Autor(es):
Aureliano, M. 
Data: 2007
Identificador Persistente: http://hdl.handle.net/10400.1/1306
Origem: Sapientia - Universidade do Algarve
Assunto(s): Decavanadate; Vanadiummetallomics
Detalhes do Documento
Biological effects of decavanadate: muscle contraction, in vivo oxidative stres...
Descrição
Decameric vanadate species (V10) can be formed at physiological pH values in vanadate solutions presumably containing only monomeric vanadate species (V1). Sarcoplasmic reticulum Ca2+-ATPase and myosin are known to interact with decameric vanadate species. V10 interaction with myosin is favored by conformational changes that takes place in myosin during the catalytic cycle. Apparently, V10 operates at a different protein state in comparison to monomeric vanadate (V1) that mimics the protein at the hydrolysis transition state. V10 also clearly differs from V1, by inhibiting sarcoplasmic reticulum calcium accumulation in non-damage native vesicles, besides affecting calcium efflux associated with ATP synthesis and proton ejection associated with ATP hydrolysis. Recently reported studies referred that V10 is stabilized by actin during the process of the protein polymerization since the decomposition half-life time increases from 5 to 27 hours, suggesting that the interaction is also support by a protein conformation induce during ATP hydrolysis followed by the formation of protein filaments. Besides affecting muscle contraction and its regulation, V10, as low as 100 nM, inhibits 50% of oxygen consumption in mitochondria, pointing that this organelle is a potential cellular target for V10, while a 100-fold higher concentration of V1 (10 µM) is needed to induce the same effect. Furthermore, in vivo studies have shown that following an acute exposure, decavanadate induced different changes, when compared to vanadate, on oxidative stress markers, vanadium intracellular accumulation as well as in lipid peroxidation. Putting it all together, it is suggested that the biological effects of decameric vanadate species contribute, at least in part, to the understanding of the versatility of vanadium biochemistry.
Decameric vanadate species (V10) can be formed at physiological pH values in vanadate solutions presumably containing only monomeric vanadate species (V1). Sarcoplasmic reticulum Ca2+-ATPase and myosin are known to interact with decameric vanadate species. V10 interaction with myosin is favored by conformational changes that takes place in myosin during the catalytic cycle. Apparently, V10 operates at a different protein state in comparison to monomeric vanadate (V1) that mimics the protein at the hydrolysis transition state. V10 also clearly differs from V1, by inhibiting sarcoplasmic reticulum calcium accumulation in non-damage native vesicles, besides affecting calcium efflux associated with ATP synthesis and proton ejection associated with ATP hydrolysis. Recently reported studies referred that V10 is stabilized by actin during the process of the protein polymerization since the decomposition half-life time increases from 5 to 27 hours, suggesting that the interaction is also support by a protein conformation induce during ATP hydrolysis followed by the formation of protein filaments. Besides affecting muscle contraction and its regulation, V10, as low as 100 nM, inhibits 50% of oxygen consumption in mitochondria, pointing that this organelle is a potential cellular target for V10, while a 100-fold higher concentration of V1 (10 µM) is needed to induce the same effect. Furthermore, in vivo studies have shown that following an acute exposure, decavanadate induced different changes, when compared to vanadate, on oxidative stress markers, vanadium intracellular accumulation as well as in lipid peroxidation. Putting it all together, it is suggested that the biological effects of decameric vanadate species contribute, at least in part, to the understanding of the versatility of vanadium biochemistry.
Tipo de Documento
Parte ou capítulo de livro
Idioma Inglês
Idioma Inglês
| Financiadores do RCAAP | |||||||
|
|
|
|
|
|
||