49 research outputs found

    Manejo de animais e pastagens em sistemas de integração silvipastoril

    Get PDF
    bitstream/item/78887/1/documento-335.pd

    Biomarkers for Mercury Exposure in Tropical Estuarine Fish

    Get PDF
    Several studies have evaluated human risks due mercury (Hg) exposure through fish consumption. However, relatively few studies have explored effects of environmental Hg concentrations in biota, especially tropical fish species. The aim of this work was to assess in situ hematological, biochemical and genotoxic effects in tropical fish due to environmental exposure to mercury in estuarine ecosystems. A total of 282 fishes were collected from September 2003 to October 2005 in two estuarine areas: Ribeira Bay (reference area - 22° 55’ to 23° 02’ S and 44° 18’ to 44° 26’ W) and Guanabara Bay (highly impacted area by human activities - 22° 40’ to 23° 00’ S and 43° 00’ to 43° 20’ E). Total mercury levels in fish from Guanabara were twice higher than in Ribeira bay for the catfish species Genidens genidens (Ariidae), with significant differences among areas after standardization using length intervals (exposure time indicator). The species Haemulon steindachneri (Haemulidae) showed the highest mercury concentration, reflecting its position in trophic chain. Among effect biomarkers, only haematocrit, global leucometry and micronucleus assays seemed to reflect the differences on mercury exposure among areas, what may support their use for evaluations of fish exposure to mercury compounds. However, it’s necessary both laboratory experiments to establish cause-effect relationship and a continuous in situ study to obtain more information, involving more trophic levels, searching for sensible species to mercury exposure

    Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?

    Get PDF
    Stress granules (SGs) are membraneless cell compartments formed in response to different stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other proteins coalesce together. SGs assembly is crucial for cell survival, since SGs are implicated in the regulation of translation, mRNA storage and stabilization and cell signalling, during stress. One defining feature of SGs is their dynamism, as they are quickly assembled upon stress and then rapidly dispersed after the stress source is no longer present. Recently, SGs dynamics, their components and their functions have begun to be studied in the context of human diseases. Interestingly, the regulated protein self-assembly that mediates SG formation contrasts with the pathological protein aggregation that is a feature of several neurodegenerative diseases. In particular, aberrant protein coalescence is a key feature of polyglutamine (PolyQ) diseases, a group of nine disorders that are caused by an abnormal expansion of PolyQ tract-bearing proteins, which increases the propensity of those proteins to aggregate. Available data concerning the abnormal properties of the mutant PolyQ disease-causing proteins and their involvement in stress response dysregulation strongly suggests an important role for SGs in the pathogenesis of PolyQ disorders. This review aims at discussing the evidence supporting the existence of a link between SGs functionality and PolyQ disorders, by focusing on the biology of SGs and on the way it can be altered in a PolyQ disease context.ALG-01-0145-FEDER-29480, SFRH/BD/133192/2017, SFRH/BD/133192/2017, SFRH/BD/148533/2019info:eu-repo/semantics/publishedVersio
    corecore