Effect of meso-hexestrol, a synthetic estrogen, on S-tubulin.
We have reported that meso-hexestrol, a synthetic estrogen, inhibits microtubule assembly and induces microtubule proteins into twisted ribbon structures. On the other hand, Serrano et al. proved that S-tubulin, which lacks the C-terminal moiety of tubulin subunits, assembles into sheet structures in the absence of microtubule-associated proteins (MAPs). In the present investigation, we attempted to clarify whether meso-hexestrol could induce the ribbon structure from S-tubulin. meso-Hexestrol delayed the initiation of polymerization of S-tubulin into sheet structures in a dose-dependent manner below 50 microM. But the effect of meso-hexestrol on S-tubulin was reduced in the presence of either tau or microtubule-associated protein 2 (MAP2) in a MAPs-concentration-dependent manner. At concentrations higher than 100 microM, meso-hexestrol inhibited the polymerization of S-tubulin into sheet structures, without forming ribbon structures. The present results may indicate that moso-hexestrol interacts with S-tubulin, and its interaction is affected by MAPs.
Sakakibara
Y
Y
Biochemistry Division, Kyoritsu College of Pharmacy, Tokyo, Japan.
Oda
T
T
Hirata
A
A
Matsuhashi
M
M
Sato
Y
Y
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006589:Hexestrol / Q000494:pharmacology*; D008869:Microtubule-Associated Proteins / Q000096:biosynthesis; D013552:Swine; D014404:Tubulin / Q000096:biosynthesis*
D008869:Microtubule-Associated Proteins; D014404:Tubulin; D006589:Hexestrol