Baird A, Wehrenberg W B, Ling N
Neuroendocrinology. 1986;42(4):273-6. doi: 10.1159/000124451.
Synthetic rat, human, bovine/caprine, porcine and ovine growth hormone-releasing factor (GRF) were tested for their capacity to release growth hormone (GH) by the rat anterior pituitary in vitro. All peptides elicited parallel and dose-dependent increases in GH release and produced similar maximal GH secretion. Rat GRF was 3-6 times more potent in stimulating the release of GH than all other GRFs, while human, bovine/caprine, porcine and ovine GRF had potencies that were not statistically different. The increased potency of both rat GRF(1-27)NH2 and rat GRF(1-23)NH2 when compared to human GRF(1-27)NH2 and human GRF(1-23)NH2, respectively, suggests that the increased potency of this molecule resides in structural differences in the amino terminal of native GRF. The results demonstrate increased sensitivity of rat pituitary cells for their homologous releasing factor.
对合成的大鼠、人、牛/羊、猪和羊生长激素释放因子(GRF)进行了测试,以检测它们在体外刺激大鼠垂体前叶释放生长激素(GH)的能力。所有肽均引起GH释放呈平行且剂量依赖性增加,并产生相似的最大GH分泌量。大鼠GRF刺激GH释放的效力比所有其他GRF高3至6倍,而人、牛/羊、猪和羊GRF的效力在统计学上无差异。与分别与人GRF(1-27)NH2和人GRF(1-23)NH2相比,大鼠GRF(1-27)NH2和大鼠GRF(1-23)NH2效力的增加表明,该分子效力的增加在于天然GRF氨基末端的结构差异。结果表明大鼠垂体细胞对其同源释放因子的敏感性增加。