Smith E M, Blalock J E
Proc Natl Acad Sci U S A. 1981 Dec;78(12):7530-4. doi: 10.1073/pnas.78.12.7530.
Human leukocyte interferon (hIFN-alpha) preparations contain immunologically and biologically recognizable endorphin and corticotropin-like (ACTH-like) activities. The ACTH bioactivity was demonstrable only after pepsin or acid treatment. Highly purified hIFN-alpha was composed of two molecular species of interferon (18,500 and 23,000 daltons). Endorphin activity was associated with both of these molecules. Pepsin treatment of the 23,000-dalton but not the 18,500-dalton hIFN-alpha generated ACTH activity. In acid, the 23,000-dalton hIFN-alpha broke down into the 18,500-dalton form and ACTH (4500 daltons). The ACTH derived from hIFN-alpha by pepsin digestion comigrated with a purified ACTH standard in NaDodSO4/polyacrylamide gel electrophoresis. hIFN-alpha-producing lymphocytes showed positive immunofluorescence after staining with highly specific antisera to ACTH alpha-(1-13) and gamma-endorphin. Essentially 100% of the human peripheral lymphocytes were capable of producing both ACTH and gamma-endorphin-related substances, presumably associated with hIFN-alpha. These results strongly suggest a circuit between the immune and neuroendocrine systems which involves neuroendocrine hormone-like substances, some of which are associated with hIFN-alpha
人白细胞干扰素（hIFN-α）制剂含有免疫和生物学上可识别的内啡肽及促肾上腺皮质激素样（ACTH样）活性。只有在胃蛋白酶或酸处理后，ACTH生物活性才得以显现。高度纯化的hIFN-α由两种分子类型的干扰素组成（18,500和23,000道尔顿）。内啡肽活性与这两种分子均相关。用胃蛋白酶处理23,000道尔顿而非18,500道尔顿的hIFN-α可产生ACTH活性。在酸性条件下，23,000道尔顿的hIFN-α分解为18,500道尔顿的形式和ACTH（4500道尔顿）。经胃蛋白酶消化从hIFN-α衍生的ACTH在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳中与纯化的ACTH标准品共迁移。用针对ACTHα-(1 - 13)和γ-内啡肽的高特异性抗血清染色后，产生hIFN-α的淋巴细胞显示出阳性免疫荧光。基本上100%的人外周淋巴细胞能够产生ACTH和γ-内啡肽相关物质，推测与hIFN-α有关。这些结果有力地表明了免疫和神经内分泌系统之间存在一个涉及神经内分泌激素样物质的回路，其中一些与hIFN-α相关
