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Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin <Emphasis Type="Italic">Strongylocentrotus nudus</Emphasis>
Authors:E V Shamshurina  M G Eliseikina  I Yu Petrova  A A Bulgakov
Institution:1.Institute of Marine Biology, Far East Branch,Russian Academy of Sciences,Vladivostok,Russia;2.Pacific Institute of Bioorganic Chemistry, Far East Branch,Russian Academy of Sciences,Vladivostok,Russia
Abstract:This study revealed a new lectin (MBL-SN) in the coelomic fluid of the sea urchin Strongylocentrotus nudus. Based on the peculiarities of molecular structure and carbohydrate specificity, MBL-SN can be assigned to the mannan-binding lectin family. Using polyclonal monospecific rabbit antibodies against MBL-SN, the presence of MBL-SN in the sea urchin was detected in two forms: a soluble form dissolved in the coelomic fluid and an extracellular matrix-bound form. The biosynthesis site of this lectin may be one of the subpopulations of morula cells-coelomic fluid cells that perform heterosynthesis. Our results demonstrate the similarity of the sea urchin lectin MBL-SN to the previously investigated MBLs of the holothurians Cucumaria japonica and Apostichopus japonicus, and suggest a similarity to MBLs of vertebrates, which also have soluble and bound forms.
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