A Membrane Glycoprotein of Aggregating <i>Dictyostelium</i> Cells with the Properties of Contact Sites

Müller, Kurt; Gerisch, Günther; Fromme, Inge; Mayer, Hubert; Tsugita, Akira

doi:10.1111/j.1432-1033.1979.tb13271.x

Cited by 94 publications

(41 citation statements)

References 40 publications

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“…Although these polyclonal antibodies react with many proteins of developed cells, the adhesion-blocking activity can be effectively neutralized by a surface glycoprotein of ca. 80,000 daltcns (gp8O) (9,10). Likewise, rabbit antibodies prepared against purified gp8O have been found to block EDTA-resistant adhesion (12).…”

mentioning

confidence: 99%

Mutations affecting a surface glycoprotein, gp80, of Dictyostelium discoideum.

Murray¹,

Wheeler²,

Jongens³

et al. 1984

Mol. Cell. Biol.

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We isolated two independent mutations in Dictyostelium discoideum that result in the absence of the antigenic determinant recognized by monoclonal antibody E28D8. This antibody reacts with a posttranslational modification on t he surface glycoprotein gp8O and several other proteins. Both of the mutations occur in the same locus, modB, which was mapped to linkage group VI. The modB mutations result in sufficient alteration of gp80 that it is absent or unrecognizable by two-dimensional gel electrophoresis. Strains carrying)modB mutations exhibit "contact sites A"-mediated cell-cell adhesion although more weakly than do wild-type strain s and develop to fruiting bodies carrying viable spores. Although gp8O has been implicated in the mechanism of cell-cell adhesion in D. discoideum, it is clear from the behavior of these mutant strains that the determinant on gp8O recognized by E28D8 is not necessary for either morphogenesis or reduced EDTYA-resistant adhesion.Cells of Dictyostelium discoideum unidergo a process of development during which they become able to form strong, EDTA-resistant intercellular adhesions (nediated by "contact sites A") (4). This EDTA-resistant adhesion can be blocked by Fab fragments of antibodies from sera prepared against developed cells. Although these polyclonal antibodies react with many proteins of developed cells, the adhesion-blocking activity can be effectively neutralized by a surface glycoprotein of ca. 80,000 daltcns (gp8O) (9, 10). Likewise, rabbit antibodies prepared against purified gp8O have been found to block EDTA-resistant adhesion (12). gp8O is undetectable during the first few hours of development and is synthesized and accumulates between 8 and 14 h of development coordinately with the acquisition of EDTAresistant adhesion (12,14). For these reasons it is thought that gp8O may play a direct role in the mechanism of cell-cell adhesion in developed D. discoideum.Rabbit serum prepared against purified gp8O reacts not only with gp8O but with several other proteins, apparently due to the presence of shared antigenic determinants (11, 12). A few of these antigenic proteins are present in vegetative cells and exhaustive absorption of this serum with vegetative cells removes some but not all immunological reactivity to gp80 (11). However, the exhaustively absorbed serum is no longer found to block EDTA-resistant intercellular adhesion (11). These results raised the possibility that some determinants on gp8O might not be critical to the mechanism of adhesion, whereas others are clearly crucial as shown by the ability of purified gp8O alone to neutralize the adhesion-blocking activity of the antiserum.Monoclonal antibodies have been raised against gp8O (11,14,15 described (11). Amoebae were mutagenized with N-methyl-N'-nitro-N-nitrosoguanidine to 10-3 to 10-4 survival and were immediately plated into microtest plates at about 1 cell per well as described previously (6). Surviving clones were grown to a density of ca. 104 to 105 cells per ml, at which point 5-pAl samples were spot...

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mentioning

confidence: 99%

Mutations affecting a surface glycoprotein, gp80, of Dictyostelium discoideum.

Murray¹,

Wheeler²,

Jongens³

et al. 1984

Mol. Cell. Biol.

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“…4) (Siu et al, 1976) increase in concentration during development. Contact site A is a plasma membrane glycoprotein (Muller & Gerisch, 1978;Muller et al, 1979) required for cell cohesion during aggregation, whereas discoidin comprises two proteins (discoidin I and II) which are lectins (Rosen et al, 1973;Simpson et al, 1974). It would also seem that the spore coat proteins accumulate during late development in the prespore cells and spores (Devine et al, 1982;Wilkinson et al, 1983).…”

Section: Differential Distribution Ofdevelopmentally Regulated Enzymesmentioning

confidence: 99%

Protein synthesis during development and differentiation in the cellular slime mould Dictyostelium discoideum

Watts¹

1984

Biochemical Journal

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“…Recently, cell surface glycoconjugates have been considered to function in cell to cell recognition and adhesion (7). The cellular slime mold provides a good example of this because the formation of pseudoplasmodia is due to the glycoprotein called contact site A (17,18) and/or the specific interaction between endogenous lectins and the cell surface receptors of the glycoconjugates. These lectins, the discoidin from Dictyostelium discoideum (26,30) and the pallidin from Polysphondylium pallidum (27,28), as well as their glycoconjugate receptors (23), have been studied extensively.…”

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confidence: 99%

Lectin binding studies on the slime mold, Physarum polycephalum.

Kitagaki

Hatakeyama

Matsumoto

et al. 1982

Cell Struct. Funct.

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ABSTRACT. Cell surface glycoconjugate receptors for wheat germ agglutinin, Ricinus communis agglutinin, concanavalin A and soybean agglutinin on two strains of myxoamoebae of Physarum polycephalum with fluorescein isothiocynate-labelled lectins were observed microscopically, but no receptors for Dolichos biflorus agglutinin, Ulex europeus agglutinin-I and Arachis hypogaea agglutinin were found. These results suggest that the myxoamoebae have cell surface glycoproteins with N-glycosidically linked hetero-saccharide chains, but not oligosaccharides with blood group A and H determinants. The number of lectin receptor sites and their affinity constants for lectins were obtained for the myxoamoebae and microplasmodia of P. polycephalum from binding assays with 125I-lectins. The densities of these lectin receptors and the magnitudes of the affinity constants were similar to those of mammalian cells. Neuraminidase treatment of the myxoamoebae and microplasmodia induced neither a decrease in WGA receptors nor an increase in RCA receptors. These results are strong evidence that sialyl residues are absent in glycoconjugates on the surface of the myxoamoebae and microplasmodia of P. polycephalum.

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A Membrane Glycoprotein of Aggregating Dictyostelium Cells with the Properties of Contact Sites

Cited by 94 publications

References 40 publications

Mutations affecting a surface glycoprotein, gp80, of Dictyostelium discoideum.

Mutations affecting a surface glycoprotein, gp80, of Dictyostelium discoideum.

Protein synthesis during development and differentiation in the cellular slime mould Dictyostelium discoideum

Lectin binding studies on the slime mold, Physarum polycephalum.

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