Effect of meso-hexestrol, a synthetic estrogen, on S-tubulin
| Autor: | Taiko Oda, Michio Matsuhashi, Yumiko Sakakibara, Aiko Hirata, Yoshihiro Sato |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Hexestrol
Swine Microtubule-associated protein Stereochemistry Ribbon diagram macromolecular substances Tubulin Microtubule Drug Discovery polycyclic compounds medicine Animals Moiety biology Chemistry fungi General Chemistry General Medicine Mechanism of action Polymerization biology.protein Biophysics Electrophoresis Polyacrylamide Gel medicine.symptom Microtubule-Associated Proteins |
| Zdroj: | Chemical and Pharmaceutical Bulletin. 38:3419-3422 |
| ISSN: | 1347-5223 0009-2363 |
| DOI: | 10.1248/cpb.38.3419 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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