Modulation of thymidine kinase activity: a biochemical strategy to enhance the activation of antineoplastic drugs
P. R. health sci. j
; 13(1): 19-23, mar. 1994.
Article
in En
| LILACS
| ID: lil-176771
Responsible library:
BR1.1
RESUMO
Thymidine kinase is a key enzyme responsible for the activation of several anticancer and antiviral drugs. As the first enzyme in the salvage pathway of thymidine, it is regulated by the feedback inhibition exerted by the end-product of the pathway, namely thymidine 5'-triphosphate. 5'-Aminothymidine is a non-toxic analogue of thymidine capable of interfering with this regulatory mechanism. In fact, it has been shown that 5'-aminothymidine increases the cytotoxicity and metabolism of various thymidine analogues currently in use of the clinic as antineoplastic agents. This mini-review article focuses in the evidence supporting the role of 5'-aminothymidine as a potential prototype drug for a new class of anticancer agents drugs which affect the regulation of key metabolic pathways that determine the efficacy of agents with cytotoxic activity. The mechanism of action, antineoplastic activities and basis for selectivity in tissue culture models are also described
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Index:
LILACS
Main subject:
Thymidine
/
Thymidine Kinase
/
Antineoplastic Agents
Limits:
Animals
/
Humans
Language:
En
Journal:
P. R. health sci. j
Journal subject:
MEDICINA
Year:
1994
Type:
Article