Characterization of hatching-associated changes in the sea urchin fertilization envelope.
The embryo of the sea urchin Strongylocentrotus purpuratus hatches from the fertilization envelope (FE) via synthesis and secretion of a hatching enzyme and by ciliary activity. Although the basic characteristics of the hatching enzyme are known, little is understood about changes in the FE during hatching. We have studied the biochemical changes in FEs during hatching. Polyacrylamide gel analysis revealed an increasingly complex polypeptide spectrum of the extractable fraction of FEs isolated during development. Immunoblotting of these polypeptides (using antiserum against the soluble polypeptides extracted from FEs isolated at 30 minutes postinsemination) revealed a decrease in the soluble FE components during hatching. Immunochemical analysis of hatching medium showed a strong correlation between the soluble FE components released and the hatching interval. Immunoblotting of hatching media indicated the presence of soluble FE polypeptides of similar and lower molecular weights than those obtained for extracts of FEs. These results imply that the hatching-associated changes in the FE of S purpuratus occur via proteolysis of FE components, which are derived from the paracrystalline protein fraction, a subset of cortical granule proteins.
D000818:Animals; D005306:Fertilization; D007118:Immunoassay; D008565:Membrane Proteins / Q000032:analysis; D010455:Peptides / Q000032:analysis; D010544:Peroxidases / Q000032:analysis; D011817:Rabbits; D012617:Sea Urchins / Q000196:embryology* / Q000201:enzymology
D008565:Membrane Proteins; D010455:Peptides; D010544:Peroxidases