Transferrin and ferritin response to bacterial infection: The role of the liver and brain in fish
IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Portugal.Developmental and comparative immunology (Impact Factor: 2.82). 08/2009; 33(7):848-57. DOI: 10.1016/j.dci.2009.02.001
Iron is essential for growth and survival, but it is also toxic when in excess. Thus, there is a tight regulation of iron that is accomplished by the interaction of several genes including the iron transporter transferrin and iron storage protein ferritin. These genes are also known to be involved in response to infection. The aim of this study was to understand the role of transferrin and ferritin in infection and iron metabolism in fish. Thus, sea bass transferrin and ferritin H cDNAs were isolated from liver, cloned and characterized. Transferrin constitutive expression was found to be highest in the liver, but also with significant expression in the brain, particularly in the highly vascularized region connecting the inferior lobe of the hypothalamus and the saccus vasculosus. Ferritin, on the other hand, was expressed in all tested organs, but also significantly higher in the liver. Fish were subjected to either experimental bacterial infection or iron modulation and transferrin and ferritin mRNA expression levels were analyzed, along with several iron regulatory parameters. Transferrin expression was found to decrease in the liver and increase in the brain in response to infection and to increase in the liver in iron deficiency. Ferritin expression was found to inversely reflect transferrin in the liver, increasing in infection and iron overload and decreasing in iron deficiency, whereas in the brain, ferritin expression was also increased in infection. These findings demonstrate the evolutionary conservation of transferrin and ferritin dual functions in vertebrates, being involved in both the immune response and iron metabolism.
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- "The lack of difference in expression of casp3 between both groups indicates that there are no differences in apoptosis (Porter & J€ anicke 1999). Synthesis of ferritin is induced when much iron is available, especially during oxidative stress (Orino, Lehman, Tsuji, Ayaki, Torti & Torti 2001) and inflammatory conditions (Torti, Kwak, Miller, Miller, Ringold & Myambo 1988; Rogers, Bridges, Durmowicz, Glass, Auron & Munro 1990; Chasteen 1998; Lieu, Heiskala , Peterson & Yang 2001; Torti & Torti 2002), whereas during severe iron deprivation its synthesis is repressed (Neves et al. 2009). In our study, the ferritin expression was not different between the groups which does not support a difference in oxidative stress, high iron availability or iron deprivation between fish fed pellets or with ragworms . "
ABSTRACT: Common sole fed with commercial pellets develop anaemia and are restricted in their growth performance. The anaemia can be the result of a difference in feed intake, a nutritional deficiency, an inflammatory response to infection or combinations of these aspects. In this study, it was investigated whether feeding ragworm would alleviate the anaemia and stimulate growth. Sole were fed one of three diets: a commercial feed, a commercial feed treated with ragworm extract or chopped ragworm. By comparing groups, three hypotheses were tested: (1) feeding ragworm alleviates the anaemia and positively affectS the sole's metabolic performance reflected in feed intake, feed efficiency and growth; (2) anaemia is alleviated by a higher feed intake when feeding ragworm and (3) anaemia is caused by an inflammatory response to infection. The sole fed with a commercial diet suffered from anaemia. Feeding sole with ragworm alleviated the anaemia as the average haematocrit level nearly doubled in these fish as compared to fish fed pellets. Investigation of the expression of genes in the liver indicated that the anaemia in sole fed pellets is a nutritional anaemia and not an anaemia due to an inflammatory response. Sole fed ragworm showed improved growth which may be a consequence of the higher haematocrit levels in these fish increasing their oxygen carrying capacity. Addition of ragworm extract to the pellets levelled the feed intake between pellets and ragworm, but did not improve the anaemic state of sole and had only a limited effect on growth.Aquaculture Research 10/2015; DOI:10.1111/are.12919 · 1.38 Impact Factor
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- "In addition, it is bacteriostatic by limiting the availability of iron to bacteria (Fig. 3). TF, which has been characterized in liver and brainof D. labrax , was identified in skin mucus (spot 98 and 99) in the present paper with the highest score (see Table 2). TF was previously identified in skin mucus of gilthead seabream  and Atlantic cod juveniles . "
ABSTRACT: Skin mucus is the first barrier of fish defence. Proteins from skin mucus of European sea bass (Dicentrarchus labrax) were identified by 2DE followed by LC-MS/MS. From all the identified proteins in the proteome map, we focus on the proteins associated with several immune pathways in fish. Furthermore, the qPCR transcript levels in skin are shown. Proteins found include apolipoprotein A1, calmodulin, complement C3, fucose-binding lectin, lysozyme and several caspases. To our knowledge, this is the first skin mucus proteome study and further transcriptional profiling of the identified proteins done on this bony fish species. This not only contributes knowledge on the routes involved in mucosal innate immunity, but also establishes a non-invasive technique based on locating immune markers with a potential use for prevention and/or diagnosis of fish diseases.This article is protected by copyright. All rights reservedProteomics 09/2015; DOI:10.1002/pmic.201500120 · 3.81 Impact Factor
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- "On the other hand, M2 showed contrasting expression in both tissues – a slight decrease in the liver but a significant increase in kidney. This observation was particularly interesting as to our knowledge; previous studies in vertebrate ferritin have consistently reported increased ferritin expression during an APR , . The different expression patterns displayed between the ferritin chains (H- and M-chains) as well as the individual isoforms (M1 and M2) appear to suggest the possibility of more distinctive and complex roles for ferritin during an immune response than previously assumed. "
ABSTRACT: Ferritin is a highly-conserved iron-storage protein that has also been identified as an acute phase protein within the innate immune system. The iron-storage function is mediated through complementary roles played by heavy (H)-chain subunit as well as the light (L) in mammals or middle (M)-chain in teleosts, respectively. In this study, we report the identification of five ferritin subunits (H1, H2, M1, M2, M3) in the Atlantic salmon that were supported by the presence of iron-regulatory regions, gene structure, conserved domains and phylogenetic analysis. Tissue distribution analysis across eight different tissues showed that each of these isoforms is differentially expressed. We also examined the expression of the ferritin isoforms in the liver and kidney of juvenile Atlantic salmon that was challenged with Aeromonas salmonicida as well as in muscle cell culture stimulated with interleukin-1β. We found that each isoform displayed unique expression profiles, and in certain conditions the expressions between the isoforms were completely diametrical to each other. Our study is the first report of multiple ferritin isoforms from both the H- and M-chains in a vertebrate species, as well as ferritin isoforms that showed decreased expression in response to infection. Taken together, the results of our study suggest the possibility of functional differences between the H- and M-chain isoforms in terms of tissue localisation, transcriptional response to bacterial exposure and stimulation by specific immune factors.PLoS ONE 07/2014; 9(7):e103729. DOI:10.1371/journal.pone.0103729 · 3.23 Impact Factor
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