Nerve growth factor modulates myelin-associated glycoprotein binding to sensory neurons
Nerve growth factor modulates myelin-associated glycoprotein binding to sensory neurons
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DOI：
10.1016/s0736-5748(98)00068-9
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发表时间：
1999-04-01
影响因子：
1.8
通讯作者：
Bartlett, PF
中科院分区：
文献类型：
--
作者：
Turnley, AM;Bartlett, PF
髓鞘相关糖蛋白(MAG)是髓鞘/轴突交界处的髓鞘细胞表达的一种分子，它与神经元上的一种未知分子结合。我们使用MAG-免疫球蛋白Fe融合蛋白来检测MAG结合分子在培养的感觉神经元上的表达和调节。MAG-Fe的结合量在24-48h达到最大值，在高表达神经丝的神经元上结合率较高。神经生长因子(SGF)以剂量依赖的方式上调MAG结合分子的表达。雪旺细胞与感觉神经元在无血清培养液中共培养，可刺激MAG结合分子的最大表达，但加入抗NGF可抑制该结合分子的表达。这表明雪旺细胞可以通过产生NGF来调节MAG结合分子的表达，可能是调节髓鞘形成和再髓鞘形成过程中MAG-MAG结合分子相互作用的一种生理机制。(C)1999年综合业务数字网。爱思唯尔科学有限公司出版。版权所有。
Myelin-associated glycoprotein (MAG) is a molecule expressed by myelinating cells at the myelin/axon interface, which binds to an as yet unidentified molecule on neurons. We have used a MAG-immunoglobulin Fe fusion protein to examine the expression and regulation of the MAG binding molecule on sensory neurons in culture. Binding of the MAG Fe reached a maximum at 24-48 h and was higher on neurons which expressed high levels of neurofilament. Nerve growth factor (SGF) upregulated expression of the MAG binding molecule in a dose dependent manner. Schwann cells co-cultured with sensory neurons in serum-free medium stimulated maximal expression of the MAG binding molecule, which was decreased by addition of anti-NGF to the co-cultures. This indicated that Schwann cells can modulate expression of the MAG binding molecule via production of NGF and may represent a physiological mechanism for regulation of MAG-MAG binding molecule interactions during myelination and remyelination. (C) 1999 ISDN. Published by Elsevier Science Ltd. All rights reserved.