Ozeki Y, Matsui T, Titani K
Institute for Comprehensive Medical Science, Fujita Health University School of Medicine, Aichi, Japan.
FEBS Lett. 1991 Sep 9;289(2):145-7. doi: 10.1016/0014-5793(91)81055-d.
Cell adhesive activity of two animal lectins, frog (Rana catesbeiana) S-type 14K lectin and echinoidin (a C-type lectin from sea urchin plasma), was studied with human rhabdomyosarcoma (RD) cells. RD cells attached to and spread on plastic plates coated with each lectin. Cell adhesion by the frog lectin was completely inhibited by the addition of lactose or asialofetuin glycopeptide. Echinoidin-induced cell adhesion was only inhibited by peptide GRGDS. Since echinoidin is known to contain an RGD-sequence, our results clearly indicate that this sequence is active as the cell adhesive signal. These results suggest that some of the animal lectins may function as a cell adhesive molecule rather than using the carbohydrate-recognition mechanism.
利用人横纹肌肉瘤（RD）细胞研究了两种动物凝集素——青蛙（牛蛙）S型14K凝集素和海胆素（一种来自海胆血浆的C型凝集素）的细胞黏附活性。RD细胞能够附着在涂有每种凝集素的塑料平板上并在其上铺展。添加乳糖或去唾液酸胎球蛋白糖肽可完全抑制青蛙凝集素引起的细胞黏附。只有肽GRGDS能抑制海胆素诱导的细胞黏附。由于已知海胆素含有RGD序列，我们的结果清楚地表明该序列作为细胞黏附信号具有活性。这些结果表明，一些动物凝集素可能作为细胞黏附分子发挥作用，而不是利用碳水化合物识别机制。
