Abstract
Heparin-column chromatography and elastase-digestion of medium from hemocyte Kc167 gave Drosophila laminin α3/5βγ trimer, α3/5LG2-3 and α3/5LG4-5 modules with eluting NaCl concentrations of 450, 280 and 450 mM, respectively. Kc167 cells bound dish surface with α3/5βγ trimer or α3/5LG4-5, but not with α3/5LG2-3 modules. Cell binding was counteracted by treating with heparin or heparan sulfate. RNA interference of syndecan in Kc167 cells impaired the binding, but that of d ally or dally-like did not. Green fluorescent protein-expressing hemocytes also bound surface with α3/5βγ trimer or α3/5LG4-5 module. Thus, syndecan-dependent binding of hemocytes to laminin may have a potential role in sessile hemocytes islets formation in T2-A8 segments of Drosophila.
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