Abstract
A novel lectin from the large globiferous pedicellariae of the sea urchin, Toxopneustes pileolus, was isolated by a combination of gel chromatography and affinity chromatography techniques. The 32 kDa lectin appeared to have sequence homology to SUL-I, a D-galactose-specific lectin (Citation). This lectin is named SUL-IA. The N-terminal 7 amino acid sequence of SUL-IA was shown to be AVGRSCE. SUL-IA induced mitogenic stimulation on murine splenocytes and T-lymphocytes. SUL-IA also induced chemotaxis for guinea-pig neutrophils and macrophages. In addition, SUL-IA produced IFN-γ in a higher dose range, but not IL-4. These results suggest that SUL-IA may be a biologically functional lectin, which is one of the multiple lectins from the pedicellarial venom of T. pileolus.
Acknowledgements
We deeply thank Mr. H. Nagata and Mr. H. Nagata for collection of T. pileolus specimens over 20 years.
Declaration of interest
The authors declare that there are no conflicts of interest.