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    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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