Characterization of laminin isoforms in human amnion

Characterization of laminin isoforms in human amnion
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DOI:
10.1016/j.tice.2007.09.001
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发表时间:
2008-04-01
期刊:
影响因子:
2.6
通讯作者:
Nikaido, Toshio
Nikaido, Toshio
中科院分区:
生物学4区
文献类型:
--
作者:
Takashima, Seiji;Yasuo, Masanori;Nikaido, Toshio

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人羊膜上皮细胞具有与肝细胞、神经元、胰腺P细胞等多种细胞相似的功能。我们以前曾报道,人羊膜上皮细胞的肝细胞样功能之一因基底膜成分的存在而增强。层粘连蛋白是基底膜的主要成分之一,对细胞分化起着至关重要的作用。层粘连蛋白有几种由α、β和伽马链组成的杂三聚体亚型,每种类型的链都有几种类型的亚单位链:α1-5、α1-3和γ1-3。在这项研究中,我们描述了人羊膜中层粘连蛋白亚单位链。层粘连蛋白是由相邻的人羊膜上皮细胞产生和分泌层粘连蛋白,因此采用RT-PCR方法研究了层粘连蛋白亚单位链基因在人羊膜上皮细胞中的表达。冰冻切片免疫组织化学染色检测它们的定位。结果表明,人羊膜基底膜含有广泛的层粘连蛋白亚型,层粘连蛋白-2、-4、-5、-6、-7、-10、-11。这些发现不仅将为理解羊膜和hAECs的生理作用提供线索,也将为将该组织用作细胞移植治疗的供体细胞来源提供线索。(C)2007年由爱思唯尔有限公司出版。
Epithelial cells of the human amnion have been reported to possess similar functions to many types of cells, such as hepatocytes, neurons, and pancreatic P-cells. We reported previously that one of the hepatocyte-like functions of human amniotic epithelial cells was reinforced by the presence of basement membrane components. Laminin is one of the main components of the basement membrane; it critically contributes to cell differentiation. Laminin has several heterotrimer isoforms composed of an alpha, a beta-, and a gamma-chain, and each type of chain has several types of subunit chains: alpha 1-5, alpha 1-3, and gamma 1-3. In this study, we characterized the laminin subunit chains in human amnion. Laminin is produced and secreted from adjacent epithelial cells, and therefore, the gene expression of laminin subunit chains in human amniotic epithelial cells was investigated by RT-PCR. Their localization was examined by immunohistochemical staining of frozen sections. The findings suggested that the basement membrane of the human amnion contains a broad spectrum of laminin isoforms, laminin-2, -4, -5, -6, -7, - 10, -11. These findings will provide clues not only for understanding the physiological roles of the amnion and hAECs, but also for applying this tissue as a source of donor cells for cell transplantation therapy. (C) 2007 Published by Elsevier Ltd.