Cell adhesion and migration in the early vertebrate embryo: location and possible role of the putative fibronectin receptor complex
Open Access
- 1 January 1986
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 102 (1), 160-178
- https://doi.org/10.1083/jcb.102.1.160
Abstract
Using a combined in vivo and in vitro approach, we have analyzed the immunofluorescent localization and function of a 140,000-mol-wt glycoprotein complex implicated in cell adhesion to fibronectin (FN), with particular emphasis on neural crest cell adhesion and migration. This putative fibronectin receptor complex (FN-receptor) was detectable in almost all tissues derived from each of the three primary germ layers. It was present in both mesenchymal and epithelial cells, and was particularly enriched at sites close to concentrations of FN, e.g., at the basal surfaces of epithelial cells. It was also present on neural crest cells. The distribution and function of this putative receptor was then analyzed on individual cells in vitro. It was diffusely organized on highly locomotory neural crest cells and somitic fibroblasts. Both motile cell types also displayed relatively low numbers of focal contacts and microfilament bundles and limited amounts of localized vinculin, alpha-actinin, and endogenous FN. In contrast, the FN-receptor in stationary embryonic cells, i.e., somitic cells after long-term culture or ectodermal cells, existed in characteristic linear patterns generally co-distributed with alpha-actinin and fibers of endogenous FN. Anti-FN-receptor antibodies inhibited the adhesion to FN of motile embryonic cells, but not of stationary fibroblasts. However, these same antibodies adsorbed to substrata readily mediated adhesion and spreading of cells, but were much less effective for cell migration. Our results demonstrate a widespread occurrence in vivo of the putative FN-receptor, with high concentrations near FN. Embryonic cell migration was associated with a diffuse organization of this putative receptor on the cell surface in presumably labile adhesions, whereas stationary cells were anchored to the substratum at specific sites linked to the cytoskeleton near local concentrations of FN-receptor.This publication has 64 references indexed in Scilit:
- Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectinCell, 1980
- The behaviour of fibroblasts migrating from chick heart explants: changes in adhesion, locomotion and growth, and in the distribution of actomyosin and fibronectinJournal of Cell Science, 1979
- Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.Proceedings of the National Academy of Sciences, 1979
- Cell-to-substratum contacts in living cells: A direct correlation between interference-reflexion and indirect-immunofluorescence microscopy using antibodies against actin and A-actininJournal of Cell Science, 1979
- The fibronexus: a transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblastsCell, 1979
- Relationships between fibronectin (LETS protein) and actinCell, 1978
- TRANSMEMBRANE LINKAGE OF FIBRONECTIN TO INTRACELLULAR ACTIN‐CONTAINING FILAMENTS IN CULTURED HUMAN FIBROBLASTS*Annals of the New York Academy of Sciences, 1978
- Adhesion among neural cells of the chick embryo. I. An immunological assay for molecules involved in cell-cell binding.Journal of Biological Chemistry, 1977
- Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface proteinCell, 1977
- Microfilament bundles and cell shape are related to adhesiveness to substratum and are dissociable from growth control in cultured fibroblastsCell, 1977