Cell surface proteins of whole Xenopus embryos identified by radioiodination

Judith Litvin, Mary Lou King

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

We have examined the proteins of Xenopus whole oocytes and embryos that are accessible to surface iodination. These cell surface proteins appear to undergo stagespecific modulation during development. The most pronounced changes were observed between oocytes and the 32-cell stage when the number of labelled proteins doubled, and between early and late gastrula when the complexity declined by two thirds. The simplification of the pattern during gastrulation may reflect changes in cell position as endodermal cells move inside leaving ectodermal cells at the external surface. The lectin binding patterns for NP-40 solubilized proteins extracted from oocytes and embryos also changed in a stage-dependent manner. Con A and WGA recognized a complex pattern of glycoproteins containing glucose and mannose residues. In contrast, SAB and RCA binding to galactose residues recognized far fewer glycoproteins. Many of the observed changes occurred during cleavage stages before embryonic gene transcription is initiated and may be due to post-translational modifications.

Original languageEnglish (US)
Pages (from-to)141-147
Number of pages7
JournalRoux's Archives of Developmental Biology
Volume198
Issue number3
DOIs
StatePublished - Oct 1 1989

Keywords

  • Cell surface
  • Embryos
  • Glycoproteins
  • Xenopus Oocytes

ASJC Scopus subject areas

  • Developmental Biology

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