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Transcriptome analysis of Cox4-2 knockout mice after OVA challenge

ABSTRACT: Cytochrome c oxidase (COX) is a 13-subunit enzyme that is a key complex of the oxidative phosphorylation system of the mitochondria, which generates the vast majority of the energy of the cell.COX subunit IV is the largest nuclear-encode subunit with important regulatory functions concerning energy metabolism. COX4-2 has been knocked out. Our study indicated strong expression of Cox4-2 in lung and therefore we test this mutant line under OVA-challenge conditions expecting a new asthma mouse model.

ORGANISM(S): Mus musculus

PROVIDER: GSE49694 | GEO | 2015/07/15

SECONDARY ACCESSION(S): PRJNA214789

REPOSITORIES: GEO

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Transcriptome analysis of Cox4-2 knockout mice after OVA challenge

Project description:Cytochrome c oxidase (COX) is a 13-subunit enzyme that is a key complex of the oxidative phosphorylation system of the mitochondria, which generates the vast majority of the energy of the cell.COX subunit IV is the largest nuclear-encode subunit with important regulatory functions concerning energy metabolism. COX4-2 has been knocked out. Our study indicated strong expression of Cox4-2 in lung and therefore we test this mutant line under OVA-challenge conditions expecting a new asthma mouse model. Total RNA obtained from 1/2 lung of 4 female mice of each analysed group (widltype, wildtype challenged, mutant, mutant challenged)

2015-07-15 | E-GEOD-49694 | biostudies-arrayexpress

Effects of OVA challenge in mouse model of asthma

Project description:Challenge with ovalbumin antigen is a common model for asthma in mice. We sought to identify the gene expression differences in lung tissue in naïve and OVA-sensitized mice, in response to OVA challenge.

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Project description:cytochrome oxidase subunit 1(cox1) amplicon sequencing

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Project description:cytochrome oxidase subunit 1(cox1) amplicon sequencing

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Effect of normal and COX6A2-deficient human pluripotent stem cells on gene expression during cardiomyocyte differentiation.

Project description:Cardiac remodeling is the initiating factor for the development of heart failure, which can result from various cardiomyopathies. Cytochrome c oxidase subunit 6A2 (COX6A2) is one of the components of cytochrome c oxidase that drives oxidative phosphorylation. We here report a COX6A2-deficient human cardiac myocyte (CM) model that mimicked the human COX6A2 homozygous mutation and determined the effects of COX6A2 dysfunction and its underlying mechanism.COX6A2 gene knockout did not affect the pluripotency and differentiation efficiency of hiPSCs. Myocardial cells with a COX6A2 gene knockout showed abnormal energy metabolism, increased oxidative stress levels, abnormal calcium transport activity, and decreased contractility. In addition, L-carnitine and trimetazidine significantly improved energy metabolism in the COX6A2-deficient human myocardial model. Taken together, our data provide a COX6A2-deficient human cardiomyocyte model that exhibits abnormal energy metabolism, this model represents an important tool to gain insight into the mechanism of action of energy metabolism disorders resulting in myocardial remodeling, elucidate the gene-phenotype relationship of COX6A2 deficiency, and facilitate drug screening.

2023-11-18 | GSE247580 | GEO

Project description:Cyanea nozakii cytochrome c oxidase subunit I (COI) gene

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Molecular characterization of a complex of Apoptosis Inducing Factor 1 (AIFM1) with cytochrome c oxidase of the mitochondrial respiratory chain

Project description:Combining mass spectrometry based chemical cross-linking and complexome profiling, we analyzed the interactome of heart mitochondria. We focused on complexes of oxidative phosphorylation and found that dimeric apoptosis inducing factor 1 (AIFM1) forms a defined complex with ~10% of monomeric cytochrome c oxidase (COX), but hardly interacts with respiratory chain supercomplexes. Multiple AIFM1 inter-crosslinks engaging six different COX subunits provided structural restraints to build a detailed atomic model of the COX-AIFM12 complex. Application of two complementary proteomic approaches thus provided unexpected insight into the macromolecular organization of the mitochondrial complexome. Our structural model excludes direct electron transfer between AIFM1 and COX. Notably however, the binding site of cytochrome c remains accessible allowing formation of a ternary complex. The discovery of the previously overlooked COX-AIFM12 complex and clues provided by the structural model hint at a role of AIFM1 in OXPHOS biogenesis and in programmed cell death.

2021-09-09 | PXD025102 | Pride

Identification of a homozygous SCO2 variant in two siblings strengthens the concept of this gene being causative for early-onset axonal Charcot-Marie-Tooth neuropathy

Project description:The mitochondrial resident SCO2 protein acts as a copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Recessive mutations in the synthesis of cytochrome C oxidase 2 gene SCO2 were reported in several cases with fatal infantile cardioencephalomyopathy associated with COX deficiency and in four cases with axonal neuropathy. Further confirming the phenotypic spectrum, we identified a homozygous variant (c.361G>C; p.(Gly121Arg)) in SCO2 in two brothers with axonal motor neuropathy. In contrast to most cases, our patients developed exclusively a motor neuropathy, and especially did not present with cardiomyopathy (leading to death in early infancy). Based on the classification of the detected amino acid substitution p.(Gly121Arg) as a variant of uncertain significance (VUS3), further studies toward a robust validation were carried out: results of segregation analysis showed homozygosity only in the two index patients but not in the healthy siblings. Protein studies including proteomic profiling showed an effect on the proteomic signature and accord with a pathogenic character of the amino acid substitution impacting on COX subunit assembly with a profound decrease of subunit II as well as on the homeostasis of proteins beyond mitochondria including such belonging to endocytic processes and opioid uptake. Hence, our combined studies strengthen the concept of SCO2 being causative for early-onset axonal Charcot-Marie-Tooth neuropathy, extend the mutational spectrum associated with this phenotype by introducing the first causative homozygous variant and provide first biochemical insights into the etiopathology.

2024-05-22 | PXD026283 | Pride

Compensatory electron transfer from the ubiquinol pool circumvents cytochrome c oxidase deficiency and restores effector and memory T cell function

Project description:The ultimate goal of immunometabolism is to modulate metabolic pathways to enhance immunity. Here, we investigate the potential of an alternative oxidase (AOX) to counteract cytochrome c oxidase (COX) deficiency in T cells. COX is vital for oxidative phosphorylation (OXPHOS), and its deficiency leads to redox imbalances, impaired metabolism, reactive oxygen species (ROS), and apoptosis, resulting in T cell immunodeficiency. We introduced an AOX into COX-deficient T cells, which revealed a normalization of genes involved in redox balance, apoptosis, and metabolic pathways. Mitochondrial function, glycolysis and TCA cycle function were also restored. AOX-enhanced T cells showed improved activation, proliferation, differentiation, and memory formation, resulting in better immune responses against viral challenges. These findings suggest that targeting the ubiquinol pool could be a promising therapeutic strategy for enhancing T cell function in conditions characterized by COX dysfunction and compromised immune responses.

2024-10-02 | GSE269797 | GEO

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