A requirement for trypsin-sensitive cell-surface components for cell-cell interactions of embryonic neural retina cells

McClay,; Godding, L R; Me, Fransen

doi:10.1083/jcb.75.1.56

Cited by 45 publications

(10 citation statements)

References 34 publications

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“…With these changes, the rates at which single cells adhered and the topographic specificity that they exhibited remained constant, but the total numbers of cells collected could be increased to only ~5%. However, using large numbers of aggregates prepared from halves of optic tecta as collecting surfaces, McClay et al (26) have corroborated the preferential adhesion of dorsal and ventral retinal cells for tectal tissue. In their experiments, >50% of the input retinal cells adhered to aggregates made from the proper halves of tecta.…”

Section: The Relation Of These Data To Neuronal Specificitymentioning

confidence: 99%

Biochemical investigations of retinotectal adhesive specificity

Marchase¹

1977

The Journal of Cell Biology

143

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The preferential adhesion of chick neural retina cells to surfaces of intact optic tecta has been investigated biochemically. The study uses a collection assay in which single cells from either dorsal or ventral halves of neural retina adhere preferentially to ventral or dorsal halves of optic tecta, respectively. The data presented support the following conclusions: (a) The adhesion of ventral retina to dorsal tecta seems to depend on proteins located on ventral retina and on terminal /3-N-acetylgalactosamine residues on dorsal tecta. (b) The adhesion of dorsal retina to ventral tecta seems to depend on proteins located on ventral tecta and on terminal fl-N-acetylgalactosamine residues on dorsal retina. (c) A double gradient model for retinotectal adhesion along the dorsoventral axis is consistent with the data presented. The model utilizes only two complementary molecules. The molecule suggested to be concentrated dorsally in both retina and rectum seems to require terminal fl-N-acetylgalactosamine residues for adhesion. Its activity is not affected by protease. A molecule fitting these qualifications, the ganglioside GM2, could not be detected in a gradient, but lecithin vesicles containing GM2 adhered preferentially to ventral tectal surfaces. The second molecule, concentrated ventrally in both retina and tectum, is a protein and seems capable of binding terminal fl-N-acetylgalactosamine residues. One enzyme, UDP-galactose:GM2 galactosyltransferase, has been found to be more concentrated in ventral retina than dorsal, but only by 30%.A topographic selectivity characterizes the adhesion of neural retina cells to optic tecta. Cell bodies from dorsal half-retina have been shown to adhere preferentially to ventral surfaces of optic tecta, while those from ventral half-retina prefer dorsal surfaces of tecta (2,3,25). Investigations of the biochemical mechanisms underlying this selectivity are reported here.The basis for this study is an assay that compares the rates at which single retinal cells adhere to limited areas of tectal surface. In this assay, either dorsal or ventral halves of neural retina are labeled with 32p and dissociated with trypsin to form a single-cell suspension. Tecta are split into equal-sized dorsal and ventral halves and fixed to the bottom of a petri dish. The labeled retinal cells are added to the dish, and the dish is reciprocated. After a collection period, typically 1 h, the tectal halves are washed and counted individually in a scintillation counter to determine the numbers of radioactive retinal cells that adhered. Since the number of collisions between the labeled retinal cells and each of the tectal halves is equal, comparisons between the numbers of cells adhering to dorsal and ventral halves provide an operational definition of adhesive specificity.

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Section: The Relation Of These Data To Neuronal Specificitymentioning

confidence: 99%

Biochemical investigations of retinotectal adhesive specificity

Marchase¹

1977

The Journal of Cell Biology

143

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“…The first is the unknown, perhaps lingering, effect of the dispersing procedure on the cell surface and on desmosome formation (10,14,21,40,72,73,77) . The second is the persistence of desmosomal remnants at the surface of the dispersed cells (48), making it difficult to judge whether a desmosome seen during or after reaggregation is the result of true, de novo formation or simply the reapposition of two remnants .…”

mentioning

confidence: 99%

Desmosome development in an in vitro model.

Dembitzer¹,

Herz²,

Schermer³

et al. 1980

The Journal of Cell Biology

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“…cells (8). Cells can be agglutinated with lectins immediately after treatment with trypsin or EDTA (EGTA), two agents which severely impair intercellular adhesion (8,18,22,24,26,27).…”

Section: Discussionmentioning

confidence: 99%

“…However, the functional significance of these surface rearrangements is not presently well understood (12). Current speculations about intercellular adhesion suggest that proteins and carbohydrates participate in adhesive bonds (9,17,22,26,32,33), that receptor mobility may be needed, and that cytoskeletal structures are involved (8,27,30,41,43). Because these features are targets of lectin activity, we studied the effects of lectin binding on the formation of adhesions between embryonic cells.…”

Section: Abstract Intercellular Adhesion Concanavalin a Cell Surfacementioning

confidence: 99%

Inhibition of intercellular adhesion by concanavalin A is associated with concanavalin A-mediated redistribution of surface receptors.

Letourneau¹

1979

The Journal of Cell Biology

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The inhibition of adhesion between aggregates and layers of embryonic retinal cells by concanavalin A (Con A) and Con A-mediated rearrangements of Con A receptors on retinal cells were studied. A short incubation of aggregates and layers with 10/xg/ml Con A substantially reduced aggregate-to-layer adhesion in a subsequent assay without soluble lectin present. This effect of Con A was dosedependent, temperature-sensitive, involved events subsequent to Con A binding, and was reduced by cytochalasin B. The inhibition produced by succinylated Con A was substantially increased by incubation with antibody to Con A. Visualization of Con A-receptor complexes by fluorescence microscopy revealed that binding of Con A induced clearing of Con A receptors from filopodia, flattened regions of growth cones, and the edges of axons. This clearing reaction was prevented by the same agents that reduced Con A's inhibition of cell adhesion: low temperature, succinylation of Con A, or cytochalasin B. Aggregate-layer adhesion was restored by releasing Con A at 37~ Inhibitors of protein and ATP synthesis did not prevent recovery of ability to make adhesions. However, release of Con A at lowered temperatures did prevent recovery. The results suggest that intercellular adhesion is inhibited by events associated with redistribution of Con A-receptor complexes on retinal cells. KEY WORDS intercellular adhesion concanavalin A cell surface rearrangements nerve growth cones filopodiaLectins have been investigated because of the interesting activities associated with their binding to cell surface polysaccharides, hemagglutination, mitogenic stimulation of lymphocytes and agglutination of tumor cells (37). Recent studies demonstrate that the binding of lectins leads to redistribution of lectin receptors within the cell surface (2,7, 11,12,39,45). These events can alter the distribution and mobility of other surface components (36, 46). However, the functional significance of these surface rearrangements is not presently well understood (12). Current speculations about intercellular adhesion suggest that proteins and carbohydrates participate in adhesive bonds (9,17,22,26,32,33), that receptor mobility may be needed, and that 128J. CELL BIOLOGY 9 The Rockefeller University Press 9

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A requirement for trypsin-sensitive cell-surface components for cell-cell interactions of embryonic neural retina cells

Cited by 45 publications

References 34 publications

Biochemical investigations of retinotectal adhesive specificity

Biochemical investigations of retinotectal adhesive specificity

Desmosome development in an in vitro model.

Inhibition of intercellular adhesion by concanavalin A is associated with concanavalin A-mediated redistribution of surface receptors.

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