Functional characterization of toposomes from sea urchin blastula embryos by a morphogenetic cell aggregation assay.
This paper documents the evidence that the large oligomeric glycoprotein complexes of unknown function first isolated as 22S particles from sea urchin embryos are the sole agents responsible for the adhesive integrity of sea urchin blastula embryos. The conclusion rests on the demonstration that polyclonal IgG (as serum or monovalent Fab) against whole membranes or butanol-solubilized components of membranes, as well as against the purified particle itself, completely blocks reaggregation of dissociated blastula cells and that this inhibition is reversed by neutralization of the inhibitory antibodies with purified 22S antigen. An essential aspect of the evidence is the combination of quantitative endpoint titrations in microtiter wells with the qualitative parameters of morphogenesis. The new data complement previous evidence that morphogenesis is mediated by a general class of particles, toposomes, responsible for mechanical linkage between cells and their positional guidance in embryogenesis.
D000818:Animals; D001755:Blastocyst / Q000166:cytology / Q000648:ultrastructure; D002449:Cell Aggregation; D004625:Embryo, Nonmammalian / Q000166:cytology* / Q000648:ultrastructure; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D008854:Microscopy, Electron; D012617:Sea Urchins / Q000196:embryology*
D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G