102
views
0
recommends
+1 Recommend
0 collections
    12
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Investigation of SNPs in the porcine desmoglein 1 gene

      research-article
      1 , 2 , , 1 , 2
      BMC Veterinary Research
      BioMed Central

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Background

          Desmoglein 1 (DSG1) is the target protein in the skin disease exudative epidermitis in pigs caused by virulent strains of Staphylococcus hyicus. The exfoliative toxins produced by S. hyicus digest the porcine desmoglein 1 (PIG)DSG1 by a very specific reaction. This study investigated the location of single nucleotide polymorphisms (SNPs) in the porcine desmoglein 1 gene (PIG) DSG1 in correlation to the cleavage site as well as if the genotype of the SNPs is correlated to susceptibility or resistance to the disease.

          Results

          DNA from 32 affected and 32 unaffected piglets with exudative epidermitis were diagnosed clinically as affected or unaffected. Two regions of the desmoglein 1 gene were sequenced and genotypes of the SNPs were established. Seven SNPs (823T>C, 828A>G, 829A>G, 830A>T, 831A>T, 838A>C and 1139C>T) were found in the analysed sequences and the allele frequencies were determined for the SNPs resulting in amino acid change. Four of the seven polymorphisms were situated in the motif known to be important for toxin cleavage. The distribution of the genotypes between affected and unaffected animals was analysed.

          Conclusion

          The study indicated a possible correlation between the genotypes of two out of seven SNPs found in the porcine desmoglein 1 gene and the susceptibility to exudative epidermitis.

          Related collections

          Most cited references12

          • Record: found
          • Abstract: found
          • Article: not found

          Cleavage of parallel-stranded DNA duplex by peplomycin metal complexes.

          Peplomycin-mediated degradation of parallel-stranded (ps) duplex was investigated. It was found that Co- and Fe-peplomycins degraded ps DNA duplex by 4'-hydrogen abstraction at 5'-GPy (pyrimidine) site in a similar manner to that of antiparallel B-DNA. While the orientation of two strands of ps and B-form DNA duplexes are reversed, peplomycin metal complex can bind to ps DNA duplex to cause oxidative DNA damage. These results indicate that peplomycin metal complex mainly interacts with one strand which is damaged.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            The cadherin superfamily: diversity in form and function.

            Over recent years cadherins have emerged as a growing superfamily of molecules, and a complex picture of their structure and their biological functions is becoming apparent. Variation in their extracellular region leads to the large potential for recognition properties of this superfamily. This is demonstrated strikingly by the recently discovered FYN-binding CNR-protocadherins; these exhibit alternative expression of the extracellular portion, which could lead to distinct cell recognition in different neuronal populations, whereas their cytoplasmic part, and therefore intracellular interactions, is constant. Diversity in the cytoplasmic moiety of the cadherins imparts specificity to their interactions with cytoplasmic components; for example, classical cadherins interact with catenins and the actin filament network, desmosomal cadherins interact with catenins and the intermediate filament system and CNR-cadherins interact with the SRC-family kinase FYN. Recent evidence suggests that CNR-cadherins, 7TM-cadherins and T-cadherin, which is tethered to the membrane by a GPI anchor, all localise to lipid rafts, specialised cell membrane domains rich in signalling molecules. Originally thought of as cell adhesion molecules, cadherin superfamily molecules are now known to be involved in many biological processes, such as cell recognition, cell signalling, cell communication, morphogenesis, angiogenesis and possibly even neurotransmission.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              The cadherin-catenin complex as a focal point of cell adhesion and signalling: new insights from three-dimensional structures.

              Cadherins are a large family of single-pass transmembrane proteins principally involved in Ca2+-dependent homotypic cell adhesion. The cadherin molecules comprise three domains, the intracellular domain, the transmembrane domain and the extracellular domain, and form large complexes with a vast array of binding partners (including cadherin molecules of the same type in homophilic interactions and cellular protein catenins), orchestrating biologically essential extracellular and intracellular signalling processes. While current, contrasting models for classic cadherin homophilic interaction involve varying numbers of specific repeats found in the extracellular domain, the structure of the domain itself clearly remains the main determinant of cell stability and binding specificity. Through intracellular interactions, cadherin enhances its adhesive properties binding the cytoskeleton via cytoplasmic associated factors alpha- catenin, beta-catenin and p120ctn. Recent structural studies on classic cadherins and these catenin molecules have provided new insight into the essential mechanisms underlying cadherin-mediated cell interaction and catenin-mediated cellular signalling. Remarkable structural diversity has been observed in beta-catenin recognition of other cellular factors including APC, Tcf and ICAT, proteins that contribute to or compete with cadherin/catenin functioning. Copyright 2004 Wiley Periodicals, Inc.
                Bookmark

                Author and article information

                Journal
                BMC Vet Res
                BMC Veterinary Research
                BioMed Central (London )
                1746-6148
                2007
                31 March 2007
                : 3
                : 4
                Affiliations
                [1 ]The National Veterinary Institute, Technical University of Denmark, Bülowsvej 27, 1790 Copenhagen V, Denmark
                [2 ]Faculty of Lifesciences, University of Copenhagen, Bülowsvej 17, 1870 Frederiksberg C, Denmark
                Article
                1746-6148-3-4
                10.1186/1746-6148-3-4
                1858681
                17397555
                b7817f01-5651-4f27-86de-2b2f6af3354f
                Copyright © 2007 Daugaard et al; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 2 October 2006
                : 31 March 2007
                Categories
                Research Article

                Veterinary medicine
                Veterinary medicine

                Comments

                Comment on this article