Fusion-inhibiting monoclonal antibodies and their relevant antigens in relation to sexual process of Dictyostelium discoideum

1992 ◽  
Vol 49 (2) ◽  
pp. 63-68 ◽  
Author(s):  
Kazuhiro Aiba ◽  
Hideko Urushihara ◽  
Kaichiro Yanagisawa
Keyword(s):  
Monoclonal Antibodies ◽  
Dictyostelium Discoideum ◽  
Sexual Process

Adhesion mutants of Dictyostelium discoideum lacking the saccharide determinant recognized by two adhesion-blocking monoclonal antibodies

1985 ◽  
Vol 109 (1) ◽  
pp. 111-117 ◽  
Author(s):  
William F. Loomis ◽  
Steve A. Wheeler ◽  
Wayne R. Springer ◽  
Samuel H. Barondes
Keyword(s):  
Monoclonal Antibodies ◽  
Dictyostelium Discoideum

scholarly journals Monoclonal antibodies binding to the tail of Dictyostelium discoideum myosin: their effects on antiparallel and parallel assembly and actin-activated ATPase activity.

1986 ◽  
Vol 103 (4) ◽  
pp. 1527-1538 ◽  
Author(s):  
K Pagh ◽  
G Gerisch
Keyword(s):  
Monoclonal Antibodies ◽  
Atpase Activity ◽  
Dictyostelium Discoideum ◽  
Blocking Agent ◽  
Distal Portion ◽  
Strong Inhibition ◽  
Essentially Normal ◽  
Unique Effect ◽  
Substantial Inhibition ◽  
Parallel Assembly

Eight monoclonal antibodies that bind to specific sites on the tail of Dictyostelium discoideum myosin were tested for their effects on polymerization and ATPase activity. Two antibodies that bind close to the myosin heads inhibited actin activation of the ATPase either partially or completely, without having an effect on polymerization. Two other antibodies bind to sites within the distal portion of the tail that has been shown, by cleavage mapping, to be important for polymerization. One of these antibodies binds close to the sites of heavy chain phosphorylation which is known to regulate both myosin polymerization and actin-activated ATPase activity. Both antibodies showed strong inhibition of polymerization accompanied by complete inhibition of the actin-activated ATPase activity. A unique effect was obtained with an antibody that binds to the end of the myosin tail. This antibody prevented the formation of bipolar filaments. It caused myosin to assemble into unipolar filaments with heads at one end and the antibody molecules at the other. Only at concentrations higher than required for its effect on polymerization did this antibody show substantial inhibition of the actin-activated ATPase. These results indicate that, using a monoclonal antibody as a blocking agent, parallel assembly of myosin can be dissected out from antiparallel association, and that essentially normal actin-activated ATPase activity could be obtained after significant reductions in filament size.

scholarly journals Identification of tubulin in Dictyostelium discoideum: characterization of some unique properties.

1983 ◽  
Vol 97 (4) ◽  
pp. 1011-1019 ◽  
Author(s):  
E White ◽  
E M Tolbert ◽  
E R Katz
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Dictyostelium Discoideum ◽  
Polyclonal Antibody ◽  
Slime Mold ◽  
Cold Sensitivity ◽  
Two Dimensional ◽  
Alpha Tubulin ◽  
Peptide Maps

We used three antitubulin antibodies to localize Dictyostelium tubulin subunits on two-dimensional polyacrylamide gels by Western blotting. All three antibodies, a polyclonal antibody against sea urchin alpha- and beta-tubulin and two monoclonal antibodies against yeast alpha-tubulin, recognize the same set of polypeptides with a molecular weight of 55,000 while focusing at a pH far more basic than all other tubulins. Each antibody specifically stains the microtubule system of slime mold amoebae by indirect immunofluorescence. The microtubule system can be isolated as a major component of the amoeba cytoskeleton, and these preparations are greatly enriched for the presumptive tubulin subunits. The microtubules of these cytoskeletons are resistant to being depolymerized by millimolar concentrations of calcium, while they retain their cold sensitivity. Comparison of peptide maps of slime mold and brain alpha-tubulins indicates that the proteins are related but not identical. Possible explanations for these unusual characteristics are discussed.

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