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 language | English |
|---|---|
| Pages (from-to) | 141-147 |
| Number of pages | 7 |
| Journal | Roux's Archives of Developmental Biology |
| Volume | 198 |
| Issue number | 3 |
| DOIs | |
| State | Published - Oct 1 1989 |
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Keywords
- Cell surface
- Embryos
- Glycoproteins
- Xenopus Oocytes
ASJC Scopus subject areas
- Developmental Biology
Cite this
Cell surface proteins of whole Xenopus embryos identified by radioiodination. / Litvin, Judith; King, Mary Lou L.
In: Roux's Archives of Developmental Biology, Vol. 198, No. 3, 01.10.1989, p. 141-147.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cell surface proteins of whole Xenopus embryos identified by radioiodination
AU - Litvin, Judith
AU - King, Mary Lou L
PY - 1989/10/1
Y1 - 1989/10/1
N2 - 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.
AB - 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.
KW - Cell surface
KW - Embryos
KW - Glycoproteins
KW - Xenopus Oocytes
UR - http://www.scopus.com/inward/record.url?scp=0024465738&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024465738&partnerID=8YFLogxK
U2 - 10.1007/BF02438939
DO - 10.1007/BF02438939
M3 - Article
AN - SCOPUS:0024465738
VL - 198
SP - 141
EP - 147
JO - Development Genes and Evolution
JF - Development Genes and Evolution
SN - 0949-944X
IS - 3
ER -