Chanat E, Hubert J F, De Monti M, Guiraud J M, Duval J
Ann Endocrinol (Paris). 1986;47(1):45-7.
Protein secretion by cultured pituitary cells from 14 day-old female rats was estimated using [35S]-méthionine incorporation, electrophoresis and autoradiography. Stimulation by LHRH promoted biosynthesis and fast release of a protein of apparent molecular weight 87,000 daltons and pI 4.6. Gonadotrophs enriched by centrifugal elutriation were particularly rich in this polypeptide which was thus called GP-87 (Gonadotrope polypeptide). Cells were then cultured with [32P]-orthophosphate and proteins were analyzed. Our first results tend to show that GP-87 is phosphorylated, at least in the cells. We suggest that this specific protein, the secretion of which is correlated with LH release, participates to the response mechanisms of gonadotrope cells stimulated by LHRH.
利用[35S] - 甲硫氨酸掺入、电泳和放射自显影技术，对14日龄雌性大鼠培养的垂体细胞的蛋白质分泌进行了评估。促黄体生成素释放激素（LHRH）刺激促进了一种表观分子量为87,000道尔顿、等电点为4.6的蛋白质的生物合成和快速释放。通过离心淘析富集的促性腺激素细胞中这种多肽特别丰富，因此将其称为GP - 87（促性腺激素细胞多肽）。然后用[32P] - 正磷酸盐培养细胞并分析蛋白质。我们的初步结果倾向于表明，GP - 87至少在细胞中被磷酸化。我们认为这种特定蛋白质的分泌与促黄体生成素（LH）释放相关，参与了促性腺激素细胞受LHRH刺激的反应机制。
