Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin Strongylocentrotus nudus

Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Marine Biology Springer Journals

Detection of two immunochemically identical forms of mannan-binding lectin in the sea urchin Strongylocentrotus nudus

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Publisher
SP MAIK Nauka/Interperiodica
Copyright
Copyright © 2010 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Freshwater & Marine Ecology
ISSN
1063-0740
eISSN
1608-3377
D.O.I.
10.1134/S1063074010040073
Publisher site
See Article on Publisher Site

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.

Journal

Russian Journal of Marine BiologySpringer Journals

Published: Aug 29, 2010

References

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