Characterization of laminin isoforms in human amnion

Seiji Takashima, Masanori Yasuo, Noriko Sanzen, Kiyotoshi Sekiguchi, Motonori Okabe, Toshiko Yoshida, Ayaka Toda, Toshio Nikaido*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Epithelial cells of the human amnion have been reported to possess similar functions to many types of cells, such as hepatocytes, neurons, and pancreatic β-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 α-, a β-, and a γ-chain, and each type of chain has several types of subunit chains: α1-5, β1-3, and γ1-3. 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.

Original languageEnglish
Pages (from-to)75-81
Number of pages7
JournalTissue and Cell
Volume40
Issue number2
DOIs
StatePublished - 2008/04

Keywords

  • Amnion
  • Basement membrane
  • Laminin
  • Stem cell

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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