Yarden Y, Weinberg R A
Whitehead Institute for Biomedical Research, Cambridge, MA 02142.
Proc Natl Acad Sci U S A. 1989 May;86(9):3179-83. doi: 10.1073/pnas.86.9.3179.
There is a growing list of oncogenes encoding transmembrane tyrosine kinases that have structures reminiscent of growth factor receptors. In most cases, the ligands for these putative receptors are unknown. Using the neu oncogene as a model system, we have developed several experimental approaches for the detection of such hypothetical ligands. The following lines of evidence collectively imply that a candidate ligand of the neu-encoded oncoprotein is secreted by ras-transformed fibroblasts: Medium conditioned by ras transformants is able to induce down-modulation of the neu-encoded p185 and to activate its intrinsic tyrosine kinase activity in vitro. In addition, a rapid increase in the phosphorylation in vivo of tyrosine residues of the neu-encoded protein is induced by the conditioned medium. Finally, transfer of the neu gene into hematopoietic cells renders them mitogenically responsive to the conditioned medium. The possibility of indirect activation of the oncoprotein through other known receptors, especially the receptor for the epidermal growth factor, was experimentally excluded.
编码跨膜酪氨酸激酶的癌基因越来越多,其结构让人联想到生长因子受体。在大多数情况下,这些假定受体的配体尚不清楚。以neu癌基因为模型系统,我们开发了几种实验方法来检测此类假设的配体。以下一系列证据共同表明,ras转化的成纤维细胞分泌neu编码癌蛋白的候选配体:ras转化体条件培养基能够诱导neu编码的p185下调,并在体外激活其内在酪氨酸激酶活性。此外,条件培养基可诱导neu编码蛋白酪氨酸残基在体内磷酸化迅速增加。最后,将neu基因转入造血细胞使其对条件培养基产生有丝分裂反应。通过实验排除了通过其他已知受体(尤其是表皮生长因子受体)间接激活癌蛋白的可能性。