Publications by authors named "Martin-Burriel I"

Current diagnostic methods for prion diseases only work in late stages of the disease when neurodegeneration is irreversible. Therefore, biomarkers that can detect the disease before the onset of clinical symptoms are necessary. High-throughput discovery proteomics is of great interest in the search for such molecules.

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In neurodegenerative diseases, including prion diseases, cellular models arise as useful tools to study the pathogenic mechanisms occurring in these diseases and to assess the efficacy of potential therapeutic compounds. In the present study, a RNA-sequencing analysis of bone marrow-derived ovine mesenchymal stem cells (oBM-MSCs) exposed to scrapie brain homogenate was performed to try to unravel genes and pathways potentially involved in prion diseases and MSC response mechanisms to prions. The oBM-MSCs were cultured in three different conditions (inoculated with brain homogenate of scrapie-infected sheep, with brain homogenate of healthy sheep and in standard growth conditions without inoculum) that were analysed at two exposure times: 2 and 4 days post-inoculation (dpi).

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() is a pathogen frequently isolated in cases of urinary tract infections (UTIs) in both humans and dogs and evidence exists that dogs are reservoirs for human infections. In addition, is associated to increasing antimicrobial resistance rates. This study focuses on the analysis of antimicrobial resistance and the presence of selected virulence genes in isolates from a Spanish dog population suffering from UTI.

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Epilepsy is one of the most prevalent complex neurological diseases in both the canine and human species, with the idiopathic form as its most common diagnosis. MicroRNAs (miRNAs) are small, noncoding RNA molecules that play a role in gene regulation processes and appear to be a promising biological target for convulsion control. These molecules have been reported as constituents of the internal content of exosomes, which are small extracellular vesicles released by cells.

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Prion diseases are fatal neurodegenerative disorders in which the main pathogenic event is the conversion of the cellular prion protein (PrP) into an abnormal and misfolded isoform known as PrP. Most prion diseases and their susceptibility and pathogenesis are mainly modulated by the PRNP gene that codes for PrP. Mutations and polymorphisms in the PRNP gene can alter PrP amino acid sequence, leading to a change in transmission efficiency depending on the place where it occurs.

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This review aims to provide a comprehensive overview of the significant molecular typing techniques currently employed in research and medical communities. The main objectives of this review are to describe the key molecular typing methods utilized in studies and to highlight the epidemiological characteristics of the most prevalent strains on a global scale. Geographically distinct regions exhibit distinct strain types of , with notable concordance observed among various typing methodologies.

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In neurodegenerative diseases, including prion diseases, cellular in vitro models appear as fundamental tools for the study of pathogenic mechanisms and potential therapeutic compounds. Two-dimensional (2D) monolayer cell culture systems are the most used cell-based assays, but these platforms are not able to reproduce the microenvironment of in vivo cells. This limitation can be surpassed using three-dimensional (3D) culture systems such as spheroids that more effectively mimic in vivo cell interactions.

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Scrapie is a neurodegenerative disorder belonging to the group of transmissible spongiform encephalopathies or prion diseases, which are caused by an infectious isoform of the innocuous cellular prion protein (PrP) known as PrP. DNA methylation, one of the most studied epigenetic mechanisms, is essential for the proper functioning of the central nervous system. Recent findings point to possible involvement of DNA methylation in the pathogenesis of prion diseases, but there is still a lack of knowledge about the behavior of this epigenetic mechanism in such neurodegenerative disorders.

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Prion diseases are transmissible spongiform encephalopathies (TSEs) caused by a conformational conversion of the native cellular prion protein (PrP) to an abnormal, infectious isoform called PrP. Amyotrophic lateral sclerosis, Alzheimer's, Parkinson's, and Huntington's diseases are also known as prion-like diseases because they share common features with prion diseases, including protein misfolding and aggregation, as well as the spread of these misfolded proteins into different brain regions. Increasing evidence proposes the involvement of epigenetic mechanisms, namely DNA methylation, post-translational modifications of histones, and microRNA-mediated post-transcriptional gene regulation in the pathogenesis of prion-like diseases.

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Article Synopsis
  • Prion diseases like scrapie are diagnosed late, when there's already significant brain damage, highlighting the need for early detection methods for asymptomatic cases.
  • In a study, proteins neurogranin (Ng) and neurofilament light chain (NfL) were evaluated as potential biomarkers in sheep with preclinical and clinical scrapie, showing decreased levels in affected animals compared to healthy ones.
  • The research found that while Ng and NfL levels dropped as disease advanced, CSF NfL levels increased, indicating their potential role in assessing neurodegeneration early in infectious prion diseases.
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Article Synopsis
  • * A study using whole-genome bisulfite sequencing (WGBS) found 8,907 differentially methylated regions (DMRs) in sheep infected with scrapie compared to healthy controls, indicating changes in DNA methylation patterns.
  • * Analysis reveals that these methylation changes affect genes related to cell functions and are linked to differential gene expression, suggesting that DNA methylation may play a regulatory role in prion-related brain disorders.
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The non-toxic C-terminal fragment of the tetanus toxin (TTC) has been described as a neuroprotective molecule since it binds to Trk receptors and activates Trk-dependent signaling, activating neuronal survival pathways and inhibiting apoptosis. Previous in vivo studies have demonstrated the ability of this molecule to increase mice survival, inhibit apoptosis and regulate autophagy in murine models of neurodegenerative diseases such as amyotrophic lateral sclerosis and spinal muscular atrophy. Prion diseases are fatal neurodegenerative disorders in which the main pathogenic event is the conversion of the cellular prion protein (PrP) into an abnormal and misfolded isoform known as PrP.

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Diagnosis of transmissible spongiform encephalopathies (TSEs), or prion diseases, is based on the detection of proteinase K (PK)-resistant PrP in post-mortem tissues as indication of infection and disease. Since PrP detection is not considered a reliable method for in vivo diagnosis in most TSEs, it is of crucial importance to identify an alternative source of biomarkers to provide useful alternatives for current diagnostic methodology. Ovine scrapie is the prototype of TSEs and has been known for a long time.

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American Criollo pigs are thought to descend mainly from those imported from the Iberian Peninsula starting in the late 15th century. Criollo pigs subsequently expanded throughout the Americas, adapting to very diverse environments, and possibly receiving influences from other origins. With the intensification of agriculture in the mid-20th century, cosmopolitan breeds largely replaced Criollo pigs, and the few remaining are mostly maintained by rural communities in marginal areas where they still play an important socio-economic and cultural role.

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Scrapie is a prion disease affecting sheep and goats and it is considered a prototype of transmissible spongiform encephalopathies (TSEs). Mesenchymal stem cells (MSCs) have been proposed as candidates for developing in vitro models of prion diseases. Murine MSCs are able to propagate prions after previous mouse-adaptation of prion strains and, although ovine MSCs express the cellular prion protein (PrP), their susceptibility to prion infection has never been investigated.

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Article Synopsis
  • Neurotrophins are essential growth factors that function in the nervous system of vertebrates and interact with two types of receptors, including p75, which can influence cell survival and death.
  • The study found that in a comparison of prion-infected mice and sheep, the levels of p75 were notably higher in infected mice, indicating a potential link between p75 and neurodegenerative processes related to prion diseases.
  • In sheep, increased levels of p75 were observed in early preclinical stages of prion disease, suggesting its role in the development of scrapie, and implicating astrocytes in this neurodegenerative process, particularly in the mouse model.
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  • In 2008, guidelines were established for researching autophagy, which has since gained significant interest and new technologies, necessitating regular updates to monitoring methods across various organisms.
  • The new guidelines emphasize selecting appropriate techniques to evaluate autophagy while noting that no single method suits all situations; thus, a combination of methods is encouraged.
  • The document highlights that key proteins involved in autophagy also impact other cellular processes, suggesting genetic studies should focus on multiple autophagy-related genes to fully understand these pathways.
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Salmonellosis is a common subclinical infection in pigs and therefore apparently healthy animals may represent a reservoir of antibiotic-resistant Salmonella for humans. This study estimates and characterizes resistance to two classes of antimicrobials considered of the highest priority within the critically important antimicrobials for humans, i.e.

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  • Autophagy is an essential cellular process that helps break down and recycle proteins and organelles, playing a crucial role in normal cell function and development, while defects in this process can lead to diseases such as prion disorders.
  • Prion diseases, characterized by misfolded proteins accumulating in the nervous system, exhibit altered autophagy which complicates our understanding of whether this process is harmful or protective during neurodegeneration.
  • Recent research has explored how autophagic mechanisms interact with prion proteins, suggesting that enhancing autophagy could aid in clearing harmful aggregates in neuronal cells and may provide new avenues for treatment.
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MicroRNAs (miRNAs) may contribute to the development and pathology of many neurodegenerative diseases, including prion diseases. They are also promising biomarker candidates due to their stability in body fluids. We investigated miRNA alterations in a Tg501 mouse model of prion diseases that expresses a transgene encoding the goat prion protein ().

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The aim of this study was to estimate the prevalence of antimicrobial resistance (AMR) in Escherichia coli from a dog population in Spain and assess specific virulence factors. Susceptibility to 22 antimicrobials was tested along with the production of extended-spectrum β-lactamases (ESBLs) and AmpC in faecal isolates from 100 dogs. Virulence-related genes associated with attaching and effacing E.

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Prion diseases affect both animals and humans. Research in the natural animal model of the disease could help in the understanding of neuropathological mechanisms and in the development of biomarkers for human pathologies. For this purpose, we studied the expression of 10 genes involved in prion propagation in vitro in the central nervous system of scrapie-infected sheep.

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Background: Epigenetic changes in obstructive sleep apnea (OSA) have been proposed as a mechanism for end-organ vulnerability. In children with OSA, Forkhead Box P3 (FOXP3) DNA methylation were associated with inflammatory biomarkers; however, the methylation pattern and its effect in the expression of this gene have not been tested in adults with OSA.

Methods: Plasma samples from subjects without comorbid conditions other than OSA were analyzed (the Epigenetics Status and Subclinical Atherosclerosis in Obstructive Sleep Apnea (EPIOSA) Study: NCT02131610).

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