Syndecan-dependent binding ofDrosophilahemocytes to laminin α3/5 chain LG4-5 modules: potential role in sessile hemocyte islets formation
| Autor: | Akira Goto, Hitoshi Mori, Ryo Narita, Shigeyuki Ichihara, Hiromi Imai, Hironobu Yamashita, Yasuo Kitagawa |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Hemocytes Syndecans LG module Molecular Sequence Data Biophysics Heparan sulfate Trimer Xenopus Proteins GFP Biochemistry Green fluorescent protein Syndecan 1 chemistry.chemical_compound RNA interference Structural Biology Laminin Cell Adhesion Genetics Animals Amino Acid Sequence Bovine serum albumin Molecular Biology Cells Cultured Binding Sites Membrane Glycoproteins biology Heparin Cell Biology Dally Molecular biology Protein Structure Tertiary chemistry Larva Hemolectin biology.protein Syndecan-3 Drosophila Proteoglycans Heparitin Sulfate Syndecan-1 |
| Zdroj: | FEBS Letters. 576:127-132 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2004.08.073 |
| Popis: | Heparin-column chromatography and elastase-digestion of medium from hemocyte Kc167 gave Drosophila laminin alpha3/5betagamma trimer, alpha3/5LG2-3 and alpha3/5LG4-5 modules with eluting NaCl concentrations of 450, 280 and 450 mM, respectively. Kc167 cells bound dish surface with alpha3/5betagamma trimer or alpha3/5LG4-5, but not with alpha3/5LG2-3 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 dally or dally-like did not. Green fluorescent protein-expressing hemocytes also bound surface with alpha3/5betagamma trimer or alpha3/5LG4-5 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. |
| Databáze: | OpenAIRE |
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