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Quantitative proteomic analysis was developed on the colon of IF1-KO and control mice

ABSTRACT: We performed a quantitative proteomic analysis of colon tissue extracts from CRL and IF1-KO mice with isobaric tags for relative and absolute quantitation (iTRAQ) labeling method coupled to tandem mass spectrometry (MS/MS).

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Colon

SUBMITTER: Sonia Domínguez

LAB HEAD: José Manuel Cuezva

PROVIDER: PXD038107 | Pride | 2023-10-24

REPOSITORIES: Pride

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IF1 ablation prevents ATP synthase oligomerization, enhances mitochondrial ATP turnover and promotes an adenosine-mediated pro-inflammatory phenotype.

Domínguez-Zorita Sonia S Romero-Carramiñana Inés I Santacatterina Fulvio F Esparza-Moltó Pau B PB Simó Carolina C Del-Arco Araceli A Núñez de Arenas Cristina C Saiz Jorge J Barbas Coral C Cuezva José M JM

Cell death & disease 20230712 7

ATPase Inhibitory Factor 1 (IF1) regulates the activity of mitochondrial ATP synthase. The expression of IF1 in differentiated human and mouse cells is highly variable. In intestinal cells, the overexpression of IF1 protects against colon inflammation. Herein, we have developed a conditional IF1-knockout mouse model in intestinal epithelium to investigate the role of IF1 in mitochondrial function and tissue homeostasis. The results show that IF1-ablated mice have increased ATP synthase/hydrolase ...[more]

PMID: 37433784

Similar Datasets

Quantitative proteomic analysis of colon tissue extracts from CRL and IF1-KO mice

Project description:Quantitative proteomic analysis of colon tissue extracts from CRL and IF1-KO mice was performed with isobaric tags for relative and absolute quantitation (iTRAQ) labeling method coupled to tandem mass spectrometry (MS/MS).

2023-10-24 | PXD038151 | Pride

Genetic regulation of the ATP synthase in neurons modulates cognition

Project description:The mitochondrial ATP synthase produces ATP by oxidative phosphorylation and integrates different signals to regulate cellular functions and fate. The ATPase inhibitory factor 1 (IF1) is a structurally-disordered protein that inhibits the ATP synthase, contributing to metabolic reprogramming and signalling through mitochondrial reactive oxygen species (mtROS). mtROS regulate kinases and transcription factors in mitohormetic responses that favour adaptation to toxic insults2. IF1 is tissue-specifically expressed and in human and mouse brain is in molar excess over the ATP synthase. Herein, we have used genetic approaches to ablate or overexpress IF1 in neurons to investigate its role in brain functions. IF1 inhibits a fraction of the ATP synthase under physiological conditions and regulates respiration, mtROS production and mitochondrial structure. Transcriptomic, proteomic and metabolomic analyses indicate that IF1 regulates synaptic transmission and cognition. Ablation of IF1 impairs short-term memory whereas IF1 overexpression increases basal synaptic transmission and learning by mtROS-dependent activation of the extracellular signal-regulated kinases 1/2 (ERK 1/2). Overall, we show that IF1 dose plays a fundamental role in the regulation of neuronal function by controlling the fraction of inhibited ATP synthase that acts as source of mitohormetic mtROS, further emphasizing the ATP synthase/IF1 as promising targets to treat cognitive disorders.

2021-05-24 | PXD020262 | Pride

Skeletal muscle wt and OXPHOS inhibited 18 months-old mice

Project description:TMT sixplex Isobaric Mass Tagging (TAM) analysis was carried out in the CBMSO Protein Chemistry Facility (ProteoRed, PRB3-ISCIII and UAM University, Spain. Chronic skeletal muscle mitochondria dyshomeostasis drives tubular aggregate formation.

2022-08-12 | PXD026771 | Pride

Skeletal muscle wt and OXPHOS inhibited 18 months-old mice treated with edaravone

Project description:Chronic skeletal muscle mitochondria dyshomeostasis drives tubular aggregate formation. TMT sixplex Isobaric Mass Tagging analysis was carried out in the CBMSO Protein Chemistry Facility (ProteoRed, PRB3-ISCIII and UAM University, Spain.

2022-08-12 | PXD026722 | Pride

C2C12 myoblast WT vs ETFDH-ko TMT

Project description:ETFDH (electron transfer flavoprotein ubiquinone oxidoreductase) is a 64 kDa protein monomer located in the inner mitochondrial membrane, in charge of transferring the electrons received from the electron transfer flavoprotein ETF to the Coenzyme Q (Q). Pathological mutations in ETFDH lead to Multiple Acyl-CoA Dehydrogenase Deficiency (MADD; OMIM #231680). C2C12 cells lacking ETFDH were analysed by TMT analysis and compared to wt cells.

2023-10-24 | PXD041825 | Pride

Proteins present in tears from control, MCI and Alzheimer disease patients

Project description:we investigated tear fluid as a novel source of disease-specific protein biomarkers for Alzheimer disease (AD) development using samples from patients suffering from mild cognitive impairment (MCI) and AD. Tear protein content was evaluated via liquid chromatography–mass spectrometry.

2019-11-04 | PXD014475 | Pride

Antimycin A-treated vs ETFDH-ko myoblasts TMT

Project description:The electron transfer flavoprotein dehydrogenase (ETFDH) is the bottleneck enzyme of fatty acid oxidation (FAO). We performed a TMT 6plex analysis on Antimycin A treated and ETFDH-ko myoblasts (compared to CRL).

2023-10-24 | PXD045588 | Pride

Proteome of the EPS of Lotmaria passim promastigotes

Project description:Honeybee health is a major ecological, agricultural and societal concern due to the critical role of these insects for plant reproduction and the massive losses of colonies observed within the last decade. The search for abiotic (e.g. pesticides) and biotic (e.g. pathogens) stressors is essential for understanding bee declines and design protection plans. Flagellated Trypanosomatid protozoan parasites and particularly Lotmaria passim, are widely distributed in honeybee colonies and have been associated with colony losses. However, little is known about their life cycles, routes for transmission and the strategies for survival inside and outside their hosts. Here we describe the proteome of L. passim Extracellular polymeric substances linked to secretion of Extracellular vesicles using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). The EPS-EVs composition will provide clues on how these pathogens survive and spread in apiaries worldwide.

2024-02-15 | PXD040355 | Pride

Metabolic pathways affected by Anaplasma in tick cells

Project description:Anaplasma phagocytophilum is an emerging zoonotic pathogen that causes human granulocytic anaplasmosis. These intracellular bacteria establish infection by affecting cell function in both the vertebrate host and the tick vector, Ixodes scapularis. Previous studies have characterized the tick transcriptome and proteome in response to A. phagocytophilum infection. However, in the post-genomic era, the integration of omics datasets through a systems biology approach allows network-based analyses to describe the complexity and functionality of biological systems such as host-pathogen interactions and the discovery of new targets for prevention and control of infectious diseases. This study reports for the first time a systems biology integration of metabolomics, transcriptomics and proteomics data to characterize essential metabolic pathways involved in the response of tick cells to A. phagocytophilum infection. The results showed that infection affected protein processing in endoplasmic reticulum and glucose metabolic pathways in tick cells. These results supported tick-Anaplasma co-evolution by providing new evidence of how tick cells limit pathogen infection, while the pathogen benefits from the tick cell response to establish infection. The results suggested that A. phagocytophilum induces protein misfolding to limit the tick cell response and facilitate infection, but requires protein degradation to prevent ER stress and cell apoptosis to survive in infected cells. Additionally, A. phagocytophilum may benefit from the tick cell’s ability to limit bacterial infection through PEPCK inhibition leading to decreased glucose metabolism, which also results in the inhibition of cell apoptosis that increases infection of tick cells. These results support the use of this experimental approach to systematically identify tick cell pathways and molecular mechanisms involved in tick-pathogen interactions.

2015-10-05 | PXD002181 | Pride

Changes in the turnover of the cellular proteome during metabolic reprogramming: A role for mtROS in proteostasis

Project description:The role played by protein turnover in metabolic reprogramming is unknown. Herein, using a SILAC approach, we have studied the changes in the half-life of two hundred and sixty-six proteins of energy metabolism and of translation during the metabolic switch induced by the prolyl hydroxylases inhibitor dimethyloxalylglycine (DMOG). DMOG induces HIF-1α expression and triggers the activation of glycolysis and the concurrent inhibition of mitochondrial respiration in colon cancer cells. Changes in the activity of energy provision pathways correlated with increased turnover rates of glycolytic enzymes and the stabilization of mitochondrial proteins. Moreover, reprograming also stabilized the proteins of translation. The partial DMOG-mediated arrest of the synthesis of mitochondrial and translation proteins results from the inhibition of the mTORC1/p70SK/S6 signaling pathway. In contrast, DMOG stimulated the synthesis of glycolytic enzymes, emphasizing the opposite and differential regulation of the two pathways of energy provision. Addition of MitoQ, a mitochondrial reactive oxygen species (mtROS) scavenger, stabilized the turnover of cellular proteins similarly as when protein degradation is inhibited with leupeptin, a serine-protease inhibitor. Overall, the results show that the higher the activity of a pathway the lower is the half-life of the proteins involved and suggest a role for mtROS in cellular proteostasis.

2019-07-15 | PXD013482 | Pride

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