Human chorionic gonadotrophin (HCG) and free alpha subunit secreted by cultured human choriocarcinoma (JEG-3) cells.

Placenta. Supplement Pub Date : 1981-01-01
R Benveniste, A Scommegna
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Abstract

The cultured human choriocarcinoma JEG-3 cells secrete biologically active HCG and free HCG alpha-subunit. When compared with the alpha-subunit dissociated from HCG obtained either from pregnancy urine or JEG-3 cells, free alpha-subunit has a larger molecular weight, is more acidic and is non-functional, lacking the property to recombine with the HCG beta-subunit. The understanding of the biochemical differences observed between free alpha-subunit and alpha-subunit found in HCG is important and should help to unravel the biosynthesis of gonadotrophins. Two proteins which bind to the cell membrane, epidermal growth factor and concanavalin A, are capable of stimulating JEG-3 cell secretion. Epidermal growth factor stimulates the secretion of HCG while concanavalin A stimulates both HCG and HCG alpha-subunit secretion. Amphotericin B, an antifungal agent commonly used in tissue cultures, which also affects the cell membrane, was shown to stimulate HCG and HCG alpha-subunit secretions. The use of these agents should contribute to the understanding of membrane-related events which lead to the secretion of HCG and alpha-subunit.

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培养的人绒毛膜癌细胞分泌的人绒毛膜促性腺激素(HCG)和游离α亚基。
培养的人绒毛膜癌JEG-3细胞分泌具有生物活性的HCG和游离HCG α亚基。与从妊娠尿液或JEG-3细胞中获得的HCG解离的α -亚基相比,游离α -亚基分子量更大,酸性更强,无功能,缺乏与HCG -亚基重组的特性。了解在HCG中发现的游离α亚基和α亚基之间观察到的生化差异是重要的,并且应该有助于揭示促性腺激素的生物合成。结合细胞膜的两种蛋白,表皮生长因子和刀豆蛋白A,能够刺激JEG-3细胞的分泌。表皮生长因子刺激HCG的分泌,而豆豆蛋白A同时刺激HCG和HCG α亚基的分泌。两性霉素B是一种抗真菌剂,通常用于组织培养,它也会影响细胞膜,被证明可以刺激HCG和HCG α -亚基分泌。这些药物的使用应该有助于理解导致HCG和α -亚基分泌的膜相关事件。
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HLA and the generation of diversity in human pregnancy. Pregnancy proteins and activation of the complement system. The development of a murine model for the study of human pregnancy zone protein (PZP, alpha 2-PAG) and pregnancy-specific beta 1-glycoprotein (SP-1, PS beta G). New soluble placental tissue proteins: their isolation, characterization, localization and quantification. Observations on the function of pregnancy-associated plasma protein A.
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