| Literature DB >> 3865216 |
H Noll, V Matranga, M Cervello, T Humphreys, B Kuwasaki, D Adelson.
Abstract
Cell adhesion in the sea urchin blastula is mediated by a 22S genus-specific glycoprotein complex consisting initially of six 160-kDa subunits that are processed proteolytically as development proceeds. Noncytolytic removal of the 22S particle from the surface with either 2.5% butanol or trypsin renders dissociated cells reaggregation incompetent, and addition restores reaggregation and development. Polyclonal antibodies against the 22S complex prevent reaggregation in a genus-specific manner while monoclonal antibodies stain cell surface structures in a pattern consistent with a code that specifies the position of a cell in the embryo by a unique combination of subunits in its cell adhesion particles. The existence of similar particles in Drosophila and amphibian embryos suggests that these glycoprotein complexes are a general class of organelles, the toposomes, that in the embryo mediate cell adhesion and express positional information.Entities:
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Year: 1985 PMID: 3865216 PMCID: PMC391442 DOI: 10.1073/pnas.82.23.8062
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205