Evidence for the existence of two assembly domains within the sea urchin fertilization envelope

Nancy M. Mozingo, Douglas E. Chandler

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

The sea urchin fertilization envelope (FE) is a complex, macromolecular aggregate assembled by the addition of cortical granule secretions to the vitelline layer. The completed, trilaminar structure has a dense layer sandwiched between surface coats of paracrystalline material. Two cortical granule enzymes, ovoperoxidase and protease, and a cell surface transglutaminase are required for the assembly process. We have examined, by quick-freeze, deep-etch, rotary-shadow electron microscopy, the effects of inhibiting each of these enzymes upon FE assembly. These experiments reveal two domains within the FE, distinguishable by their enzymatic requirements for proper maturation. The first domain consists of the microvillar casts which require both protease and transglutaminase activities to obtain a normal paracrystalline coat. The second domain comprises the regions between casts and appears to mature by ovoperoxidase-mediated cross-linking of paracrystalline material to the envelope.

Original languageEnglish (US)
Pages (from-to)148-157
Number of pages10
JournalDevelopmental Biology
Volume146
Issue number1
DOIs
StatePublished - Jul 1991

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ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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