Matsuyoshi N, Hamaguchi M, Taniguchi S, Nagafuchi A, Tsukita S, Takeichi M
Department of Dermatology, Faculty of Medicine, Kyoto University, Japan.
J Cell Biol. 1992 Aug;118(3):703-14. doi: 10.1083/jcb.118.3.703.
Rat 3Y1 cells acquire metastatic potential when transformed with v-src, and this potential is enhanced by double transformation with v-src and v-fos (Taniguchi, S., T. Kawano, T. Mitsudomi, G. Kimura, and T. Baba. 1986. Jpn. J. Cancer Res. 77:1193-1197). We compared the activity of cadherin cell adhesion molecules of normal 3Y1 cells with that of v-src transformed (SR3Y1) and v-src and v-fos double transformed (fosSR3Y1) 3Y1 cells. These cells expressed similar amounts of P-cadherin, and showed similar rates of cadherin-mediated aggregation under suspended conditions. However, the aggregates or colonies of these cells were morphologically distinct. Normal 3Y1 cells formed compacted aggregates in which cells are firmly connected with each other, whereas the transformed cells were more loosely associated, and could freely migrate out of the colonies. Overexpression of exogenous E-cadherin in these transformed cells had no significant effect on their adhesive properties. We then found that herbimycin A, a tyrosine kinase inhibitor, induced tighter cell-cell associations in the aggregates of the transformed cells. In contrast, vanadate, a tyrosine phosphatase inhibitor, inhibited the cadherin-mediated aggregation of SR3Y1 and fosSR3Y1 cells but had little effect on that of normal 3Y1 cells. These results suggest that v-src-mediated tyrosine phosphorylation perturbs cadherin function directly or indirectly, and the inhibition of tyrosine phosphorylation restores cadherin action to the normal state. We next studied tyrosine phosphorylation on cadherins and the cadherin-associated proteins, catenins. While similar amounts of catenins were expressed in all of these cells, the 98-kD catenin was strongly tyrosine phosphorylated only in SR3Y1 and fosSR3Y1 cells. Cadherins were also weakly tyrosine phosphorylated only in the transformed cells. The tyrosine phosphorylation of these proteins was enhanced by vanadate, and inhibited by herbimycin A. Thus, the tyrosine phosphorylation of the cadherin-catenin system itself might affect its function, causing instable cell-cell adhesion.
用v-src转化大鼠3Y1细胞时,该细胞获得转移潜能,而用v-src和v-fos双重转化可增强这种潜能(谷口史郎、川野哲、光富俊己、木村浩、马场隆. 1986. 日本癌症研究杂志. 77:1193 - 1197)。我们比较了正常3Y1细胞与v-src转化的(SR3Y1)以及v-src和v-fos双重转化的(fosSR3Y1)3Y1细胞中钙黏蛋白细胞黏附分子的活性。这些细胞表达相似量的P-钙黏蛋白,并且在悬浮条件下表现出相似的钙黏蛋白介导的聚集率。然而,这些细胞的聚集体或集落形态不同。正常3Y1细胞形成紧密的聚集体,其中细胞彼此牢固连接,而转化细胞的连接较松散,并且能够自由地从集落中迁移出来。在这些转化细胞中外源E-钙黏蛋白的过表达对其黏附特性没有显著影响。然后我们发现,酪氨酸激酶抑制剂赫伯霉素A在转化细胞的聚集体中诱导更紧密的细胞间结合。相反,酪氨酸磷酸酶抑制剂钒酸盐抑制SR3Y1和fosSR3Y1细胞的钙黏蛋白介导的聚集,但对正常3Y1细胞的聚集影响很小。这些结果表明,v-src介导的酪氨酸磷酸化直接或间接扰乱钙黏蛋白功能,并且酪氨酸磷酸化的抑制将钙黏蛋白作用恢复到正常状态。接下来我们研究了钙黏蛋白和钙黏蛋白相关蛋白连环蛋白上的酪氨酸磷酸化。虽然所有这些细胞中表达的连环蛋白量相似,但98-kD连环蛋白仅在SR3Y1和fosSR3Y1细胞中被强烈酪氨酸磷酸化。钙黏蛋白也仅在转化细胞中被弱酪氨酸磷酸化。这些蛋白质的酪氨酸磷酸化被钒酸盐增强,被赫伯霉素A抑制。因此,钙黏蛋白-连环蛋白系统本身的酪氨酸磷酸化可能影响其功能,导致细胞间黏附不稳定。