Immunocytochemical localization of the vanilloid receptor 1 (VR1):: relationship to neuropeptides, the P2X3 purinoceptor and IB4 binding sites
Immunocytochemical localization of the vanilloid receptor 1 (VR1):: relationship to neuropeptides, the P2X3 purinoceptor and IB4 binding sites
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DOI：
10.1046/j.1460-9568.1999.00503.x
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发表时间：
1999-03-01
影响因子：
3.4
通讯作者：
Elde, R
中科院分区：
文献类型：
--
作者：
Guo, A;Vulchanova, L;Elde, R
辣椒素受体（VR 1）蛋白既是辣椒素的受体，又是有害热刺激的转换器。为了确定这种蛋白质的表达和靶向，我们已经产生了针对VR 1的氨基和羧基末端的抗血清。在大鼠的背顶叶和三叉神经节内，VR 1免疫反应（VR 1-ir）仅限于中小型神经元。VRI免疫反应阳性神经元分布于这些初级传入神经元的中枢和外周突起，表现为：（i）VRI免疫反应阳性神经元分布于背角浅层第一层和第二层的神经纤维和终末，并与皮肤和角膜中的小直径神经纤维相联系;和（iii）VR 1-ir在坐骨神经结扎近端的积聚。在超微结构水平，VR 1-ir与背根神经节的神经元胞体和背角的神经末梢的质膜有关。在三叉神经脊束核和孤束核的神经纤维和终末也可见VR 1免疫阳性反应。在大部分背根神经节神经元及其轴突末梢中，VR 1-ir与P2 X（3）嘌呤受体的染色和凝集素IB 4的结合位点共定位。令人惊讶的是，VR 1-IR基本上没有共存于神经纤维和终端，含有P物质和降钙素基因相关肽，这表明复杂的机制，这些神经肽的释放响应辣椒素的应用。
The vanilloid receptor (VR1) protein functions both as a receptor for capsaicin and a transducer of noxious thermal stimuli. To determine the expression and targetting of this protein, we have generated antisera against both the amino and carboxy termini of VR1. Within the dorsal roof and trigeminal ganglia of rats VR1-immunoreactivity (VR1-ir) was restricted to small and medium sized neurons. VRI-ir was transported into both the central and peripheral processes of these primary afferent neurons, as evidenced by: (i) the presence of VR1-ir in nerve fibres and terminals in lamina I and lamina II of the superficial dorsal horn, and the association of VRI-ir with smalt diameter nerve fibres in the skin and cornea; (ii) the reduction of VR1-ir in the spinal cord after dorsal rhizotomy; and (iii) the accumulation of VR1-ir proximal to sciatic nerve ligation. At the ultrastructural level, VR1-ir was associated with plasma membranes of neuronal perikarya in dorsal root ganglia and nerve terminals in the dorsal horn. VR1-ir was also seen in nerve fibres and terminals in the spinal trigeminal nucleus and nucleus of the solitary tract. Within a large proportion of dorsal root ganglion neurons and the terminals of their axons, VR1-ir was colocalized with staining for the P2X(3) purinoceptor, and with binding sites for the lectin IB4. Surprisingly, VR1-ir did not coexist substantially in nerve fibres and terminals that contain substance P and calcitonin gene-related peptide, suggesting complex mechanisms for the release of these neuropeptides in response to capsaicin application.