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  • DKFZ Publication Database  (2)
  • 1
    Keywords: CELLS ; EXPRESSION ; Germany ; CLONING ; GENE ; HYBRIDIZATION ; PROTEIN ; DOMAIN ; IN-SITU ; EVOLUTION ; innate immunity ; LECTIN ; DOMAINS ; in situ hybridization ; Hydractinia ; neuron ; CNIDARIAN ; invertebrate immunity ; TACHYPLEUS-TRIDENTATUS
    Abstract: Tachylectin-related proteins are a recently characterized group of pattern recognition molecules, functioning in the innate immunity of various animals, from the ancient sponges to vertbrates. Tachylectins are characterized by six internal tandem repeats forming beta-propeller domains. We have identified and characterized a tachylectin-related gene in the colonial marine hydroid, Hydractinia echinata. The predicted gene product, termed CTRN, contained an N-terminal signal peptide and had a well-conserved tachylectin-like structure. RT-PCR analyses revealed only post-metamorphic expression while no mRNA was detected during embryonic development or in planula larvae. Exposure of colonies to LPS under conditions known to activate an immune response in Hydractinia did not result in upregulation of the gene. In situ hybridization analysis of metamorphosed animals detected CTRN transcripts only in a small subpopulation of neurons and their precursor cells, localized in a ring-like structure around the mouth of polyps. The same ring-like structure of CTRN expressing neurons was also observed in young polyp buds, predicting the position of the future mouth. This type of expression pattern can hardly be attributed to an immunerelevant gene. Thus, despite high structural similarity to tachylectins, this cnidarian member of this group seems to be an exception to all other tachylectins identified so far as it seems to have no function in cnidarian innate immunity. (c) 2005 Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 15975655
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  • 2
    Keywords: EXPRESSION ; Germany ; CLASSIFICATION ; CDNA ; ENZYMES ; HYBRIDIZATION ; TISSUE ; FAMILY ; primary ; TISSUES ; STAGE ; IN-SITU ; RT-PCR ; IMMUNITY ; HOST-DEFENSE ; in situ hybridization ; DEFENSE ; pathogen ; PATHOGENS ; ECHINATA ; Hydractinia ; HYDROID HYDRACTINIA ; chitin ; allorecognition ; GLYCOSYL HYDROLASES ; periderm
    Abstract: Chitinases are enzymes that degrade chitin, the second most abundant polymer in nature. They are ubiquitous among living organisms where they play a role in development, food-digestion and innate immunity. We have cloned and characterized the first cnidarian chitinase cDNA from the hydroid Hydractinia. The Hydractinia chitinase exhibits a typical secreted family 18 hydrolases primary structure. In situ hybridization and RT-PCR experiments showed that it is exclusively expressed in ectodermal tissues of the animal, only following metamorphosis while undetectable in embryonic and larval stages. Most prominent expression was observed in the stolonal compartment of colonies, structures that are covered by a chitinous periderm. Chitinase mRNA was detected in new branching points along stolons and in hyperplastic stolons indicating a role of the enzyme in pattern formation and allorecognition. It was also expressed in polyps where it was mostly restricted to their basal portion. This expression pattern suggests that HyChitI also fulfills a role in host defense, probably against fungal and nematode pathogens. Endodermal expression of HyChitI has never been observed, suggesting that the enzyme does not participate in food-digestion. (C) 2004 Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 15236928
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