4.2 Article

Hyalin is a cell adhesion molecule involved in mediating archenteron-blastocoel roof attachment

Journal

ACTA HISTOCHEMICA
Volume 110, Issue 4, Pages 265-275

Publisher

ELSEVIER GMBH
DOI: 10.1016/j.acthis.2007.11.004

Keywords

hyalin; sea urchin embryo; blastocoel roof-archenteron tip interaction; specific cell adhesion molecule

Categories

Funding

  1. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [S06GM048680] Funding Source: NIH RePORTER
  2. NIGMS NIH HHS [S06 GM048680-140011] Funding Source: Medline
  3. PHS HHS [S0648680] Funding Source: Medline

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The US National Institutes of Health has designated the sea urchin embryo as a model organism because around 25 discoveries in this system have led to insights into the physiology of higher organisms, including humans. Hyalin is a large glycoprotein in the hyaline Layer of sea urchin embryos that functions to maintain general. adhesive relationships in the developing embryo. It consists of the hyalin repeat domain that has been identified in organisms as diverse as bacteria, worms, flies, mice, sea urchins and humans. Here we show, using a polyclonal antibody raised against the 11.6 S species of hyalin, that it localizes at the tip of the archenteron and on the roof of the blastocoel exactly where these two structures bond in an adhesive interaction that has been of interest for over a century. In addition, the antibody blocks the interaction between the archenteron tip and blastocoel roof. These results, in addition to other recent findings from this Laboratory that will. be discussed, suggest that hyalin is involved in mediating this cellular interaction. This is the first demonstration that suggests that hyalin functions as a cell adhesion molecule in many organisms, including humans. (C) 2007 Elsevier GmbH. All rights reserved.

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