Buckley A R, Rao Y P, Buckley D J, Gout P W
Department of Pharmacology and Toxicology, University of North Dakota School of Medicine, Grand Forks 58202-9037.
Biochem Biophys Res Commun. 1994 Nov 15;204(3):1158-64. doi: 10.1006/bbrc.1994.2584.
The coupling of prolactin (PRL) receptor ligation to activation of mitogen-activated protein (MAP) kinase was sought in rat Nb2 lymphoma cells, a pre-T lymphocyte line dependent upon lactogens for proliferation. Addition of PRL (20 ng/ml) to Nb2 cells, growth arrested in the early G1 phase of cell cycle, stimulated rapid tyrosyl phosphorylation of MAP kinase (min). Phosphorylated MAP kinase subsequently translocated to the nucleus, with kinetics essentially identical to those demonstrated for nuclear accumulation of PRL. The rapidity of MAP kinase activation suggests an intermediary role for this enzyme in PRL receptor signalling. Moreover, nuclear translocation of MAP kinase provides an interactive mechanism by which PRL, together with its nuclear receptor, may regulate transcription requisite for mitogenesis.
在大鼠Nb2淋巴瘤细胞（一种依赖催乳素进行增殖的前T淋巴细胞系）中，研究催乳素（PRL）受体连接与丝裂原活化蛋白（MAP）激酶激活之间的偶联关系。向处于细胞周期G1期早期生长停滞状态的Nb2细胞中添加PRL（20 ng/ml），可刺激MAP激酶迅速发生酪氨酰磷酸化（数分钟内）。随后，磷酸化的MAP激酶转位至细胞核，其动力学与PRL核积累所显示的基本相同。MAP激酶激活的快速性表明该酶在PRL受体信号传导中起中间作用。此外，MAP激酶的核转位提供了一种相互作用机制，通过该机制，PRL与其核受体一起可能调节有丝分裂所需的转录。
