King B F, Blankenship T N
Department of Cell Biology and Human Anatomy, School of Medicine, University of California, Davis 95616, USA.
Microsc Res Tech. 1997;38(1-2):42-51. doi: 10.1002/(SICI)1097-0029(19970701/15)38:1/2<42::AID-JEMT6>3.0.CO;2-W.
The objective of this study was to examine the developmental appearance of the extracellular matrix glycoprotein fibrillin in macaque placentas and fetal membranes and to compare this distribution to that seen in term human placentas and fetal membranes. Standard immunoperoxidase methods were used on paraformaldehyde-fixed, paraffin-embedded tissues. At early gestational ages (26-30 days), fibrillin was found in cell columns and cytotrophoblastic shell, with weak staining in the villous stroma. Staining was abundant in the shell and columns at 53 days as well, and stronger staining was seen in the stroma of the chorionic plate and stem villi. Staining in the shell and remnants of the cell columns in later gestation continued to be positive, though variable. Generally, the strongest staining was present in the distal cytotrophoblastic shell. Stroma in the tips of anchoring villi was also strongly positive. Later in gestation, fibrillin was observed around the multilayered cytotrophoblast of the chorionic plate. Fibrillin was abundant in the stromal cores of human term placental villi. In early macaque amnion, fibrillin staining was abundant in a layer beneath the amniotic epithelium. Later in gestation, macaque chorioamnion staining was generally similar to human term chorioamnion staining, with the heaviest staining in portions of the compact and reticular layers. Fibrillin was sometimes localized in regions known to be rich in connective tissue microfibrils, but, in other regions known to have abundant microfibrils, fibrillin staining was weak. This suggests that some microfibrils in placenta may be composed predominantly of some other protein(s). The function of fibrillin in the various placental compartments is unknown at present. It may provide attachment points for cells while at the same time providing a strong, yet flexible, matrix to accommodate growth particularly in areas subject to shear stress.
本研究的目的是检查猕猴胎盘和胎膜中细胞外基质糖蛋白原纤维蛋白的发育情况,并将这种分布与足月人类胎盘和胎膜中的分布进行比较。对经多聚甲醛固定、石蜡包埋的组织采用标准免疫过氧化物酶方法。在妊娠早期(26 - 30天),原纤维蛋白存在于细胞柱和细胞滋养层壳中,绒毛基质染色较弱。在53天时,壳和细胞柱中的染色也很丰富,在绒毛膜板和主干绒毛的基质中可见更强的染色。妊娠后期,壳和细胞柱残余物中的染色仍为阳性,但存在差异。一般来说,最强的染色出现在远端细胞滋养层壳中。固定绒毛尖端的基质也呈强阳性。妊娠后期,在绒毛膜板的多层细胞滋养层周围观察到原纤维蛋白。足月人类胎盘绒毛的基质核心中原纤维蛋白丰富。在猕猴羊膜早期,原纤维蛋白染色在羊膜上皮下方的一层中丰富。妊娠后期,猕猴绒毛膜羊膜染色通常与足月人类绒毛膜羊膜染色相似,致密层和网状层部分染色最重。原纤维蛋白有时定位于已知富含结缔组织微原纤维的区域,但在其他已知有丰富微原纤维的区域,原纤维蛋白染色较弱。这表明胎盘中的一些微原纤维可能主要由其他某种蛋白质组成。目前尚不清楚原纤维蛋白在胎盘各部分中的功能。它可能为细胞提供附着点,同时提供一个坚固但灵活的基质,以适应生长,特别是在承受剪切力的区域。