%0 Journal Article
%T Recent perspectives into biochemistry of decavanadate
%A Manuel Aureliano
%A FCT
%A University of Algarve
%A Gambelas
%J World Journal of Biological Chemistry
%D 2011
%I Baishideng Publishing Group Co. Limited
%R 10.4331/wjbc.v2.i10.215
%X The number of papers about decavanadate has doubled in the past decade. In the present review, new insights into decavanadate biochemistry, cell biology, and antidiabetic and antitumor activities are described. Decameric vanadate species (V10) clearly differs from monomeric vanadate (V1), and affects differently calcium pumps, and structure and function of myosin and actin. Only decavanadate inhibits calcium accumulation by calcium pump ATPase, and strongly inhibits actomyosin ATPase activity (IC50 = 1.4 ¦̀mol/L, V10), whereas no such effects are detected with V1 up to 150 ¦̀mol/L; prevents actin polymerization (IC50 of 68 ¦̀mol/L, whereas no effects detected with up to 2 mmol/L V1); and interacts with actin in a way that induces cysteine oxidation and vanadate reduction to vanadyl. Moreover, in vivo decavanadate toxicity studies have revealed that acute exposure to polyoxovanadate induces different changes in antioxidant enzymes and oxidative stress parameters, in comparison with vanadate. In vitro studies have clearly demonstrated that mitochondrial oxygen consumption is strongly affected by decavanadate (IC50, 0.1 ¦̀mol/L); perhaps the most relevant biological effect. Finally, decavanadate (100 ¦̀mol/L) increases rat adipocyte glucose accumulation more potently than several vanadium complexes. Preliminary studies suggest that decavanadate does not have similar effects in human adipocytes. Although decavanadate can be a useful biochemical tool, further studies must be carried out before it can be confirmed that decavanadate and its complexes can be used as anticancer or antidiabetic agents.
%K Decavanadate
%K Vanadate
%K Calcium pump
%K Myosin
%K Actin
%K Actin polymerization
%K Insulin mimetic
%K Antidiabetic agent
%K Antitumor agent
%U http://www.wjgnet.com/1949-8454/full/v2/i10/215.htm