Summary
A β-1,3-glucan-binding protein (βGBP) was purified from crayfish plasma, and incubated with laminarin (L), a β-1,3-glucan. The βGBP reacted with laminarin (βGBP-L) induced strong spreading and partial degranulation of isolated and separated crayfish granular haemocytes. However, neither the βGBP nor laminarin alone induced any changes in the crayfish granular cells. When monolayers of granular haemocytes were incubated with 20 μg of βGBP-L, more than 82% of the haemocytes were affected. The activity of βGBP-L on granular cells was dose-dependent and a plateau was reached at 10 μg of βGBP-L. The degranulation of crayfish haemocytes induced by βGBP-L seemed to occur by a regulated exocytosis, since it was strongly inhibited by specific blockers of this process such as SITS or calmidazolium. Monospecific anti-βGBP antibodies also totally blocked the effect of βGBP-L on crayfish granular cells. Indirect immunofluoresence staining demonstrated that the βGBP-L could bind to the surface of granular cells, whereas βGBP did not bind or bound very weakly to the haemocyte surface.
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Barracco, M.A., Duvic, B. & Söderhäll, K. The β-1,3-glucan-binding protein from the crayfish Pacifastacus leniusculus, when reacted with a β-1,3-glucan, induces spreading and degranulation of crayfish granular cells. Cell Tissue Res 266, 491–497 (1991). https://doi.org/10.1007/BF00318590
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DOI: https://doi.org/10.1007/BF00318590