1. A C-type lectin from the Tunicate, Styela plicata, that modulates cellular activity
- Author
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Monika Burandt, Aimee Hutchinson, Robert L. Raison, Sham V. Nair, and David A. Raftos
- Subjects
Interleukin 2 ,Hemocytes ,Physiology ,Health, Toxicology and Mutagenesis ,Molecular Sequence Data ,Toxicology ,Biochemistry ,Cell Line ,Mice ,Phagocytosis ,Cell surface receptor ,C-type lectin ,Lectins ,medicine ,Animals ,Lectins, C-Type ,Urochordata ,Amino Acid Sequence ,Receptor ,Peptide sequence ,Cells, Cultured ,Chromatography, High Pressure Liquid ,biology ,Interleukin ,Receptors, Interleukin-2 ,Blood Proteins ,Cell Biology ,General Medicine ,biology.organism_classification ,Tunicate ,Styela plicata ,Immunology ,Interleukin-2 ,Electrophoresis, Polyacrylamide Gel ,Mitogens ,Cell Division ,medicine.drug - Abstract
Previous studies have identified proteins from tunicates (invertebrate members of the Phylum Chordata) that have physicochemical and functional properties similar to those of the inflammatory cytokine, interleukin 1 (IL-1). Here we characterize one of those proteins from the tunicate, Styela plicata, that can stimulate tunicate and mammalian cell proliferation, activate phagocytosis, increase interleukin 2 (IL-2) secretion by mammalian peripheral blood mononuclear cells and enhance IL-2 receptor (IL-2R) expression by mammalian EL-4.IL-2 cells. Partial amino acid sequence data showed that the S. plicata protein resembles three C-type lectins (TC14, TC14-1 and TC14-2) from a closely related tunicate species, Polyandrocarpa misakiensis. Its similarity to carbohydrate recognition domains (CRDs) from P. misakiensis lectins suggests that the S. plicata protein modulates the activities of mammalian immunocompetent cells by interacting with carbohydrate moieties of glycosylated cell surface receptors.
- Published
- 2001
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