Altered molecular properties of tubulin in a multidrug-resistant variant of Chinese hamster cells selected for resistance to vinca alkaloids
✍ Scribed by J. Pain; F. M. Sirotnak; J. R. Barrueco; C-H. Yang; J. L. Biedler
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 788 KB
- Volume
- 136
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
The basis for the markedly altered intracellular binding of ['Hlvincristine in a multidrug-resistant variant (DC-3FNCRd-SL) of Chinese hamster lung cells [DC-3F) was investigated. Binding of [3Hlvincristine by protein in cytosol derived from each cell type exhibited a differing requirement for GTP in MgC12 containing buffer of low-ionic strength. Binding of ['Hlvincristine occurred to cytosolic protein derived from both variant and parental DC-3F cells, but after removal of GTP, binding only occurred to cytosolic protein from parental cells regardless of the presence of added GTP. Although binding by cytosolic protein from parental DC-3F cells did not require GTP, the addition of 0.1 m M CTP increased by two-fold the rate and extent of binding. When cytosol from variant and parental DC-3F cells was incubated with low concentrations of ['Hlvincristine in high-ionic strength buffer and analyzed by molecular-sieve HPLC, most of the protein binding ['Hlvincristine in parentally derived cytosol eluted as M,