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TRP14 is the rate limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation.

ABSTRACT: Identification of cysteinylated proteins in parental HEK cells and TRP14 knockdown HEK cells.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Luz Valero

LAB HEAD: Juan Sastre

PROVIDER: PXD050210 | Pride | 2024-05-10

REPOSITORIES: Pride

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			Action	DRS
	PM_190207-sample1.wiff	Wiff
	PM_190207-sample1.wiff.scan	Wiff
	PM_190207-sample1_MGFPeaklist.mgf	Mgf
	PM_190207-sample2.wiff	Wiff
	PM_190207-sample2.wiff.scan	Wiff

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TRP14 is the rate limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. 42 proteins showed higher cysteinylation levels in TRP14 knockdown cells compared to wild-type cells upon biotinylated cysteine incubation and subsequent streptavidin pulldown. Figure 2C.

Project description:It has remained unknown how cells reduce cystine taken up from the extracellular space, which is a required step for further utilization of cysteine in key processes such as protein or glutathione synthesis. Here we show that the thioredoxin-related protein of 14 kDa (TRP14, encoded by TXNDC17) is the rate limiting enzyme for intracellular cystine reduction. When TRP14 is genetically knocked out, cysteine synthesis through the transsulfuration pathway becomes the major source of cysteine in human cells, and knockout of both pathways becomes lethal in C. elegans subjected to proteostatic stress. TRP14 can also reduce cysteinyl moieties on proteins, rescuing their activities as here shown with cysteinylated peroxiredoxin 2. Txndc17 knock-out mice were, surprisingly, protected in an acute pancreatitis model, concomitant with activation of Nrf2-driven antioxidant pathways and upregulation of transsulfuration. We conclude that TRP14 is the evolutionary conserved enzyme principally responsible for intracellular cystine reduction in C. elegans, mice and humans.

2024-06-05 | PXD038965 | Pride

Bull sperm SWATH-MS-based proteomics reveals link between high fertility and energy production, motility structures, and sperm-oocyte interaction. Quantitation

Project description:Prediction of male or semen fertility potential remains a persistent challenge that has yet to be fully resolved. This work analyzed several in vitro parameters and proteome of spermatozoa in bulls cataloged as high (HF; n=5) and low field (LF; n=5) fertility after more than a thousand artificial inseminations. Sperm motility was evaluated by Computer-Assisted Sperm Analysis. Sperm viability, mitochondrial membrane potential (MMP), and reactive oxygen species (mROS) of spermatozoa were assessed by flow cytometry. Proteome was evaluated by SWATH-MS procedure. Spermatozoa of HF bulls showed significantly higher total motility than the LF group (41.4% vs. 29.7%). Rates of healthy sperm (live, high MMP, and low mROS) for HF and LF bull groups were 49% and 43%, respectively (p > 0.05). Spermatozoa of HF bulls showed higher presence of differentially abundant proteins (DAPs) related to both energy production (COX7C), mainly OXPHOS pathway, and to the development of structures linked with the motility process (TPPP2, SSMEM1 and SPAG16). Furthermore, we observed that EQTN, together with other DAPs related to the interaction with the oocyte, were overrepresented in HF bull spermatozoa. The biological processes related to protein processing, catabolism, and protein folding were found to be overrepresented in LF bull sperm in which the HSP90AA1 chaperone was identified as the most DAP

2023-10-18 | PXD042286 | Pride

Cryopreservation differently alters proteome in epididymal and ejaculated pig spermatozoa

Project description:Cryopreservation induces differential remodeling of the proteome in mammalian spermatozoa. How these proteome changes relate with the loss of sperm function during cryopreservation remains unsolved. The present study attempted to clarify this issue evaluating differential changes in the proteome of pig spermatozoa retrieved from the cauda epididymis and the ejaculate, with clear differences in cryotolerance, comparing fresh and frozen-thawed cells. Sperm samples were collected from 10 healthy, sexually mature and fertile boars, and cryopreserved using a standard 0.5 mL straw protocol. Total and progressive motility, viability and mitochondria membrane potential were higher and membrane fluidity and reactive oxygen species generation lower in frozen-thawed (FT) cauda epididymal than ejaculated spermatozoa. Quantitative proteomics of fresh and FT sperm samples were analyzed using a LC-ESI-MS/MS-based SWATH approach. Cryopreservation quantitatively altered more proteins in ejaculated than cauda epididymal spermatozoa. Differential protein-protein networks highlighted a set of proteins directly involved in mitochondrial functionality among those quantitatively altered in ejaculated spermatozoa, which would explain the worse post-thaw quality of ejaculated pig spermatozoa.

2019-11-11 | PXD012984 | Pride

Proteomic and pathway profiling of four Breast Cancer cell lines.

Project description:Biomarker discovery in breast cancer (BC) is a clinical need for therapeutics and non-invasive diagnostics. In a single study, we provide a comparative differential proteomic profile of four invasion, metastasis, angiogenesis and drug resistance. Exosome proteome profile reflects their different BC cell origin suggesting potential indicators of BC subtype. Further, our pathway inference analysis reveals a differential role of exosomes in BC signalling pathways in recipient cells, according to their protein cargo and cell origin. Our results may significantly contribute to further studies for the design of BC biomarker predictor to stratify BC patients and the development of novel therapeutic strategies.BC cell lines and their derived- exosomes, representative of the most relevant BC subtypes in clinic. Differentially-expressed proteins, in both cells and exosomes, include indicators of

2024-10-17 | PXD024304 | Pride

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2020-10-19 | PXD019542 | Pride

Phosphoproteomics of porcine neutrophils infected by Salmonella Typhimurium

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2024-07-30 | PXD037112 | Pride

Translation factor eIF5A controls mitochondrial protein import through the translation regulation of the mitochondrial inner membrane translocase receptor Tim50

Project description:The import of nuclear-encoded proteins into mitochondria is a key process for the right mitochondrial function. The evolutionarily conserved translation factor eIF5A is primarily known as an elongation factor which binds ribosomes to facilitate the translation of motifs with polyprolines or combinations of proline with glycine and charged amino acids. eIF5A expression is up-regulated by the transcription factor Hap1 under respiratory conditions and is essential to maintain the mitochondrial activity. Here we identify an essential polyproline-containing protein as a direct eIF5A target for translation: the mitochondrial inner membrane protein Tim50, which is the receptor subunit of the TIM23 translocase complex. We show how eIF5A directly controls the mitochondrial protein import through the alleviation of ribosome stalling along Tim50 sequence at the mitochondrial surface. Thus, the absence of eIF5A leads to the accumulation of mitochondrial protein precursors in the cytosol as well as to the induction of the mitoCPR stress response. Moreover, we show that eIF5A also affects mitochondrial functionality by reducing the translation and levels of many mitochondrial proteins. Overall, these results show for the first time how ribosome stalling negatively impacts the mitochondrial import process and explain why eIF5A is essential for the mitochondrial function.

2024-10-23 | PXD043905 | Pride

The proteome of large or small extracellular vesicles in pig seminal plasma differs and defines sources and biological functions. Spectral Library

Project description:Seminal plasma contains many and morphologically heterogeneous extracellular vesicles (sEVs) which, released by cells of the testis, epididymis and accessory sex glands, are involved in male and female reproductive processes. The goal of this study was to describe the proteome of porcine sEVs isolated by a size exclusion chromatography (SEC)-based procedure and size-classed as small (S-EVs) or large (L-EVs). The sEV-subsets were characterized for their total protein concentration, morphology, size distribution, EV-specific protein markers and purity. A total of 988 proteins were identified by LC-MS/MS and 737 of them were quantified by SWATH in S-EVs, L-EVs and EVs-free samples. The differential expression analysis revealed 197 differentially abundant proteins between both EV-subsets, and 37 and 199 between S-EVs and L-EVs vs EVs-free samples, respectively. The gene ontology (GO) enrichment analysis of differentially abundant proteins suggested, by the type of protein detected, that S-EVs would be released mainly through an apocrine blebbing pathway and be involved in modulating the immune environment of the female reproductive tract as well as during sperm-oocyte interaction. In contrast, the protein types detected might imply L-EVs are released by fusion of multivesicular bodies with the plasma membrane and would be involved in sperm physiological processes, such as capacitation and avoidance of oxidative stress. In conclusion, this study provides a procedure capable of isolating of subsets of EVs from pig seminal plasma with a high degree of purity and shows differences in the proteomic profile between EV-subsets, suggesting different sources and biological functions.

2023-02-15 | PXD039833 | Pride

Proteomic and pathway profiling of four Breast Cancer cell lines exosomes

2024-10-17 | PXD024300 | Pride

Protein identification of spermatozoa and seminal plasma in bottlenose dolphin (Tursiops truncatus)

Project description:Proteins play an important role in many reproductive functions such as sperm maturation and physiology, sperm transit in the female genital tract or sperm-oocyte interaction. However, little information concerning reproductive features is available in the case of aquatic animals. The present study aims to characterize the proteome of both spermatozoa and seminal plasma of bottlenose dolphins (Tursiops truncatus) as a model organism for cetaceans. Ejaculate samples were obtained voluntarily from two trained dolphins housed in an aquarium. Spermatozoa and seminal plasma were analyzed by means of proteomic analyses using a LC-MS/MS and a list with the gene symbols corresponding to each protein was submitted to DAVID database. A total of 423 and 307 proteins were identified in spermatozoa and seminal plasma, respectively, and the samples shared 111 proteins. Furthermore, 70 proteins were identified as involved in reproductive processes, 39 in spermatozoa, and 31 in seminal plasma. The top-5 most abundant proteins were also identified in these samples: AKAP3, ODF2, TUBB, GST3, ROPN1 for spermatozoa and CST11, LTF, ALB, HSP90B1, PIGR for seminal plasma. In conclusion, this proteomic study provides the first characterization of proteomic expression patterns in cetacean sperm and seminal plasma, opening a window to future research on the discovery of biomarkers, analysis of conservation capacity or additional applications in the field of assisted reproduction technologies.

2021-06-14 | PXD024588 | Pride

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