Interaction of Arenastatin A with Porcine Brain Tubulin

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 presenc...

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Veröffentlicht in:Biological & pharmaceutical bulletin 1997/02/15, Vol.20(2), pp.171-174
Hauptverfasser: MORITA, Koji, KOISO, Yukiko, HASHIMOTO, Yuichi, KOBAYASHI, Motomasa, WANG, Weiqi, OHYABU, Naoki, IWASAKI, Shigeo
Format: Artikel
Sprache:eng
Schlagworte:
Animals
antimitotic agent
arenastatin A
Binding, Competitive
Biological and medical sciences
Brain - metabolism
Colchicine - metabolism
Depsipeptides
General pharmacology
Lactones - metabolism
Macrolides
Medical sciences
Peptides, Cyclic - metabolism
Pharmacognosy. Homeopathy. Health food
Pharmacology. Drug treatments
Protein Binding
Swine
triamide analog
tubulin
Tubulin - metabolism
Vinblastine - metabolism
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Zusammenfassung: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 1.8×10-6 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.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.20.171