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Expression of adhesion molecules during the formation and differentiation of the avian endocardial cushion tissue

Academic Article
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Overview

authors

  • Crossin, Kathryn
  • Hoffman, S.

publication date

  • June 1991

journal

  • Developmental Biology  Journal

abstract

  • The expression of cytotactin, the cytotactin-binding (CTB) proteoglycan, and the neural cell adhesion molecule, N-CAM, was examined during the development of the avian endocardial cushion tissue (ECT). N-CAM was present in the cardiac mesoderm from its earliest time of development. At the time when endothelial cells converted to mesenchyme and began to migrate, they ceased their expression of N-CAM. Cytotactin and CTB proteoglycan were present in the cardiac jelly (into which the ECT cells migrate) in patterns that were correlated with cell migration. At early times of migration (stage 18), the region of the cardiac jelly near the endocardium contained cytotactin in the vicinity of the migrating cells. During later migration (stage 22), cytotactin remained associated with the leading zone of cell migration, but its expression began to decrease in areas where cells had accumulated. After ECT cell migration had ceased, cytotactin expression decreased, remaining high only in the peripheral portion of the aorticopulmonary septum and absent from its ridges. CTB proteoglycan was expressed during early migration at high levels in and adjacent to the myocardium. By stage 22, its distribution had become more uniform throughout the ECT regions and in the myocardium. The combined results of this study suggest that cytotactin, CTB proteoglycan, and N-CAM each play a distinct, critical role in pattern formation in the early heart.

subject areas

  • Animals
  • Carrier Proteins
  • Cell Adhesion Molecules, Neuronal
  • Cell Differentiation
  • Cell Movement
  • Chick Embryo
  • Endocardium
  • Extracellular Matrix Proteins
  • Gene Expression
  • Heart
  • Membrane Glycoproteins
  • Microscopy, Phase-Contrast
  • Myocardium
  • Proteoglycans
  • Tenascin
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Identity

International Standard Serial Number (ISSN)

  • 0012-1606

Digital Object Identifier (DOI)

  • 10.1016/0012-1606(91)90126-n

PubMed ID

  • 1710192
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Additional Document Info

start page

  • 277

end page

  • 286

volume

  • 145

issue

  • 2

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