http://www.cnr.it/ontology/cnr/individuo/prodotto/ID38650
Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs (Articolo in rivista)
- Type
- Label
- Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.ccr.2009.02.026 (literal)
- Alternative label
Bindoli A., Rigobello M.P., Scutari G., Gabbiani C., Casini A., Messori L. (2009)
Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs
in Coordination chemistry reviews (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Bindoli A., Rigobello M.P., Scutari G., Gabbiani C., Casini A., Messori L. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Neuroscienze (CNR), Sezione di Padova, c/o Dipartimento di Chimica Biologica, Viale G. Colombo 3, 35121 Padova, Italy
Dipartimento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, 35121 Padova, Italy
Laboratory of \"Metals in Medicine\" (METMED), Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Firenze, Italy
Laboratory of Organometallic and Medicinal Chemistry, Ecole Polytechnique Fédérale de Lausanne, SB-ISIC LCOM, BCH 2404, CH-1015 Lausanne, Switzerland (literal)
- Titolo
- Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs (literal)
- Abstract
- The thioredoxin system plays a key role in regulating the overall intracellular redox balance. It basically
comprises the small redox protein thioredoxin (Trx), nicotinamide adenine dinucleotide phosphate, in
its reduced form (NADPH), and thioredoxin reductase (TrxR), a large homodimeric selenzoenzyme controlling
the redox state of thioredoxin. Details of the thioredoxin system are provided herein, particular
emphasis being given to the protein chemistry of thioredoxin reductases. Several lines of evidence point
out today that the thioredoxin system represents an effective \"druggable\" target for the development
of new anticancer agents. Accordingly, a number of established anticancer agents were retrospectively
found to be potent inhibitors of thioredoxin reductases and to induce severe oxidative stress. During the
last decade a variety of gold compounds, either gold(I) or gold(III), were reported to manifest outstanding
antitumor properties, forming a promising class of experimental anticancer agents. In turn, recent
studies have revealed that several cytotoxic gold compounds, either gold(I) or gold(III), are potent TrxR
inhibitors. Details of their mechanism of selenoenzyme inhibition are currently under investigation, in
our laboratory, and some newresultswill be anticipated here; notably, preferential gold targeting of active
site selenolate could be experimentally supported. Based on the numerous experimental evidences now
available, both at the molecular and cellular level,we propose that the relevant cytotoxic actions produced
by gold compounds are mainly the result of potent inhibition of thioredoxin reductase; the alterations
of mitochondrial functions, elicited by profound TrxR inhibition, would eventually lead to cell apoptosis.
A general and unitary framework is thus offered to interpret the mode of action of cytotoxic gold compounds,
according to which they should be primarily considered as antimitochondrial drugs. The peculiar
properties of gold compounds highlighted in this review might be further exploited for the obtainment
of newer and selective anticancer agents. (literal)
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- Autore CNR
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