Healy D L
Baillieres Clin Obstet Gynaecol. 1991 Mar;5(1):95-105. doi: 10.1016/s0950-3552(05)80072-0.
The role of prolactin in human implantation and human endometrial function is still unclear. Synthesis of prolactin from human endometrium and decidua was first demonstrated in 1977. Prolactin mRNA isolation from term decidua subsequently confirmed expression of the prolactin gene in human endometrium. More recently, a glycosylated form of prolactin has been isolated from both the human pituitary and human endometrium. It appears that predominately glycosylated prolactin is secreted in the late luteal phase of the menstrual cycle, with increasingly greater amounts of non-glycosylated prolactin secreted as pregnancy advances. The biological significance and regulation of prolactin glycosylation is uncertain, although glycosylated ovine prolactin has only 20-33% of the lactogenic activity of ovine prolactin. Pituitary lactotropes, of ectodermal origin, produce pituitary prolactin and are regulated by dopamine, oestradiol and thyrotropin releasing hormone. Decidual cells, of mesodermal origin, are not influenced by these pituitary secretogogues. Progesterone and calcium both appear to stimulate pituitary and decidual prolactin secretion, while arachidonic acid seems to inhibit decidual prolactin release. More recently, insulin like growth factor-1, a polypeptide growth factor implicated in the oestrogen promoted growth reproductive tissues, has been found in high concentration in the pig uterus and has been shown to stimulate the synthesis and secretion of prolactin from human decidua. Prolactin receptors have not been reported on endothelium of blood vessels and no clear evidence exists that endometrial prolactin may modulate the secretion of endothelin, endothelium derived relaxing factor or other potentially important substances controlling menstruation. Prolactin does appear necessary for the normal production of macrophage activating factors, including interferon, and may have a local immunomodulatory role upon human implantation for this reason. Human alpha 2-interferon has sequence homology to ovine trophoblast protein-1 and is found in high concentration in human pregnancy and fetal tissues. There is some evidence that interferon may reduce human endometrial prolactin secretion, but whether endometrial or decidual prolactin is critical to human implantation awaits further study.
催乳素在人类着床及人类子宫内膜功能中的作用仍不明确。1977年首次证实了人类子宫内膜和蜕膜能合成催乳素。随后从足月蜕膜中分离出催乳素mRNA，进一步证实了催乳素基因在人类子宫内膜中的表达。最近，已从人垂体和人子宫内膜中分离出一种糖基化形式的催乳素。似乎在月经周期的黄体晚期主要分泌糖基化催乳素，随着妊娠进展，非糖基化催乳素的分泌量逐渐增加。尽管糖基化的绵羊催乳素的泌乳活性仅为绵羊催乳素的20 - 33%，但催乳素糖基化的生物学意义及调控尚不确定。起源于外胚层的垂体催乳细胞产生垂体催乳素，并受多巴胺、雌二醇和促甲状腺激素释放激素的调节。起源于中胚层的蜕膜细胞不受这些垂体促分泌素的影响。孕酮和钙似乎都能刺激垂体和蜕膜催乳素的分泌，而花生四烯酸似乎能抑制蜕膜催乳素的释放。最近，胰岛素样生长因子-1，一种与雌激素促进生殖组织生长有关的多肽生长因子，在猪子宫中含量很高，并且已被证明能刺激人蜕膜中催乳素的合成和分泌。血管内皮上尚未报道有催乳素受体，也没有明确证据表明子宫内膜催乳素可能调节内皮素、内皮源性舒张因子或其他控制月经的潜在重要物质的分泌。催乳素似乎是正常产生包括干扰素在内的巨噬细胞激活因子所必需的，因此可能在人类着床过程中具有局部免疫调节作用。人α2 -干扰素与绵羊滋养层蛋白-1具有序列同源性，在人类妊娠和胎儿组织中含量很高。有证据表明干扰素可能会减少人子宫内膜催乳素的分泌，但子宫内膜或蜕膜催乳素对人类着床是否至关重要还有待进一步研究。
