Literature DB >> 2971668

Fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells.

J L Duband1, G H Nuckolls, A Ishihara, T Hasegawa, K M Yamada, J P Thiery, K Jacobson.   

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 appreciably (2 X 10(-10) cm2/S less than or equal to D less than or equal to 4 X 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 degrees C (82 +/- 14% at 37 degrees 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.

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Year:  1988        PMID: 2971668      PMCID: PMC2115255          DOI: 10.1083/jcb.107.4.1385

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  57 in total

1.  A monoclonal antibody identifies a glycoprotein complex involved in cell-substratum adhesion.

Authors:  K A Knudsen; A F Horwitz; C A Buck
Journal:  Exp Cell Res       Date:  1985-03       Impact factor: 3.905

2.  The interaction of plasma fibronectin with fibroblastic cells in suspension.

Authors:  S K Akiyama; K M Yamada
Journal:  J Biol Chem       Date:  1985-04-10       Impact factor: 5.157

3.  Tension in the culture dish: microfilament organization and migratory behavior of quail neural crest cells.

Authors:  R P Tucker; B F Edwards; C A Erickson
Journal:  Cell Motil       Date:  1985

4.  Cell migrations in embryos.

Authors:  N M Le Douarin
Journal:  Cell       Date:  1984-09       Impact factor: 41.582

5.  Characterization of a membrane-associated glycoprotein complex implicated in cell adhesion to fibronectin.

Authors:  T Hasegawa; E Hasegawa; W T Chen; K M Yamada
Journal:  J Cell Biochem       Date:  1985       Impact factor: 4.429

Review 6.  Mechanisms of cell migration in the vertebrate embryo.

Authors:  J P Thiery
Journal:  Cell Differ       Date:  1984-11

7.  Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture.

Authors:  C H Damsky; K A Knudsen; D Bradley; C A Buck; A F Horwitz
Journal:  J Cell Biol       Date:  1985-05       Impact factor: 10.539

8.  Alterations in neural crest migration by a monoclonal antibody that affects cell adhesion.

Authors:  M Bronner-Fraser
Journal:  J Cell Biol       Date:  1985-08       Impact factor: 10.539

9.  Lateral diffusion of an 80,000-dalton glycoprotein in the plasma membrane of murine fibroblasts: relationships to cell structure and function.

Authors:  K Jacobson; D O'Dell; J T August
Journal:  J Cell Biol       Date:  1984-11       Impact factor: 10.539

10.  Development of cell surface linkage complexes in cultured fibroblasts.

Authors:  W T Chen; E Hasegawa; T Hasegawa; C Weinstock; K M Yamada
Journal:  J Cell Biol       Date:  1985-04       Impact factor: 10.539

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  62 in total

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2.  The lateral diffusion of selectively aggregated peptides in giant unilamellar vesicles.

Authors:  Clarence C Lee; Matthew Revington; Stanley D Dunn; Nils O Petersen
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3.  Activation-enhanced alpha(IIb)beta(3)-integrin-cytoskeleton interactions outside of focal contacts require the alpha-subunit.

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Journal:  Mol Biol Cell       Date:  2001-05       Impact factor: 4.138

Review 4.  New insights into Nm23 control of cell adhesion and migration.

Authors:  Henri-Noël Fournier; Corinne Albigès-Rizo; Marc R Block
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5.  The roles of the myofibroblast in idiopathic pulmonary fibrosis. Ultrastructural and immunohistochemical features of sites of active extracellular matrix synthesis.

Authors:  C Kuhn; J A McDonald
Journal:  Am J Pathol       Date:  1991-05       Impact factor: 4.307

Review 6.  Neural crest cells and motor axons in avians: Common and distinct migratory molecules.

Authors:  Catherine E Krull
Journal:  Cell Adh Migr       Date:  2010 Oct-Dec       Impact factor: 3.405

7.  Characterization and fine-structural localization of actin- and fibronectin-like proteins in planaria (Dugesia lugubris s.l.).

Authors:  R Pascolini; F Panara; I Di Rosa; A Fagotti; S Lorvik
Journal:  Cell Tissue Res       Date:  1992-03       Impact factor: 5.249

8.  Dynamics of beta1-integrins in living fibroblasts--effect of substratum wettability.

Authors:  I Zlatanov; T Groth; A Lendlein; G Altankov
Journal:  Biophys J       Date:  2005-08-26       Impact factor: 4.033

9.  Nerve growth factor stimulates the accumulation of beta1 integrin at the tips of filopodia in the growth cones of sympathetic neurons.

Authors:  P W Grabham; D J Goldberg
Journal:  J Neurosci       Date:  1997-07-15       Impact factor: 6.167

10.  Localization of integrin receptors for fibronectin, collagen, and laminin in human skin. Variable expression in basal and squamous cell carcinomas.

Authors:  J Peltonen; H Larjava; S Jaakkola; H Gralnick; S K Akiyama; S S Yamada; K M Yamada; J Uitto
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