Vanadium Compounds: Biochemical and Therapeutic Applications: 16 - Rilegato

Rilegato

ISBN 10: 079233762X ISBN 13: 9780792337621

Casa editrice: Kluwer Academic Pub, 2007

Riassunto

In vitro and animal studies show that vanadate and other Because most cellular components contain hydroxyl and/or vanadium compounds increase glucose transport activity and phosphate groups, vanadate reacts as shown in eq. 1, and 2 normalize glucose metabolism [1-5]. Furthermore, these with a variety of metabolites. For example, the reaction of insulin-mimetic compounds can be administered orally. Vana­ vanadate with the 2'-hydroxyl group of the cofactor NAD date enhances the phosphoprotein formation which is attrib­ generates an NADP analog, NADV (path b) [22]. NADV is uted to either the activation of protein kinases or inhibition an excellent cofactor for enzymes such as glucose-6-phos­ of protein phosphatases. Despite the interest in document­ phate dehydrogenase, 6-phosphogluconate dehydrogenase, ing the effects of vanadate on protein kinases, most reports and alcohol dehydrogenase [22]. The presence ofNADV have used indirect methods and studies with purified kinases could affect the levels of reducing equivalents in the cell, im­ show weak, if any, interaction of vanadate with kinases as portant in maintaining a normal glucose metabolism. This a group of enzymes (reviewed in Refs. [6-8]). Vanadate type of mechanism is distinct from the vanadate-induced interacts potently with phosphatases and the inhibition is NADH oxidation by plasma membranes [23]. Organic attributed to a five-coordinate vanadate complex which vanadates have been shown to substitute for organic phos­ mimics the transition state of the phosphate ester hydroly­ phates in many of the enzymes related to glucose metabolism sis reaction (reviewed in Refs. [7,9]).

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Contenuti

Preface; A.K. Srivastava, J.-L. Chiasson. Chemistry. The chemistry of peroxovanadium compounds relevant to insulin mimesis; A. Shaver, et al. Vanadium chemistry and biochemistry of relevance for use of vanadium compounds as antidiabetic agents; D.C. Crans, et al. Peroxo heteroligand vanadates(V): synthesis, spectra-structure relationships, and stability toward decomposition; C. Djordjevic, et al. Chemically and photochemically initiated DNA cleavage by an insulin- mimetic bisperoxovanadium complex; C. Hiort, et al. Biochemical and physiological studies. Insulin-like actions of vanadate are mediated in an insulin- receptor-independent manner via non-receptor protein tyrosine kinases and protein phosphotyrosine phosphatases; Y. Shechter, et al. Peroxovanadium compounds: biological actions and mechanism of insulin-mimesis; A.P. Bevan, et al. Unique and selective mitogenic effects of vanadate on SV40-transformed cells; H. Wang, R.E. Scott. Vanadium compounds stimulate mitogen-activated protein (MAP) kinases and rebosomal S 6 kinases; S.K. Pandey, et al. Protective effect of vanadate on oxyradical-induced changes in isolated perfused heart; T. Matsubara, et al. In vivo effects of vanadate on hepatic glycogen metabolizing and lipogenic enzymes in insulin-dependent and insulin-resistant diabetic animals; R.L. Khandelwal, S. Pugazthenthi. The relationship between insulin and vanadium metabolism in insulin target tissues; F.G. Hamel, W.C. Duckworth. Modulation of insulin action by vanadate: evidence of a role for phosphotyrosine phosphatase activity to alter cellular signalling; I.G. Fantus, et al. Reversal of defective G-proteins and adenylyl cyclase/cAMP signal transduction by vanadyl sulfate therapy; M.B. Anand-Srivastava, et al. Effects of vanadate on the expression of genes involved in fuel homeostasis in animal models of type I and type II diabetes; S.M. Brichard. Decrease in protein tyrosine phosphatase activities in vanadate-treated obese Zucker (fa/fa) rat liver; S. Pugazthenthi, et al. Evidence for selective effects of vanadium on adipose cell metabolism involving actions on cAMP-dependent protein kinase; R.W. Brownsey, et al. The enhancement of pervanadate of tyrosine phosphorylation on prostatic proteins occurs through the inhibition of membrane-associated tyrosine phosphatases; M. Boissoneault, et al. Contractile effects of vanadate on aorta rings from virgin and pregnant rats; J. St-Louis, et al. In vivo modulation of N- myristoyltransferase activity by orthovanadate; M.J. King, et al. Regulation and control of glucose overutilization in erythrocytes by vanadate; N.Z. Baquer, et al. In vitro and in vivo antineoplastic effects of orthovanadate; T.F. Cruz, et al. Membrane&endash;vanadium interaction: a toxicokinetic evaluation; R.K. Upreti. Potential use in therapy and toxicological studies. Increased potency of vanadium using organic ligands; J.H. McNeill, et al. In vivo effects of peroxovanadium compounds in BB rats; J.-F. Yale, et al. Long-term antidiabetic activity of vanadyl after treatment with withdrawal restoration of insulin secretion; G. Cros, et al. Long-term correction of STZ-diabetic rats after short-term i.p. VOSO4 treatment: persistence on insulin secreting capacities assessed by isolated pancreas studies; P. Poucheret, et al. Antihypertensive effects of vanadium compounds in hyperinsilinemic, hypertensive rats; S. Bhanot, et al. Toxicology of vanadium compounds in diabetic rats: the action of chelating ag

Dettagli dell?edizione

• Editore: Kluwer Academic Pub
• Data di pubblicazione: 2007
• Lingua: Inglese
• ISBN 10: 079233762X
• ISBN 13: 9780792337621
• Rilegatura: Copertina rigida
• Numero di pagine: 244
• Redattore: Srivastava A. K., Chiasson Jean-Louis
• Contatto del produttore: non disponibile
• Persona responsabile: CMN Printpool Inh. Mathis Neumann; https://www.also.com/ec/cms5/en_6000/6000/index.jsp; ; Friedrich-Karl-Str. 9; Hamburg; Germania