Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin Strongylocentrotus nudus
Identifieur interne : 002728 ( Main/Exploration ); précédent : 002727; suivant : 002729Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin Strongylocentrotus nudus
Auteurs : E. V. Shamshurina [Russie] ; M. G. Eliseikina [Russie] ; I. Yu. Petrova [Russie] ; A. A. Bulgakov [Russie]Source :
- Russian Journal of Marine Biology [ 1063-0740 ] ; 2010-07-01.
English descriptors
Abstract
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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DOI: 10.1134/S1063074010040073
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<front><div type="abstract" xml:lang="en">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.</div>
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