Knockout of the Acyl CoA binding protein (ACBP) in mice - expression profile from the liver of 21 days old ACBP-/- and +/+ mice.
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE24451 | GEO | 2010/11/26
SECONDARY ACCESSION(S): PRJNA132695
REPOSITORIES: GEO
Similar Datasets
Project description:The ACBP knockout were created by targeted disruption of the gene in mice. The expression profiling was performed on liver tissue from ACBP-/- (KO) and +/+ (WT) mice at the age of 21 days, which in our study is the time immediately before weaning. The mice used for this experiment were taken directly away from their mother. Thus, having free access to chow and breast milk until sacrificed at 8-11am 15 ACBP-/- and 15 +/+ control mice divided into 6 groups (KO1, KO2, KO3, WT1, WT2 and WT3) with 5 individuals in each group were used for this study.
2010-11-26 | E-GEOD-24451 | biostudies-arrayexpress
Project description:Acyl coenzyme A binding protein (ACBP), encoded by the diazepam binding protein (DBI) gene, plays a pivotal role in stimulating appetite and lipo-anabolic reactions, showing correlations with laboratory indications of metabolic syndrome in ostensibly healthy individuals. In a screening effort targeting inhibitors of ACBP/DBI expression among distinct neuroendocrine factors, we discovered that glucocorticoids induce ACBP/DBI secretion in cultured cells. In mouse models of iatrogenic Cushing syndrome, antibody-mediated neutralization of ACBP/DBI prevented the metabolic consequences of prolonged glucocorticoid administration. Our findings suggest that a surge in extracellular ACBP/DBI may mediate crucial aspects of Cushing syndrome.
2024-10-02 | GSE248672 | GEO
Project description:The plasma concentrations of acyl coenzyme A binding protein (ACBP, also known as diazepam-binding inhibitor, DBI, or ‘endozepine’) increase with age and obesity, two parameters that are also the most important risk factors for cancer. In mice bearing MCA205 fibrosarcoma, antibody mediated ACBP/DBI neutralization enhanced the anticancer T-cell response in the context of chemoimmunotherapy. T-cells infiltrating MCA205 tumors were sorted and submitting to single-cell TCR sequencing and single-cell RNA sequencing (scRNAseq) to identify the mechanisms driving this improvement.
2024-09-11 | GSE242119 | GEO
Project description:Total liver RNA extracts from adult male mice (8 weeks old, C57BL/6) injected with monoclonal anti-ACBP/DBI (1 dose per week) and subjected to Methionine and Choline Deficient Diet (regime duration: 4weeks) were analyzed to describe the effect of neutralization of ACBP/DBI to NASH-induced transcriptomic alterations.
2023-02-24 | GSE194346 | GEO
Project description:Acyl-CoA-binding protein (ACBP) is a 10 kDa protein that binds C12-C22 acyl-CoA esters with high affinity. In vitro and in vivo experiments suggest that it is involved in multiple cellular tasks including modulation of fatty acid biosynthesis, enzyme regulation, regulation of the intracellular acyl-CoA pool size, donation of acyl-CoA esters for beta-oxidation, vesicular trafficking, complex lipid synthesis and gene regulation. In the present study, we delineate the evolutionary history of ACBP to get a complete picture of its evolution and distribution among species. ACBP homologues were identified in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and eleven eubacterial species. ACBP homologues were not detected in any other known bacterial species, or in archaea. Nearly all of the ACBP-containing bacteria are pathogenic to plants or animals, suggesting that an ACBP gene could have been acquired from a eukaryotic host by horizontal gene transfer. Many bacterial, fungal and higher eukaryotic species only harbour a single ACBP homologue. However, a number of species, ranging from protozoa to vertebrates, have evolved two to six lineage-specific paralogues through gene duplication and/or retrotransposition events. The ACBP protein is highly conserved across phylums, and the majority of ACBP genes are subjected to strong purifying selection. Experimental evidence indicates that the function of ACBP has been conserved from yeast to humans and that the multiple lineage-specific paralogues have evolved altered functions. The appearance of ACBP very early on in evolution points towards a fundamental role of ACBP in acyl-CoA metabolism, including ceramide synthesis and in signalling.
| S-EPMC1316265 | biostudies-literature
Project description:Recently, we reported that, in mice, hunger causes the autophagy-dependent release of a protein called "acyl-CoA-binding protein" or "diazepam binding inhibitor" (ACBP/DBI) from cells, resulting in an increase in plasma ACBP concentrations. Administration of extra ACBP is orexigenic and obesogenic, while its neutralization is anorexigenic in mice, suggesting that ACBP is a major stimulator of appetite and lipo-anabolism. Accordingly, obese persons have higher circulating ACBP levels than lean individuals, and anorexia nervosa is associated with subnormal ACBP plasma concentrations. Here, we investigated whether ACBP might play a phylogenetically conserved role in appetite stimulation. We found that extracellular ACBP favors sporulation in Saccharomyces cerevisiae, knowing that sporulation is a strategy for yeast to seek new food sources. Moreover, in the nematode Caenorhabditis elegans, ACBP increased the ingestion of bacteria as well as the frequency pharyngeal pumping. These observations indicate that ACBP has a phylogenetically ancient role as a 'hunger factor' that favors food intake.
| S-EPMC6944704 | biostudies-literature
Project description:Total liver RNA extracts from adult female mice (8-week-old) subjected to CRS (chronic restraint stress) or CDDP (cisplatin) induced anorexia with or without ACBP/DBI delivery to investigate the impact of ACBP/DBI on anorexia-induced transcriptomic alterations.
2024-07-12 | GSE237766 | GEO
Project description:G-quadruplex structure (G4) is a type of DNA secondary structure that widely exists in the genomes of many organisms. G4s are believed to participate in multiple biological processes. Acyl- CoA binding protein (ACBP), a ubiquitously expressed and highly conserved protein in eukaryotic cells, plays important roles in lipid metabolism by transporting and protecting acyl-CoA esters. Here, we report the functional identification of a G4 in the promoter of the ACBP gene in silkworm and human cancer cells. We found that G4 exists as a conserved element in the promoters of ACBP genes in invertebrates and vertebrates. The BmACBP G4 bound with G4-binding protein LARK regulated BmACBP transcription, which was blocked by the G4 stabilizer pyridostatin (PDS) and G4 antisense oligonucleotides. PDS treatment with 5 th instar silkworm larvae decreased the BmACBP expression and triacylglycerides (TAG) level, resulting in reductions in fat body mass, body size and weight and growth and metamorphic rates. PDS treatment and knocking out of the HsACBP G4 in human hepatic adenocarcinoma HepG2 cells inhibited the expression of HsACBP and decreased the TAG level and cell proliferation. Altogether, our findings suggest that G4 of the ACBP genes is involved in regulation of lipid metabolism processes in invertebrates and vertebrates.
2022-05-04 | GSE201939 | GEO
Project description:Eight male C57BL/6 mice were used in this study. Four (denoted by My*, V*, E*, S*) of the mice were from the same litter of one biological mother (207H), and the other four mice (denoted by J, Ms, N, U) were from the same litter of another biological mother (189C). To explore the potential maternal and co-housing effects, the eight mice were housed in three different individual ventilated cages as follows: My* and V* (littermates of mother mouse 207H) were housed in cage 1; N and U (littermates of mother mouse 189C) were housed in cage 3; E* and S* (littermates of mother mouse 207H), and J and Ms (littermates of mother mouse 189C) were co-housed in cage 2. All mice were housed in a 12-hr light/dark cycle and fed irra- diated water and standard food after weaning at the age of 21 days. Mice were obtained from the Animal and Plant Care Facility of The Hong Kong University of Science and Technology, and were bred at the core facility. All experimental procedures involving animals were conducted in compliance with the Animal User Manual and approval was obtained from the Animal Ethics Committee of The Hong Kong University of Science and Technology.
Fecal samples of each mouse were independently collected on the 21st, 22nd, 23rd, 29th, 30th, and 31st day after birth. For individual mouse, fecal samples from the 21st and 22nd day (--3 weeks of age, 1st and 2nd day after weaning), and samples from the 29th and 30th day (--4 weeks of age, 9th and 10th day after weaning), were pooled and subjected to metagenomic sequencing, respectively; samples from the 23rd day (--3 weeks of age, 3rd day after weaning), and the 31 days (--4 weeks of age, 11th day after weaning) were subjected to metaproteomic analysis separately.
The 16 metaproteomic samples were analyzed by metaSpectraST, which indicated a clear gut microbiome changes throughout the short period after weaning, which was possibly associated with the dietary shift from milk to solid food, while no distinctive changes were observed by metagenomic analysis.
2022-05-09 | MSV000089443 | MassIVE
Project description:The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved. ACBP is a carrier for activated long-chain fatty acids and has been associated with many aspects of lipid metabolism. Its secondary structure is highly similar to that of the corresponding form of bovine ACBP and exhibits the unique flattened alpha-helical bundle (up-down-down-up) motif reported for animal, yeast and insect ACBPs. Conformational differences are located in loops and turns, although these structural differences do not suffice to account for features that could be related to the unusual biochemistry and lipid metabolism of the Harderian gland.
| S-EPMC2225200 | biostudies-literature