Yu C L, Jove R, Burakoff S J
Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
J Immunol. 1997 Dec 1;159(11):5206-10.
The Lck protein, a Src family tyrosine kinase, plays a critical role in T cell maturation and activation. Dysregulation of Lck expression or Lck kinase activity has been implicated in T cell leukemias from mice to humans, although the mechanism underlying Lck-mediated oncogenesis is still largely unclear. We report here that both DNA binding activities and tyrosine phosphorylation of STAT3 and STAT5, but not STAT1, are constitutively enhanced in the mouse T cell lymphoma LSTRA, which is a well-characterized cell line that overexpresses Lck protein and exhibits high levels of Lck kinase activity. Furthermore, Janus kinase 1 (jak1) and Jak2 protein tyrosine kinases are constantly activated in these cells, as determined by their autophosphorylation in an in vitro kinase assay and increased levels of tyrosine phosphorylation on immunoblots. Therefore, like Src-transformed cells, Lck-overexpressing LSTRA cells also exhibit constitutive activation of distinct Jak and STAT proteins.
Lck蛋白是一种Src家族酪氨酸激酶,在T细胞成熟和激活过程中发挥关键作用。从鼠到人的T细胞白血病中均涉及Lck表达失调或Lck激酶活性异常,尽管Lck介导肿瘤发生的机制仍不清楚。我们在此报告,在小鼠T细胞淋巴瘤LSTRA中,STAT3和STAT5(而非STAT1)的DNA结合活性及酪氨酸磷酸化均呈组成性增强,LSTRA是一种特征明确的细胞系,该细胞系Lck蛋白过表达且Lck激酶活性水平较高。此外,通过体外激酶分析中的自身磷酸化及免疫印迹上酪氨酸磷酸化水平升高确定,Janus激酶1(Jak1)和Jak2蛋白酪氨酸激酶在这些细胞中持续被激活。因此,与Src转化细胞一样,Lck过表达的LSTRA细胞也表现出不同Jak和STAT蛋白的组成性激活。