Erythro-9-[3-(2-hydroxynonyl)]adenine and vanadate as probes for microtubule-based cytoskeletal mechanochemistry.
As probes for the involvement of dynein-like mechanochemical ATPases in microtubule-based cytoskeletal motility, the dynein ATPase inhibitors EHNA and vanadate are rendered impractical by their lack of specificity. Rapid inhibition of motility by both agents in permeabilized cell models, in conjunction with controls such as those outlined in Table II, would be consistent with the involvement of dynein-microtubule mechanochemistry. It would then be essential to analyze cell-free preparations for the presence of a dynein-like ATPase, based initially on criteria such as those suggested in Table I. Convincing evidence for the involvement of dynein-microtubule mechanochemistry will probably require, ultimately, the inhibition of cytoplasmic motility by a specific anticytoplasmic dynein antibody, analogous to experiments demonstrating the dependence of cytokinesis on actomyosin mechanochemistry.
D000199:Actins / Q000037:antagonists & inhibitors; D000225:Adenine / Q000031:analogs & derivatives* / Q000494:pharmacology; D058892:Adenosine Deaminase Inhibitors; D000818:Animals; D002463:Cell Membrane Permeability; D002470:Cell Survival / Q000187:drug effects; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism*; D004398:Dyneins / Q000037:antagonists & inhibitors; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
D000199:Actins; D058892:Adenosine Deaminase Inhibitors; D014639:Vanadium; D014638:Vanadates; C010192:9-(2-hydroxy-3-nonyl)adenine; D004398:Dyneins; D000225:Adenine