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The role of membrane lectins in dictyostelium discoideum aggregation as ascertained by specific univalent antibodies against discoidin I
Author(s) -
Cano Amparo,
Pestaña Angel
Publication year - 1984
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240250104
Subject(s) - dictyostelium discoideum , antibody , in vitro , morphogenesis , lectin , chemistry , immunofluorescence , cell , microbiology and biotechnology , biochemistry , biology , immunology , gene
Antibodies against pure discoidin I have been used as a tool to ascertain the role of this lectin in aggregation of Dictyostelium discoideum. Discoidin I is widely expressed over the cell surface of aggregation‐competent AX‐2 cells, as ascertained by indirect immunofluorescence with specific (antidiscoidin I) antibodies. Univalent antidiscoidin I antibodies (Fab fragments) inhibit the aggregation‐specific intercellular adhesion of D discoideum AX‐2 cells in an in vitro assay. This inhibition depends on antibody concentration and cell density; a 50% inhibition of cell aggregation was obtained at antidiscoidin I Fab concentration of 4.5 mg/ml and 1 × 10 6 cells/ml. Aggregation and morphogenesis on solid support is also effectively inhibited when AX‐2 cells are starved in the presence of antidiscoidin I Fab fragments. The inhibition of morphogenesis is also dose dependent and more effective than in the in vitro assay. No inhibition of aggregation either in the in vitro assay or on morphogenesis on solid support was observed with preimmune Fab fragments at any of the concentrations tested (up to 9.6 mg/ml).