fabY can be suppressed by supplementation of the growth media with exogenous decanoate fatty acid, suggesting a compensatory mechanism. Fatty acids eight carbons or longer rescue growth by generating acyl coenzyme A (acyl-CoA) thioester ?-oxidation degradation intermediates that are shunted into FAS downstream of FabY. Using a set of perdeuterated fatty acid feeding experiments, we show that the open reading frame PA3286 in P. aeruginosa PAO1 intercepts C(8)-CoA by condensation with malonyl-ACP to make the FAS intermediate ?-keto decanoyl-ACP. This key intermediate can then be extended to supply all of the cellular fatty acid needs, including both unsaturated and saturated fatty acids, along with the 3-hydroxyl fatty acid acyl groups of lipopolysaccharide. Heterologous PA3286 expression in Escherichia coli likewise established the fatty acid shunt, and characterization of recombinant ?-keto acyl synthase enzyme activity confirmed in vitro substrate specificity for medium-chain-length acyl CoA thioester acceptors. The potential for the PA3286 shunt in P. aeruginosa to curtail the efficacy of inhibitors targeting FabY, an enzyme required for FAS initiation in the absence of exogenous fatty acids, is discussed.

| S-EPMC3457203 | biostudies-literature

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