There are striking similiarities present between the behavior of invasive placentaL cells and that of invasive cancer cells. Matrix metalloproteinases (MMPs) are one of the most important mediators. MMP-28, the new me...There are striking similiarities present between the behavior of invasive placentaL cells and that of invasive cancer cells. Matrix metalloproteinases (MMPs) are one of the most important mediators. MMP-28, the new member of MMPs, was sequenced and identified recently. Expression of MMP-28 mRNA and protein in the cytotrophoblast cells and a choriocarcinoma cell line, JEG-3 cell, was conducted by zymography, RT-PCR and Northern blot. There is MMP-28 mRNA expression in both the cytotrophoblast cells and JEG-3 cells by RT-PCR. The activity of MMP-28 in cytotrophoblast cells was significantly weaker than that in JEG-3 (P 【 0.01) by zymography. Furthermore, mRNA expression of MMP-28 was significantly stronger (P 【 0.001) in JEG-3 than in human cytotrophoblast cells in a time-dependent way by Northern Blot. Our results suggest that MMP-28 may play a role in some of the tissue-remodeling events associated with normal pregnancy and tumor progression.展开更多
NUCC-3 choriocarcinoma cell line was used as an in vitro placental cell model to investigate the effects of follistatin on GnRH-stimulated hCG secretion and its subunit mRNA level and stability. Follistatin alone did ...NUCC-3 choriocarcinoma cell line was used as an in vitro placental cell model to investigate the effects of follistatin on GnRH-stimulated hCG secretion and its subunit mRNA level and stability. Follistatin alone did not affect basal hCG secretion and its subunit mRNA level. GnRH increased hCG secretion and hCG β-mRNA level in a dose-dependent manner. Follistatin significantly suppressed GnRH-stimulated hCG secretion and hCG α- and β-mRNA level. It inhibited hCG secretion in response to PMA, and did not affect the stability of hCG α- and β-mRNA. The authors suggest that follistatin inhibits GnRH-stimulated hCG secretion as well as hCG α- and β-RNA level by decreasing the rate of transcription through the second messenger transduction system--protein kinase-C.展开更多
基金This work was supported by the Special Funds for the Major State Basic Research Project (Grant No. G1999055903)the Climbing Project of China (Grant No. 970211019-3)the Hundred-Scientist-Program of the Chinese Academy of Sciences.
文摘There are striking similiarities present between the behavior of invasive placentaL cells and that of invasive cancer cells. Matrix metalloproteinases (MMPs) are one of the most important mediators. MMP-28, the new member of MMPs, was sequenced and identified recently. Expression of MMP-28 mRNA and protein in the cytotrophoblast cells and a choriocarcinoma cell line, JEG-3 cell, was conducted by zymography, RT-PCR and Northern blot. There is MMP-28 mRNA expression in both the cytotrophoblast cells and JEG-3 cells by RT-PCR. The activity of MMP-28 in cytotrophoblast cells was significantly weaker than that in JEG-3 (P 【 0.01) by zymography. Furthermore, mRNA expression of MMP-28 was significantly stronger (P 【 0.001) in JEG-3 than in human cytotrophoblast cells in a time-dependent way by Northern Blot. Our results suggest that MMP-28 may play a role in some of the tissue-remodeling events associated with normal pregnancy and tumor progression.
文摘NUCC-3 choriocarcinoma cell line was used as an in vitro placental cell model to investigate the effects of follistatin on GnRH-stimulated hCG secretion and its subunit mRNA level and stability. Follistatin alone did not affect basal hCG secretion and its subunit mRNA level. GnRH increased hCG secretion and hCG β-mRNA level in a dose-dependent manner. Follistatin significantly suppressed GnRH-stimulated hCG secretion and hCG α- and β-mRNA level. It inhibited hCG secretion in response to PMA, and did not affect the stability of hCG α- and β-mRNA. The authors suggest that follistatin inhibits GnRH-stimulated hCG secretion as well as hCG α- and β-RNA level by decreasing the rate of transcription through the second messenger transduction system--protein kinase-C.
