Department of Clinical Biochemistry, Laboratory Medicine, Birmingham Heartlands Hospital, Bordesley Green East, Birmingham B9 5SS, UK.
Reprod Biol Endocrinol. 2011 May 15;9:64. doi: 10.1186/1477-7827-9-64.
Placental hCG and pitutary LH transduce signals in target tissues through a common receptor (LHCGR). We demonstrate that recombinant LHCGR proteins which include the hormone-binding domain are secreted from transfected cells and that natural LHCGR is also secreted from human placental explants. LHCGR recombinant proteins representing varying lengths of the N-terminal extracellular domain were expressed in Chinese Hamster Ovary cells in suspension culture. Secretion was minimal up to 72h but by 96h 24-37% of the LHCGR had been released into the culture medium. The secreted proteins were folded and sensitive to glycosidases suggesting N-linked glycosylation. Secretion was independent of recombinant size and was mediated via structurally defined membrane vesicles (50-150nm). Similarly cultured human early pregnancy placental explants also released LHCGR via microvesicles. These studies provide the first experimental evidence of the possible mechanistic basis of the secretion of LHCGR.
胎盘 hCG 和垂体 LH 通过共同受体 (LHCGR) 在靶组织中传递信号。我们证明,包含激素结合域的重组 LHCGR 蛋白可从转染细胞中分泌出来,并且天然 LHCGR 也可从人胎盘外植体中分泌出来。在悬浮培养的中国仓鼠卵巢细胞中表达了代表不同长度的 N 端细胞外结构域的 LHCGR 重组蛋白。分泌量在 72 小时内最小,但在 96 小时时,24-37%的 LHCGR 已释放到培养基中。分泌的蛋白质是折叠的,并且对糖苷酶敏感,表明存在 N 连接的糖基化。分泌是不依赖于重组大小的,并通过结构定义的膜泡(50-150nm)介导。同样在培养的人类早孕胎盘外植体中也通过微泡释放 LHCGR。这些研究为 LHCGR 分泌的可能机制基础提供了第一个实验证据。