Hantzopoulos Petros A, Suri Chitra, Glass David J, Goldfarb Mitchell P, Yancopoulos George D
Regeneron Pharmaceuticals, Inc., Tarrytown, New York 10591.
Neuron. 1994 Jul;13(1):187-201. doi: 10.1016/0896-6273(94)90469-3.
NGF and the other neurotrophins all bind to the low affinity NGF receptor (LNGFR). Although early studies suggested that the LNGFR was absolutely required for the formation of a functional neurotrophin receptor, current evidence indicates that the Trk family of receptor tyrosine kinases, in the absence of the LNGFR, can directly bind to and mediate responses to the neurotrophins. Here we describe a functional approach, in fibroblasts, designed to assay for the ability of the LNGFR to potentiate Trk-mediated responses to the neurotrophins. We report that although collaboration between the LNGFR and the Trks could be detected in this system, a truncated form of the LNGFR displayed a much more dramatic ability to interact functionally with each of the Trks, potentiating masked autocrine loops as well as responses to limiting amounts of exogenously provided neurotrophins.
神经生长因子（NGF）和其他神经营养因子都与低亲和力NGF受体（LNGFR）结合。尽管早期研究表明，功能性神经营养因子受体的形成绝对需要LNGFR，但目前的证据表明，在没有LNGFR的情况下，受体酪氨酸激酶的Trk家族可以直接结合并介导对神经营养因子的反应。在这里，我们描述了一种在成纤维细胞中的功能性方法，旨在检测LNGFR增强Trk介导的对神经营养因子反应的能力。我们报告说，尽管在这个系统中可以检测到LNGFR和Trk之间的协作，但LNGFR的截短形式显示出与每个Trk在功能上相互作用的能力更强，增强了隐蔽的自分泌环以及对外源提供的有限量神经营养因子的反应。
