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      Proteome changes in the small intestinal mucosa of broilers ( Gallus gallus) induced by high concentrations of atmospheric ammonia

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          Abstract

          Background

          Ammonia is a well-known toxicant both existing in atmospheric and aquatic system. So far, most studies of ammonia toxicity focused on mammals or aquatic animals. With the development of poultry industry, ammonia as a main source of contaminant in the air is causing more and more problems on broiler production, especially lower growth rate. The molecular mechanisms that underlie the negative effects of ammonia on the growth and intestine of broilers are yet unclear. We investigated the growth, gut morphology, and mucosal proteome of Arbor Acres broilers ( Gallus gallus) exposed to high concentrations of atmospheric ammonia by performing a proteomics approach integrated with traditional methods.

          Results

          Exposure to ammonia interfered with the development of immune organ and gut villi. Meanwhile, it greatly reduced daily weight gain and feed intake, and enhanced feed conversion ratio. A total of 43 intestinal mucosal proteins were found to be differentially abundant. Up-regulated proteins are related to oxidative phosphorylation and apoptosis. Down-regulated proteins are related to cell structure and growth, transcriptional and translational regulation, immune response, oxidative stress and nutrient metabolism. These results indicated that exposure to ammonia triggered oxidative stress, and interfered with nutrient absorption and immune function in the small intestinal mucosa of broilers.

          Conclusions

          These findings have important implications for understanding the toxic mechanisms of ammonia on intestine of broilers, which provides new information that can be used for intervention using nutritional strategies in the future.

          Electronic supplementary material

          The online version of this article (doi:10.1186/s12953-015-0067-4) contains supplementary material, which is available to authorized users.

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          Most cited references66

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          Filamins as integrators of cell mechanics and signalling.

          Filamins are large actin-binding proteins that stabilize delicate three-dimensional actin webs and link them to cellular membranes. They integrate cellular architectural and signalling functions and are essential for fetal development and cell locomotion. Here, we describe the history, structure and function of this group of proteins.
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            A high-fat diet coordinately downregulates genes required for mitochondrial oxidative phosphorylation in skeletal muscle.

            Obesity and type 2 diabetes have been associated with a high-fat diet (HFD) and reduced mitochondrial mass and function. We hypothesized a HFD may affect expression of genes involved in mitochondrial function and biogenesis. To test this hypothesis, we fed 10 insulin-sensitive males an isoenergetic HFD for 3 days with muscle biopsies before and after intervention. Oligonucleotide microarray analysis revealed 297 genes were differentially regulated by the HFD (Bonferonni adjusted P < 0.001). Six genes involved in oxidative phosphorylation (OXPHOS) decreased. Four were members of mitochondrial complex I: NDUFB3, NDUFB5, NDUFS1, and NDUFV1; one was SDHB in complex II and a mitochondrial carrier protein SLC25A12. Peroxisome proliferator-activated receptor gamma coactivator-1 (PGC1) alpha and PGC1beta mRNA were decreased by -20%, P < 0.01, and -25%, P < 0.01, respectively. In a separate experiment, we fed C57Bl/6J mice a HFD for 3 weeks and found that the same OXPHOS and PGC1 mRNAs were downregulated by approximately 90%, cytochrome C and PGC1alpha protein by approximately 40%. Combined, these results suggest a mechanism whereby HFD downregulates genes necessary for OXPHOS and mitochondrial biogenesis. These changes mimic those observed in diabetes and insulin resistance and, if sustained, may result in mitochondrial dysfunction in the prediabetic/insulin-resistant state.
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              Activities of Ligatin and MCT-1/DENR in eukaryotic translation initiation and ribosomal recycling.

              Eukaryotic translation initiation begins with ribosomal recruitment of aminoacylated initiator tRNA (Met-tRNA(Met)(i)) by eukaryotic initiation factor eIF2. In cooperation with eIF3, eIF1, and eIF1A, Met-tRNA(Met)(i)/eIF2/GTP binds to 40S subunits yielding 43S preinitiation complexes that attach to the 5'-terminal region of mRNAs and then scan to the initiation codon to form 48S initiation complexes with established codon-anticodon base-pairing. Stress-activated phosphorylation of eIF2alpha reduces the level of active eIF2, globally inhibiting translation. However, translation of several viral mRNAs, including Sindbis virus (SV) 26S mRNA and mRNAs containing hepatitis C virus (HCV)-like IRESs, is wholly or partially resistant to inhibition by eIF2 phosphorylation, despite requiring Met-tRNA(Met)(i). Here we report the identification of related proteins that individually (Ligatin) or together (the oncogene MCT-1 and DENR, which are homologous to N-terminal and C-terminal regions of Ligatin, respectively) promote efficient eIF2-independent recruitment of Met-tRNA(Met)(i) to 40S/mRNA complexes, if attachment of 40S subunits to the mRNA places the initiation codon directly in the P site, as on HCV-like IRESs and, as we show here, SV 26S mRNA. In addition to their role in initiation, Ligatin and MCT-1/DENR can promote release of deacylated tRNA and mRNA from recycled 40S subunits after ABCE1-mediated dissociation of post-termination ribosomes.
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                Author and article information

                Contributors
                jzz2006@126.com
                lc15350@163.com
                xiangfangtang@163.com
                luqingping@sina.com
                sa6289@126.com
                zhanghf6565@vip.sina.com
                Journal
                Proteome Sci
                Proteome Sci
                Proteome Science
                BioMed Central (London )
                1477-5956
                21 February 2015
                21 February 2015
                2015
                : 13
                : 9
                Affiliations
                State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing, 100193 People’s Republic of China
                Article
                67
                10.1186/s12953-015-0067-4
                4347970
                25741220
                bd346603-4ed8-40b8-812b-22e68ccd4f9a
                © Zhang et al.; licensee BioMed Central. 2015

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                : 27 October 2014
                : 11 February 2015
                Categories
                Research Article
                Custom metadata
                © The Author(s) 2015

                Molecular biology
                proteome,ammonia,small intestinal mucosa,broilers
                Molecular biology
                proteome, ammonia, small intestinal mucosa, broilers

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