Fischer A, Kummer W, Couraud J Y, Adler D, Branscheid D, Heym C
Institute for Anatomy and Cell Biology I, University of Heidelberg, Germany.
Lab Invest. 1992 Sep;67(3):387-93.
Tissue sections of human cervical trachea were processed for immunohistochemical demonstration of receptors for substance P [using an anti-SP anti-idiotypic antiserum directed toward the ligand binding site of the receptor (Couraud J-Y, Escher ED, Regoli D, Imhof V, Rossignol B, Pradelles P. Anti-substance P anti-idiotypic antibodies: Characterization and biological activities. J Biol Chem 1985;260:9461-9; Couraud J-Y, Maillet S, Grassi J, Frobert Y, Pradelles P. Characterization and properties of anti-substance P antiidiotypic antibodies. Methods Enzymol 1989; 178:275-300)] and vasoactive intestinal peptide (VIP; utilizing a monoclonal antibody toward VIP receptors of an adenocarcinoma cell line (Pichon J, Hirn M, Muller J-M, Mangeat P, Marvaldi J. Anticell surface monoclonal antibodies which antagonize the action of VIP in a human adenocarcinoma cell line (HT29). EMBO J 1983;2:1017-22)], respectively. Mucus cells of the submucosal glands (identified by periodic acid Schiff staining) and neuroendocrine cells of the respiratory epithelium (identified by immunoreactivity to protein gene product 9.5) displayed intense VIP receptor-immunoreactivity. Other tissue components known to respond to exogenously administered VIP, e.g., trachealis muscle, lacked VIP receptor-immunoreactivity, indicating that the monoclonal antibody did not label all receptor subtypes. In accordance with the known pharmacological actions of substance P upon the airways, the anti-substance P receptor antibody labeled the trachealis muscle, submucosal glands, and respiratory epithelium, predominantly at the luminal aspect. Since substance P as well as the structurally related tachykinin, neurokinin A, competed with the anti-receptor antibody in binding to the tissue section, it is likely that both NK-1 and NK-2 receptor subtypes were labeled. The present histochemical approach to localize peptide receptors in the trachea allowed precise analysis of distribution unreached by previous studies using autoradiography. Together with pharmacological data, these morphological findings contribute to the understanding of the sequences of events evoked by the neuropeptides, substance P and VIP, in the human trachea.
对人颈段气管组织切片进行处理，分别用于免疫组织化学显示P物质受体[使用针对受体配体结合位点的抗P物质抗独特型抗血清（库劳德J - Y、埃舍尔E D、雷戈利D、因霍夫V、罗西尼奥尔B、普拉德莱斯P。抗P物质抗独特型抗体：特性与生物学活性。《生物化学杂志》1985年；260:9461 - 9；库劳德J - Y、马耶特S、格拉西J、弗罗贝尔Y、普拉德莱斯P。抗P物质抗独特型抗体的特性与性质。《酶学方法》1989年；178:275 - 300）]和血管活性肠肽（VIP；利用针对腺癌细胞系VIP受体的单克隆抗体（皮雄J、欣M、米勒J - M、芒热P、马尔瓦尔迪J。拮抗人腺癌细胞系（HT29）中VIP作用的抗细胞表面单克隆抗体。《欧洲分子生物学组织杂志》1983年；2:1017 - 22）]。黏膜下腺的黏液细胞（通过过碘酸希夫染色鉴定）和呼吸上皮的神经内分泌细胞（通过对蛋白基因产物9.5的免疫反应性鉴定）显示出强烈的VIP受体免疫反应性。已知对外源性给予的VIP有反应的其他组织成分，如气管肌，缺乏VIP受体免疫反应性，这表明单克隆抗体并未标记所有受体亚型。根据P物质对气道的已知药理作用，抗P物质受体抗体标记了气管肌、黏膜下腺和呼吸上皮，主要在管腔面。由于P物质以及结构相关的速激肽神经激肽A在与组织切片结合时与抗受体抗体竞争，很可能NK - 1和NK - 2受体亚型都被标记了。目前在气管中定位肽受体的组织化学方法能够精确分析以往放射自显影研究未涉及的分布情况。这些形态学发现与药理学数据一起，有助于理解神经肽P物质和VIP在人气管中引发的一系列事件。
