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Confocal and conventional immunofluorescence and ultrastructural localisation of intracellular strength-giving components of human amniochorion

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • C Ockleford
  • T Malak
  • A Hubbard
  • K Bracken
  • S A Burton
  • N Bright
  • G Blakey
  • J Goodliffe
  • D Garrod
  • C d'Lacey
<mark>Journal publication date</mark>12/1993
<mark>Journal</mark>Journal of Anatomy
Volume183 ( Pt 3)
Number of pages23
Pages (from-to)483-505
Publication StatusPublished
<mark>Original language</mark>English
Externally publishedYes


Key cytoskeletal polypeptides of human fetal membranes have been localised at subcellular level using confocal and conventional indirect immunofluorescence microscopy. Correlation with electron microscope data has allowed us to examine how cellular compartments of this multilaminar tissue maintain their mechanical integrity until the time of membrane rupture at parturition. Evidence is presented for myofibroblastic characteristics of cells in both the fibroblast and reticular layers which may therefore have tension-generating, position-adjustment and wound-healing roles in the amniochorion. Desmin and vimentin are coexpressed in these cells, but a small localised population of cells in the fibroblast layer contains vimentin alone. An interaction of cytokeratin filaments with nuclei and desmosomes of amniotic epithelium in vivo is demonstrated, indicating that nuclei of cells of ectodermal origin are integrated into a mechanical structure extending throughout the tissue as a whole. Cells of the basal 1 or 2 layers of trophoblast have been shown to have a more extensive and better integrated cytoskeletal organisation than those overlying and forming the boundary with decidua. Structures within the trophoblast, identified previously as degenerate villi, contain cells with intermediate filaments with similar immunofluorescence properties to those of the neighbouring reticular layer and thus may represent papillae that prevent shearing at this interface.