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Potent inhibition of human telomerase by helenalin.
- Source :
-
Cancer letters [Cancer Lett] 2005 Sep 28; Vol. 227 (2), pp. 169-74. Date of Electronic Publication: 2004 Dec 24. - Publication Year :
- 2005
-
Abstract
- Telomerase activity is repressed in normal human somatic cells, but is activated in most cancers, suggesting that telomerase may be an important target for cancer therapy. Inhibition of telomerase in cancer cells has been shown to limit the growth of human cancer cells in culture. In this study, we report that helenalin, a natural sesquiterpene lactone, is a potent and selective inhibitor for human telomerase. In vitro studies indicate that this drug can inactivate telomerase directly in a manner that is dependent on concentration and time. The inhibitory action of this drug on telomerase is selective since the presence of excessive externally added proteins did not protect the inhibition and all of the other enzymes tested in this study were not inhibited by this drug. Furthermore, we demonstrated that helenalin can inhibit the expression of hTERT and telomerase in hematopoietic cancer cells. Therefore, the anti-tumor activity of helenalin is attributed, at least in part, to the inhibition of telomerase.
- Subjects :
- DNA-Binding Proteins genetics
DNA-Directed DNA Polymerase metabolism
DNA-Directed RNA Polymerases metabolism
HL-60 Cells enzymology
Humans
In Vitro Techniques
Jurkat Cells enzymology
RNA, Messenger genetics
RNA, Messenger metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sesquiterpenes, Guaiane
Telomerase genetics
Toxins, Biological
Antineoplastic Agents, Phytogenic pharmacology
DNA-Binding Proteins antagonists & inhibitors
DNA-Binding Proteins metabolism
Sesquiterpenes pharmacology
Telomerase antagonists & inhibitors
Telomerase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0304-3835
- Volume :
- 227
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Cancer letters
- Publication Type :
- Academic Journal
- Accession number :
- 16112419
- Full Text :
- https://doi.org/10.1016/j.canlet.2004.11.045