Induction of senescence in a translational cell model for testicular cells by Bleomycin treatment.
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Callithrix Jacchus
TISSUE(S): Peritubular Myoid Cell
SUBMITTER: 
Thomas Fröhlich
LAB HEAD: Thomas Fröhlich
PROVIDER: PXD073445 | Pride | 2026-05-13
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Sample_Info.txt | Txt | |||
| checksum.txt | Txt | |||
| iMKTPC_B1.raw | Raw | |||
| iMKTPC_B2.raw | Raw | |||
| iMKTPC_B3.raw | Raw |
Items per page: 5 1 - 5 of 11 |
Similar Datasets
Project description:Age-related changes of the human testis may include morphological alterations, disturbed steroidogenesis and impaired spermatogenesis. However, the specific impact of cell age remains poorly understood and difficult to assess. Testicular peritubular cells fulfill essential functions, including sperm transport, contributions to the spermatogonial stem cell niche and paracrine interactions within the testis. To study their role in age-associated decline of testicular functions, we performed comprehensive proteome and secretome analyses of repeatedly passaged peritubular cells from Callithrix jacchus. This nonhuman primate model better reflects the human testicular biology than rodents and further gives access to young donors unavailable from humans. Among 5095 identified proteins, 583 were differentially abundant between samples with low and high passage numbers. The alterations indicate a reduced ability of senescent peritubular cells to contract and secrete proteins, as well as disturbances in NF-κB signaling and a reduced capacity to handle reactive oxygen species. Since this in vitro model may not exactly mirror all molecular aspects of in vivo aging, we investigated the proteomes and secretomes of testicular peritubular cells from young and old donors. Even though the age-related alterations at the protein level were less pronounced, we found evidence for impaired protein secretion, altered NF-κB signaling and reduced contractility of these in vivo aged peritubular cells.
2020-11-18 | PXD022165 | Pride
Project description:Abstract: Clonidine has been used in clinical medicine, e.g. to treat high blood pressure, and its use has been linked to impairments of male fertility, but the underlying reasons are not known. Clonidine is an agonist at the α2A-adrenoceptor (ADRA2A) which is expressed by cells of the testis, hence interference at the testicular level is plausible to assume. Because the human testis and its cells are not readily accessible to experimental testing, we used cultured human testicular peritubular cells (HTPCs), which represent a unique experimental window into the human peritubular wall compartment to clarify direct actions of this antihypertensive drug. Immuno-histochemical / immuncytochemical and PCR techniques proved ADRA2A expression in human testis and cultured HTPCs. Clonidine when tested over a concentration range (1-1000 µM) did not visibly affect HTPC morphology and no obvious toxic actions became apparent over a 24 h period. Already at 1 µM, clonidine significantly stimulated IL6 mRNA, yet most effective increase was found at 10 µM which was used for further studies. ELISA measurements confirmed this action of clonidine. In gel contraction assays, clonidine exerted a slight relaxing action. Results of a pro-teomic study revealed that the exposure to clonidine for 24 h did not significantly change protein abundance of HTPCs. Thus, ADRA2A, is expressed in the human testis, among others in perit-ubular cells and represents a target of clonidine, other drugs and natural catecholamines. Based on our studies in HTPCs, such agonists of ADRA2A may have the potential to interfere with human testicular functions.
2024-10-17 | PXD052220 | Pride
Project description:Recent studies on the contribution of satellite cells (SC) to Duchenne muscular dystrophy (DMD) documented altered division capacities and impaired regeneration potential of SC in muscle tissue of DMD patients and animal models. Hence, it is crucial to unravel if SC-intrinsic effects trigger these deficiencies at pre-contractile stages of myogenesis rather than resulting consequently from the pathologic environment. Addressing this, we isolated SC from muscle biopsies of a porcine DMD model for cultivation and characterization.
2025-06-30 | PXD059983 | Pride
Project description:Duchenne muscular dystrophy is a fatal X-linked disease caused by mutations in the DMD gene, leading to the absence of dystrophin and progressive degeneration of skeletal and cardiac muscles. Pigs lacking DMD exon 52 (DMDΔ52) are a clinically severe model for DMD, mimicking molecular, functional, and pathological hallmarks of the human disease. Dystrophin expression can be restored by additionally deleting exon 51 (DMDΔ51-52), which reframes DMD transcripts and alleviates pathological alterations. DMDΔ51-52 pigs model Becker muscular dystrophy (BMD), a milder and slower-progressing form of muscle degeneration.
2026-03-12 | PXD064879 | Pride
Project description:The cuticles of arthropods, including aquatic crustaceans like Daphnia, provide an interface between the organism and its environment. Thus, the cuticle’s structure influences how the organism responds to and interacts with its surroundings. Here, we used label-free quantification proteomics to provide a proteome of the molted cuticle of Daphnia magna, which has long been a prominent subject of studies on ecology, evolution, and developmental biology, anddetected 278 high confidence proteins. Using protein sequence domain and functional enrichment analyses, we identified chitin-binding structural proteins and chitin modifying enzymes as most abundant protein groups in the cuticle proteome.Structural cuticular protein families showed a similar distribution to those found in other arthropods and indicated proteins responsible for the soft and flexible structure of the Daphnia cuticle . Finally, cuticle protein genes were clustered as tandem gene arrays in the Daphnia genome, indicating their importance for adaptation to environmental change. The cuticle proteome presented here will be a valuable resource to the Daphnia research community, informing investigations on diverse topics such as the genetic basis of interactions with predators and parasites.
2024-09-02 | PXD040228 | Pride
Project description:The use of cell factories to convert sugars from lignocellulosic biomass into chemicals in which oleochemicals and food additives, such as carotenoids, play an important role is essential for the shift towards sustainable processes. Rhodotorula toruloides is a yeast that naturally metabolises a wide range of substrates, including lignocellulosic hydrolysates, and converts them into lipids and carotenoids. In this study, xylose, the main component of hemicellulose, was used as the sole substrate for R. toruloides, and a detailed physiology characterisation combined with absolute proteomics and genome-scale metabolic models was carried out to understand the regulation of lipid and carotenoid production. To improve these productions, oxidative stress was induced by hydrogen peroxide and light irradiation and further enhanced by adaptive laboratory evolution. Based on the online measurements of growth and CO2 excretion, three distinct growth phases were identified during batch cultivations. The intracellular flux estimations correlated well with the measured protein levels and demonstrated improved NADPH regeneration and phosphoketolase activity and reduced beta-oxidation, correlating with increasing lipid yields. Light irradiation conditions resulted in 70% higher carotenoid and 40% higher lipid yields. The presence of hydrogen peroxide did not affect the carotenoid yield but culminated in the highest lipid yield of 0.65 ± 0.06 g/gDCW. The adapted strain showed improved fitness and 130% higher carotenoid yield than the parental strain. This work presented a holistic view of xylose conversion into microbial oil and carotenoids by R. toruloides for further cost-effective and renewable production of these molecules.
2020-07-29 | PXD019305 | Pride
Project description:Aging of the human testis and associated cellular changes are difficult to assess, thus we used a translational non-human primate model to get insights into underlying biochemical processes. Using proteomics we analyzed testicular tissue of six young (age 2 to 3) and four old (age 10 to 12) C. jacchus individuals. Mass spectrometry identified 63124 peptides, which could be assigned to 5924 proteins. Among them we found proteins, which are specific for germ cells, Leydig cells, and somatic cells, indicating the relevance of the dataset. The quantitative analysis showed 31 differentially abundant proteins, of which 29 proteins were more abundant in old animals. An increased abundance of several anti-proliferative proteins, among them CDKN2A, indicate slowed cell proliferation in older testes. Immunohistochemistry localized CDKN2A in spermatogonia and spermatocytes, suggesting altered spermatogenesis. Additionally, an increased abundance of several extracellular proteins and small leucine rich repeat proteoglycans was observed, which may be related to impaired cell migration and fibrotic events. An increased abundance of proteins with inhibitory roles in smooth muscle cell contraction like CNN1, indicate functional alterations, specifically in peritubular cells and may mirror a reduced capacity of these cells, to contract in aged testes. In summary, these results document several age-associated changes in the testicular proteome of a non-human primate model and provides new insight into testicular aging.
2021-06-21 | PXD024844 | Pride
Project description:Processing food and feed challenges official control e.g. by modifying proteins, which leads to significant underestimation in targeted, MS-based protein quantification. Whereas numerous studies identified processing-induced changes on proteins in various combinations of matrices and processing conditions, studying their impact semi-quantitatively on specific protein sequences might unveil approaches to improve protein quantification accuracy. Thus, 335 post-translational modifications (e.g. oxidation, deamidation, carboxymethylation, Amadori, acrolein adduction) were identified by bottom-up proteomic analysis of 37 bovine materials relevant in food and feed (meat, bone, blood, milk) with varying processing degrees (raw, spray-dried, pressure-sterilized). To mimic protein recovery in a targeted analysis, peak areas of marker and reference peptides were compared to those of their modified versions, which revealed peptide-specific recoveries and variances across all samples. Detailed analysis suggests that incorporating two modified versions additionally to the unmodified marker may significantly improve quantification accuracy in targeted MS-based food and feed control in processed matrices.
2025-06-05 | PXD047055 | Pride
Project description:Growth conditions with different light and nitrogen supply, to understand the transcriptional response caused by the environmental conditions.
2019-02-01 | E-MTAB-3651 | biostudies-arrayexpress
Project description:Bacteria such as Staphylococcus aureus are generally engulfed by the host with a membrane when internalized by non-professional phagocytic host cells. These vacuoles then mature to phagosomes which can fuse with lysosomes enabling killing and digestion of the pathogen. Former proteome approaches enriching S. aureus from lysed host cells after infection did not cover secreted virulence factors. However, secreted S. aureus proteins should be trapped within the phagosomes and, hence, these compartments were enriched from human bronchial epithelial S9 cells infected with S. aureus HG001 to also explore the virulence factor repertoire of S. aureus following internalization by host cells. Using shotgun mass spectrometry we monitored 92 phagosomal proteins over time unraveling a heterogeneous composition of phagosomal proteins in regard to maturation stages. Furthermore, we quantified 36 bacterial proteins within the phagosomes during the first 6.5 h post infection by applying targeted single reaction monitoring. Among them were secreted bacterial virulence factors like lipases, hemolysins, and secreted adhesins which are usually hard to detect from infected sample material by proteomics approaches due to low abundance. Thus, we provide insight into the fate and early adaptation of S. aureus HG001 after internalization by epithelial cells by simultaneous analysis of the phagosomal environment and virulence factors of S. aureus.
2018-06-29 | PXD007885 | Pride