<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ramos, S.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Aureliano, M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Actin as a potential target for decavanadate</style></title><secondary-title><style face="normal" font="default" size="100%">J Inorg Biochem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Actins/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Adenosine Triphosphate/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Rabbits</style></keyword><keyword><style  face="normal" font="default" size="100%">Vanadates/*chemistry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Dec</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=20807665 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">12</style></number><volume><style face="normal" font="default" size="100%">104</style></volume><pages><style face="normal" font="default" size="100%">1234-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;ATP prevents G-actin cysteine oxidation and vanadyl formation specifically induced by decavanadate, suggesting that the oxometalate-protein interaction is affected by the nucleotide. The ATP exchange rate is increased by 2-fold due to the presence of decavanadate when compared with control actin (3.1x10(-3) s(-1)), and an apparent dissociation constant (k(dapp)) of 227.4+/-25.7 muM and 112.3+/-8.7 muM was obtained in absence or presence of 20 muM V(10), respectively. Moreover, concentrations as low as 50 muM of decameric vanadate species (V(10)) increases the relative G-actin intrinsic fluorescence intensity by approximately 80% whereas for a 10-fold concentration of monomeric vanadate (V(1)) no effects were observed. Upon decavanadate titration, it was observed a linear increase in G-actin hydrophobic surface (2.6-fold), while no changes were detected for V(1) (0-200 muM). Taken together, three major ideas arise: i) ATP prevents decavanadate-induced G-actin cysteine oxidation and vanadate reduction; ii) decavanadate promotes actin conformational changes resulting on its inactivation, iii) decavanadate has an effect on actin ATP binding site. Once it is demonstrated that actin is a new potential target for decavanadate, being the ATP binding site a suitable site for decavanadate binding, it is proposed that some of the biological effects of vanadate can be, at least in part, explained by decavanadate interactions with actin.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">20807665</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;1873-3344 (Electronic)0162-0134 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">DCBB-FCT and CCMar, University of Algarve, 8005-139 Faro, Portugal.</style></auth-address></record></records></xml>