den Hertog J, Pals C E, Peppelenbosch M P, Tertoolen L G, de Laat S W, Kruijer W
Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Utrecht.
EMBO J. 1993 Oct;12(10):3789-98. doi: 10.1002/j.1460-2075.1993.tb06057.x.
Here we report that protein tyrosine phosphatases (PTPases), like their enzymatic counterpart the protein tyrosine kinases, can play an important role in cell differentiation. Expression of the transmembrane PTPase receptor protein tyrosine phosphatase alpha (RPTP alpha) is transiently enhanced during neuronal differentiation of embryonal carcinoma (EC) and neuroblastoma cells. Retinoic acid induces wild type P19 cells to differentiate into endoderm- and mesoderm-like cells. By contrast, retinoic acid treatment leads to neuronal differentiation of P19 cells, ectopically expressing functional RPTP alpha, as illustrated by their ability to generate action potentials. Endogenous pp60c-src kinase activity is enhanced in the RPTP alpha-transfected cells, which may be due to direct dephosphorylation of the regulatory Tyr residue at position 527 in pp60c-src by RPTP alpha. Our results demonstrate that RPTP alpha is involved in neuronal differentiation and imply a role for pp60c-src in the differentiation process.
在此我们报告，蛋白质酪氨酸磷酸酶（PTPases）与其酶促对应物蛋白质酪氨酸激酶一样，可在细胞分化中发挥重要作用。跨膜PTPase受体蛋白酪氨酸磷酸酶α（RPTPα）的表达在胚胎癌（EC）和神经母细胞瘤细胞的神经元分化过程中短暂增强。视黄酸诱导野生型P19细胞分化为内胚层和中胚层样细胞。相比之下，视黄酸处理导致异位表达功能性RPTPα的P19细胞发生神经元分化，这可通过它们产生动作电位的能力来证明。内源性pp60c-src激酶活性在转染RPTPα的细胞中增强，这可能是由于RPTPα直接使pp60c-src中第527位的调节性酪氨酸残基去磷酸化所致。我们的结果表明RPTPα参与神经元分化，并暗示pp60c-src在分化过程中发挥作用。
