Maeda Reiko, Ida Tomoaki, Ihara Hideshi, Sakamoto Tatsuji
Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, Japan.
Biosci Biotechnol Biochem. 2012;76(3):501-5. doi: 10.1271/bbb.110813.
Polysaccharides were extracted from Caulerpa lentillifera by treating with water and then purified by size-exclusion chromatography. The purified polysaccharides, termed SP1, were found to be sulfated xylogalactans with a molecular mass of more than 100 kDa. Adding SP1 to murine macrophage RAW 264.7 cells increased the production of nitric oxide (NO) in a dose-dependent manner. NO was found by immunoblotting and RT-PCR analyses to be synthesized by an inducible NO synthase. SP1 caused the degradation of IκB-α and the nuclear translocation of nuclear factor (NF)-κB subunit p65 in macrophage cells. SP1 also increased the phosphorylation of p38 mitogen-activated protein kinase (MAPK). These results demonstrate that SP1 activated macrophage cells via both the NF-κB and p38 MAPK signaling pathways. Moreover, SP1 increased the expression of various genes encoding cytokines, and the phagocytic activity of macrophage cells. These combined results show that SP1 immunostimulated the activity of macrophage cells.
通过用水处理从小孔蕨中提取多糖，然后通过尺寸排阻色谱法进行纯化。纯化后的多糖称为SP1，被发现是分子量超过100 kDa的硫酸化木糖半乳聚糖。将SP1添加到小鼠巨噬细胞RAW 264.7细胞中，一氧化氮（NO）的产生呈剂量依赖性增加。通过免疫印迹和RT-PCR分析发现，NO是由诱导型NO合酶合成的。SP1导致巨噬细胞中IκB-α的降解和核因子（NF）-κB亚基p65的核转位。SP1还增加了p38丝裂原活化蛋白激酶（MAPK）的磷酸化。这些结果表明，SP1通过NF-κB和p38 MAPK信号通路激活巨噬细胞。此外，SP1增加了各种编码细胞因子的基因的表达以及巨噬细胞的吞噬活性。这些综合结果表明，SP1免疫刺激了巨噬细胞的活性。
