Wolter H J
Peptides. 1986 May-Jun;7(3):389-92. doi: 10.1016/0196-9781(86)90003-3.
By the use of the immunofluorescent microscopic staining technique, adjacent serial sections through the rat duodenum were alternately stained with specific antisera directed to the opioid peptides alpha-neo-endorphin and dynorphin-A(1-8). alpha-Neo-endorphin immunoreactivity has been revealed exclusively within perikarya lying intramurally in the longitudinal muscle layer. These alpha-neo-endorphin and dynorphin-A(1-8) immunoreactive perikarya were large in diameter, round in shape, contained a large and round nucleus, and were recognized only occasionally there. alpha-Neo-endorphin immunoreactivity was coexistent with dynorphin-A(1-8)-positive material within these perikarya. Since no alpha-neo-endorphin material was detected within duodenal nerve fibres and terminals, it might be concluded that this peptide is further enzymatically cleaved to the opioid pentapeptide Leu-enkephalin during its axonal transport from intramural perikarya to nerve terminals and during its storage there.
通过使用免疫荧光显微镜染色技术,对大鼠十二指肠的相邻连续切片交替用针对阿片肽α-新内啡肽和强啡肽A(1-8)的特异性抗血清进行染色。仅在纵肌层壁内的核周体中发现了α-新内啡肽免疫反应性。这些α-新内啡肽和强啡肽A(1-8)免疫反应性核周体直径大、呈圆形、含有一个大的圆形细胞核,且仅偶尔在那里被识别。在这些核周体中,α-新内啡肽免疫反应性与强啡肽A(1-8)阳性物质共存。由于在十二指肠神经纤维和终末内未检测到α-新内啡肽物质,因此可以得出结论,该肽在从壁内核周体向神经终末的轴突运输过程中以及在那里储存期间会进一步被酶解为阿片五肽亮氨酸脑啡肽。