Wolff C H, Akerman K E
Biochim Biophys Acta. 1982 Dec 22;693(2):315-9. doi: 10.1016/0005-2736(82)90437-0.
Addition of the mitogenic lectin concanavalin A to rat spleen cells results in a small increase in the steady-state Ca2+ content of the cells. 45Ca2+ fluxes were measured under conditions where artifacts due to Ca2+ binding to concanavalin A could be excluded. Both 45Ca2+ influx into and efflux from these cells are significantly activated by the lectin. If 45Ca2+ is added 30 min after concanavalin A the rate of influx is further enhanced. The increase in 45Ca2+ influx correlates well with binding of concanavalin A to the cells. At low concentrations (optimal mitogenic) of the lectin (1 and 3 micrograms/ml) no significant increase in 45Ca2+ influx occurs but an increase in 45Ca2+ efflux is still observed. The results suggest that concanavalin A binding to the cell surface causes an increase in Ca2+ influx into the cells and that activation of Ca2+ efflux occurs as a response to an increase in the cytosolic Ca2+ activity. Thus, Ca2+ may well play a role in triggering lymphocyte activation.
向大鼠脾细胞中添加促有丝分裂凝集素伴刀豆球蛋白A会使细胞内稳态Ca2+含量略有增加。在可以排除因Ca2+与伴刀豆球蛋白A结合而产生假象的条件下测量45Ca2+通量。这种凝集素能显著激活这些细胞对45Ca2+的摄取和流出。如果在加入伴刀豆球蛋白A 30分钟后再添加45Ca2+,摄取速率会进一步提高。45Ca2+摄取的增加与伴刀豆球蛋白A与细胞的结合密切相关。在凝集素的低浓度(最佳促有丝分裂浓度)(1和3微克/毫升)下,45Ca2+摄取没有显著增加,但仍观察到45Ca2+流出增加。结果表明,伴刀豆球蛋白A与细胞表面的结合会导致细胞对Ca2+摄取增加,并且Ca2+流出的激活是对胞质Ca2+活性增加的一种反应。因此,Ca2+很可能在触发淋巴细胞激活中起作用。