Interaction of arenastatin A with porcine brain tubulin.
Arenastatin A, isolated from the Okinawan marine sponge Dysidea arenaria, is an antimitotic depsipeptide containing a 16-membered ring. Interaction of the compound with tubulin was investigated by the use of [3H]arenastatin A and other microtubule disruptors. Scatchard analysis indicated the presence of one binding site for arenastatin A per tubulin heterodimer with a dissociation constant (Kd) of 1.8 x 10(-6) M. Rhizoxin was a competitive inhibitor of arenastatin A binding, and vinblastine also inhibited arenastatin A binding in a partially competitive manner. Arenastatin A had no inhibitory effect on colchicine binding to tubulin.
Morita
K
K
Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.
Koiso
Y
Y
Hashimoto
Y
Y
Kobayashi
M
M
Wang
W
W
Ohyabu
N
N
Iwasaki
S
S
D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism*; D003078:Colchicine / Q000378:metabolism; D047630:Depsipeptides; D007783:Lactones / Q000378:metabolism; D018942:Macrolides; D010456:Peptides, Cyclic / Q000378:metabolism*; D011485:Protein Binding; D013552:Swine; D014404:Tubulin / Q000378:metabolism*; D014747:Vinblastine / Q000378:metabolism
D047630:Depsipeptides; D007783:Lactones; D018942:Macrolides; D010456:Peptides, Cyclic; D014404:Tubulin; C096566:arenastatin A; C087237:ustiloxin A; D014747:Vinblastine; C041443:rhizoxin; D003078:Colchicine