Laboratory of Immunopharmacology of Microbial Products Tokyo College of Pharmacy 1432-1 Horinouchi Hachioji-shi Tokyo 192-03 Japan.
Mediators Inflamm. 1997;6(4):251-6. doi: 10.1080/09629359791569.
We studied the activities of several kinds of beta-glucans, including sonifilan, grifolan, Sclerotinia sclerotiorum glucan, laminarin and zymosan, on macrophages. Preculture of macrophages with inactive beta-glucans rendered the cells unresponsive to subsequent stimulation with grifolan, suggesting a specific pathway in the beta-glucan structure. The importance of protein C and phosphorylation of mitogen-activated protein kinase was demonstrated in the activation with grifolan or zymosan. Immunoprecipitation of complement receptor (CR3), coprecipitated other proteins carrying phosphotyrosine residues in stimulation with grifolan. These data suggest that protein kinase C and tyrosine kinases are essential for signal transduction, and that CR3 might participate in the activation through interaction with other intracellular proteins.
我们研究了几种β-葡聚糖的活性,包括 sonifilan、grifolan、核盘菌葡聚糖、昆布多糖和zymosan,对巨噬细胞的作用。用非活性β-葡聚糖预先培养巨噬细胞,使细胞对随后的 grifolan 刺激无反应,这表明β-葡聚糖结构中有一个特定的途径。在 grifolan 或zymosan 的激活中,证明了蛋白 C 和有丝分裂原激活的蛋白激酶的磷酸化的重要性。用 grifolan 刺激时,补体受体(CR3)的免疫沉淀,共沉淀了带有磷酸酪氨酸残基的其他蛋白质。这些数据表明,蛋白激酶 C 和酪氨酸激酶是信号转导所必需的,CR3 可能通过与其他细胞内蛋白的相互作用参与激活。