Cytoskeletal drugs
From Wikipedia, the free encyclopedia
Cytoskeletal drugs are small molecules that interact with actin or tubulin. Some cytoskeltal drugs stabilize a cytoskeletal component, such as taxol which stabilized microtubules. Other prevent polymerization. For example, Cytochalasin D binds to actin monomers and prevents polymerization of actin filaments. Some of these drugs are used therapeutically while others are only available for research.[1]
| Drug Name | Target cytoskeletal component | Effect | Clinical applications |
|---|---|---|---|
| Colchicine[2] | microtubules | prevents polymerization | Used to treat gout |
| Cytochalasins[3] | actin | prevents polymerization | none |
| Demecolcine[4] | microtubules | depolymerizes | chemotherapy |
| Latrunculin[5] | actin | prevent polymerization | none |
| Jasplakinolide[6][7] | actin | enhances polymerization | none |
| Nocodazole[8] | microtubules | prevents polymerization | none |
| Paclitaxel (taxol)[9] | microtubules | stabilizes microtubules and therefore prevents mitosis | chemotherarpy |
| Phalloidin[10] | actin | stabilizes | none |
| Swinholide[11] | actin | sequesters actin dimers | none |
| Vinblastine[1] | microtubules | prevents polymerization | none |
See also
References
- ↑ 1.0 1.1 Jordan, M. A.; Leslie, W. (2004). "Microtubules as a Target for Anticancer Drugs". Nature Reviews Cancer 4 (4): 253–265. doi:10.1038/nrc1317. PMID 15057285.
- ↑ Vandecandelaere, A ; Martin, S R; Engelborghs, Y (April 1, 1997). "Response of microtubules to the addition of colchicine and tubulin-colchicine: evaluation of models for the interaction of drugs with microtubules". Biochem J 323 (Pt 1): 189–196. PMC 1218294. PMID 9173881.
- ↑ Cooper, J. A. (1987). "Effects of Cytochalasin and Phalloidin on Actin" (pdf). Journal of Cell Biology 105 (4): 1473–1478. doi:10.1083/jcb.105.4.1473. PMC 2114638. PMID 3312229.
- ↑ Jordan, Mary Ann; Wilson, Leslie (2004). "Microtubules as a target for anticancer drugs". Nature reviews. Cancer 4 (4): 253–65. doi:10.1038/nrc1317. PMID 15057285.
- ↑ Yarmola, E.G., Somasundaram, T., Boring, T.A., Spector, I., Bubb, M.R. (2000). "Actin-Latrunculin A Structure and Function". Journal of Biological Chemistry 275 (36): 28120–28127. doi:10.1074/jbc.M004253200. PMID 10859320.
- ↑ Sasse, F; Kunze, B; Gronewold, TM; Reichenbach, H (Oct 21, 1998). "The chondramides: cytostatic agents from myxobacteria acting on the actin cytoskeleton.". Journal of the National Cancer Institute 90 (20): 1559–63. PMID 9790549.
- ↑ Bubb, Michael R.; Spector I., Beyer B.B., Fosen K.M. (2000). "Effects of Jasplakinolide on the Kinetics of Actin Polymerization". J Biol Chem 275 (7): 5163–70. PMID 10671562.
- ↑ Vasquez, R.J., et al. (1997). "Nanomolar concentrations of nocodazole alter microtubule dynamic instability in vivo and in vitro". Mol. Biol. Cell 8: 973–985.
- ↑ Wani M, Taylor H, Wall M, Coggon P, McPhail A (1971). "Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia". J Am Chem Soc 93 (9): 2325–7. doi:10.1021/ja00738a045. PMID 5553076.
- ↑ Buchwalow, Igor B., Böcker, Werner (2010). Immunohistochemistry: Basics and Methods. Springer,. p. 92. ISBN 978-3-642-04608-7.
- ↑ Bubb, MR; Spector, I; Bershadsky, AD; Korn, ED (1995). "Swinholide a is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments". The Journal of Biological Chemistry 270 (8): 3463–6. PMID 7876075.
This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.