Luteinizing hormone-releasing hormone neurons in human preoptic/hypothalamus: differential intraneuronal localization of immunoreactive forms.
Luteinizing hormone-releasing hormone neurons in human preoptic/hypothalamus: differential intraneuronal localization of immunoreactive forms.
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人类视前/下丘脑中的黄体生成素释放激素神经元：免疫反应形式的神经元内定位差异。
DOI：
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发表时间：
1985
影响因子：
5.8
通讯作者：
E. Stopa
中科院分区：
文献类型：
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作者：
J. C. King;E. Anthony;D. Fitzgerald;E. Stopa
促黄体生成激素释放激素（LRH）可以作为一个更大的激素原的一部分合成，就像其他几种神经肽一样。在这项研究中，我们不仅要确定人类视前区和下丘脑内LRH神经元的分布和形态学特征，而且要确定LRH在这些神经元中的初始合成、翻译后转化为十肽和储存的位点。免疫反应性分子的形式进行了区分，使用一系列的抗血清具有不同的特异性，在过氧化物酶-抗过氧化物酶技术。这些抗血清能够检测完全加工的激素以及扩展的十肽序列。免疫阳性LRH神经元更丰富的漏斗区的下丘脑比视前区。反应产物的免疫阳性胞体数目和亚细胞分布随抗血清的结合要求而变化。处理后的抗血清，需要充分加工的十肽结合，反应产物几乎完全与颗粒的胞体和过程，而很少与粗糙内质网（RER）或高尔基体。与此相反，与能够检测延长形式的十肽的抗血清，RER和高尔基体被标记，除了颗粒。从这些数据，我们推断，在人类中，成熟的十肽是存在于颗粒内LRH神经元胞体和过程。此外，与RER和高尔基体相关的分子形式可能是十肽序列延伸的前体。
Luteinizing hormone-releasing hormone (LRH) may be synthesized as part of a larger prohormone, as are several other neuropeptides. In this study, we sought not only to define the distribution and morphological characteristics of LRH neurons within the human preoptic area and hypothalamus, but also to identify sites of initial synthesis, posttranslational conversion to the decapeptide, and storage of LRH in these neurons. Immunoreactive molecular forms were differentiated using a series of antisera with distinct specificities in the peroxidase-antiperoxidase technique. These antisera were capable of detecting the fully processed hormone as well as extended decapeptide sequences. Immunopositive LRH neurons were more abundant in the infundibular area of the hypothalamus than in the preoptic area. Numbers of immunopositive perikarya and subcellular distribution of reaction product varied with binding requirements of the antisera. After treatment with an antiserum that requires the fully processed decapeptide for binding, the reaction product was associated almost entirely with granules in perikarya and processes, while very little was associated with either rough endoplasmic reticulum (RER) or Golgi apparatus. In contrast, with an antiserum capable of detecting extended forms of the decapeptide, the RER and Golgi were labeled in addition to granules. From these data, we infer that in humans, mature decapeptide is present in granules within LRH neuronal perikarya and processes. Furthermore, the molecular forms associated with RER and Golgi may be precursors in which the decapeptide sequence is extended.