Ali I U, Hynes R O
Biochim Biophys Acta. 1977 Nov 15;471(1):16-24. doi: 10.1016/0005-2736(77)90388-1.
We have investigated the effects of the drugs cytochalasin B and colchicine on the surface levels of the large, external, transformation-sensitive (LETS) glycoprotein. Colchicine neither removed LETS protein from the surface, nor inhibited its regeneration after removal by mild trypsinization. Cells treated with cytochalasin B, however, showed both a 2-3-fold increase in the turnover rate of their surface LETS protein and a marked inhibition in its regeneration. Inhibition of regeneration was not due to inhibition of synthesis or transport to the surface. In fact, in the presence of cytochalasin B, increased quantities of LETS protein were released into the medium. The results are consistent with the idea of an association of LETS protein with the actin-containing microfilaments. However, other possible explanations, such as effects on cellular morphology or on transport of sugar precursors cannot yet be excluded.
我们研究了细胞松弛素B和秋水仙碱这两种药物对大的、外部的、转化敏感(LETS)糖蛋白表面水平的影响。秋水仙碱既没有从表面去除LETS蛋白,也没有抑制其在经温和胰蛋白酶处理后被去除后的再生。然而,用细胞松弛素B处理的细胞,其表面LETS蛋白的周转率增加了2至3倍,并且其再生受到明显抑制。再生抑制并非由于合成或向表面运输的抑制。事实上,在细胞松弛素B存在的情况下,更多数量的LETS蛋白被释放到培养基中。这些结果与LETS蛋白与含肌动蛋白的微丝相关的观点一致。然而,其他可能的解释,如对细胞形态或糖前体运输的影响,目前尚不能排除。