These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Structure, assembly and function of the surface envelope (fertilization envelope) from eggs of the sea urchin, Strongylocentrotus purpuratus.
    Author: Carroll EJ, Acevedo-Duncan M, Justice RW, Santiago L.
    Journal: Adv Exp Med Biol; 1986; 207():261-91. PubMed ID: 3548240.
    Abstract:
    The sea urchin fertilization envelope (FE) is formed following initial sperm-egg interaction from the egg surface vitelline envelope (VE) and the paracrystalline protein fraction (PCF), derived from cortical granules. Although mature FEs are physicochemically hardened postinsemination, a major protein fraction consisting of seven major polypeptides was extracted from Strongylocentrotus purpuratus FEs and the major, separated components were immunologically cross-reactive with the principal polypeptides in PCF and isolated cortical granules. Antibodies prepared against extracted, core FEs were immunologically crossreactive with isolated VEs, but not with PCF, suggesting that only VE components are covalently crosslinked. Based on protease inhibitor experiments, our model of FE development is that a benzamidine-sensitive, cortical granule protease cleaves a 200 kD VE polypeptide during initial envelope elevation to set up the morphological change in FE papillae which occurs later. Divalent cations precipitate the PCF and form metal proteinate bridges between the VE and PCF. Based on peroxidase inhibitor experiments, we suggest that the cortical granule peroxidase crosslinks VE polypeptides, beginning at 2-3 min postinsemination, to restrict the permeability of the VE so that normal envelope thickening occurs. A 305 kD VE polypeptide was isolated and appears to be important in sperm-egg interaction based on inhibition of sperm binding and fertilization by antibodies against the purified polypeptide.
    [Abstract] [Full Text] [Related] [New Search]