Ignelzi M A, Miller D R, Soriano P, Maness P F
Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599-7260.
Neuron. 1994 Apr;12(4):873-84. doi: 10.1016/0896-6273(94)90339-5.
The nonreceptor tyrosine protein kinases pp60c-src, p59fyn, and pp62c-yes are localized in growth cones of developing neurons, but their function is undefined. To determine whether these tyrosine kinases were capable of regulating substrate-dependent axon growth, cultures of cerebellar neurons from wild-type, src-, fyn-, and yes- mice were analyzed for neurite outgrowth on the neural cell adhesion molecule L1 or the extracellular matrix protein laminin. The rate of neurite extension on L1 was reduced in src-, but not in fyn- or yes- neurons. Neurite extension on laminin was unaltered in src-, fyn-, or yes- neurons, indicating that pp60c-src, p59fyn, or pp62c-yes is not likely to participate in integrin-dependent axon growth. These results demonstrate that pp60c-src is a component of the intracellular signaling pathway in L1-mediated axonal growth and suggest that Src-related nonreceptor tyrosine kinases may have distinct, nonredundant functions in the nervous system.
非受体酪氨酸蛋白激酶pp60c-src、p59fyn和pp62c-yes定位于发育中神经元的生长锥，但它们的功能尚不清楚。为了确定这些酪氨酸激酶是否能够调节依赖底物的轴突生长，对来自野生型、src-、fyn-和yes-小鼠的小脑神经元培养物进行分析，观察其在神经细胞粘附分子L1或细胞外基质蛋白层粘连蛋白上的神经突生长情况。src-神经元在L1上的神经突延伸速率降低，但fyn-或yes-神经元未出现这种情况。src-、fyn-或yes-神经元在层粘连蛋白上的神经突延伸未发生改变，这表明pp60c-src、p59fyn或pp62c-yes不太可能参与整合素依赖的轴突生长。这些结果表明，pp60c-src是L1介导的轴突生长中细胞内信号通路的一个组成部分，并提示Src相关的非受体酪氨酸激酶在神经系统中可能具有不同的、非冗余的功能。
