Fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells.
Open Access
- 1 October 1988
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 107 (4) , 1385-1396
- https://doi.org/10.1083/jcb.107.4.1385
Abstract
The dynamic process of embryonic cell motility was investigated by analyzing the lateral mobility of the fibronectin receptor in various locomotory or stationary avian embryonic cells, using the technique of fluorescence recovery after photobleaching. The lateral mobility of fibronectin receptors, labeled by a monoclonal antibody, was defined by the diffusion coefficient and mobile fraction of these receptors. Even though the lateral diffusion coefficient did not vary appreciable (2 .times. 10-10 cm2/s .ltoreq. D .ltoreq. 4 .times. 10-10 cm2/s) with the locomotory state and the cell type, the mobile fraction was highly dependent on the degree of cell motility. In locomoting cells, the population of fibronectin receptors, which was uniformly distributed on the cell surface, displayed a high mobile fraction of 66 .+-. 19% at 25.degree.C (82 .+-. 14% at 37.degree.C). In contrast, in nonmotile cells, the population of receptors was concentrated in focal contacts and fibrillar streaks associated with microfilament bundles and, in these sites, the mobile fraction was small (16 .+-. 8%). When cells were in a stage intermediate between highly motile and stationary, the population of fibronectin receptors was distributed both in focal contacts with a small mobile fraction and in a diffuse pattern with a reduced mobile fraction (33 .+-. 9%) relative to the diffuse population in highly locomotory cells. The mobile fraction of the fibronectin receptor was found to be temperature dependent in locomoting but not in stationary cells. The mobile fraction could be modulated by affecting the interaction between the receptor and the substratum. The strength of this interaction could be increased by growing cells on a substratum coated with polyclonal antibodies to the receptor. This caused the mobile fraction to decrease. The interaction could be decreased by using a probe, monoclonal antibodies to the receptor known to perturb the adhesion of certain cell types which caused the mobile fraction to increase. From these results, we conclude that in locomoting embryonic cells, most fibronectin receptors can readily diffuse in the plane of the membrane. This degree of lateral mobility may be correlated to the labile adhesions to the substratum presumably required for high motility. In contrast, fibronectin receptors in stationary cells are immobilized in focal contacts and fibrillar streaks which are in close association with both extracellular and cytoskeletal structures; these stable complexes appear to provide firm anchorage to the substratum.This publication has 57 references indexed in Scilit:
- Alterations in neural crest migration by a monoclonal antibody that affects cell adhesion.The Journal of cell biology, 1985
- Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture.The Journal of cell biology, 1985
- The interaction of plasma fibronectin with fibroblastic cells in suspension.Journal of Biological Chemistry, 1985
- Development of cell surface linkage complexes in cultured fibroblasts.The Journal of cell biology, 1985
- A monoclonal antibody identifies a glycoprotein complex involved in cell-substratum adhesionExperimental Cell Research, 1985
- Tension in the culture dish: Microfilament organization and migratory behavior of quail neural crest cellsCell Motility, 1985
- Characterization of a membrane‐associated glycoprotein complex implicated in cell adhesion to fibronectinJournal of Cellular Biochemistry, 1985
- Mechanisms of cell migration in the vertebrate embryoCell Differentiation, 1984
- Lateral diffusion of an 80,000-dalton glycoprotein in the plasma membrane of murine fibroblasts: relationships to cell structure and function.The Journal of cell biology, 1984
- Cell migrations in embryosCell, 1984