Membrane transport of vanadium compounds and the interaction with the erythrocyte membrane

作者: Xiaogai Yang , Kui Wang , Jingfen Lu , Debbie C Crans

DOI: 10.1016/S0010-8545(02)00247-3

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摘要: In the present work, membrane transport and biotransformation of vanadate, bis(maltolato)oxovanadium (VO(ma)2), vanadyl acetylacetonate (VO(acac)2) were investigated to explore relationship with their insulin-like activity. Cellular uptake kinetics performed by ICP-AES EPR. The VO(acac)2 VO(ma)2 human erythrocytes showed intracellular vanadium level higher than NaVO3 these two complexes was presumed be via passive diffusion mechanism. A fraction oxidized anionic vanadium(V) species also entered cells anion channel. stability oxidation in erythrocyte vesicles using found more sensitive aqueous buffer solution. However, presence vesicles, retarded differences between them became insignificant. Thus, lifetime might prolonged physiological fluids. interaction membranes appears important stabilization complexes. Meanwhile, structural changes proteins observed. observed attribute insulin-mimetic mechanisms toxicities.

参考文章(31)
Boyan Zhang, Li Ruan, Baowei Chen, Jinfen Lu, Kui Wang, Binding of vanadate to human erythrocyte ghosts and subsequent events. Biometals. ,vol. 10, pp. 291- 298 ,(1997) , 10.1023/A:1018324416694
Theodore L. Steck, Jeffrey A. Kant, Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes. Methods in Enzymology. ,vol. 31, pp. 172- 180 ,(1974) , 10.1016/0076-6879(74)31019-1
G R Willsky, D A White, B C McCabe, Metabolism of added orthovanadate to vanadyl and high-molecular-weight vanadates by Saccharomyces cerevisiae. Journal of Biological Chemistry. ,vol. 259, pp. 13273- 13281 ,(1984) , 10.1016/S0021-9258(18)90689-7
L.C. Cantley, P. Aisen, The fate of cytoplasmic vanadium. Implications on (NA,K)-ATPase inhibition. Journal of Biological Chemistry. ,vol. 254, pp. 1781- 1784 ,(1979) , 10.1016/S0021-9258(17)37721-9
Patrick Poucheret, Subodh Verma, Marc D. Grynpas, John H. McNeill, Vanadium and diabetes Molecular and Cellular Biochemistry. ,vol. 188, pp. 73- 80 ,(1998) , 10.1023/A:1006820522587
Debbie C Crans, Chemistry and insulin-like properties of vanadium(IV) and vanadium(V) compounds. Journal of Inorganic Biochemistry. ,vol. 80, pp. 123- 131 ,(2000) , 10.1016/S0162-0134(00)00048-9
P.S. Low, P. Rathinavelu, M.L. Harrison, Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3. Journal of Biological Chemistry. ,vol. 268, pp. 14627- 14631 ,(1993) , 10.1016/S0021-9258(18)82379-1
I. G. Fantus, G. Deragon, R. Lai, S. Tang, Modulation of insulin action by vanadate: evidence of a role for phosphotyrosine phosphatase activity to alter cellular signaling Molecular and Cellular Biochemistry. ,vol. 153, pp. 103- 112 ,(1995) , 10.1007/BF01075924
Bénédicte A Reul, Sean S Amin, Jean-Pierre Buchet, Lumbe N Ongemba, Debbie C Crans, Sonia M Brichard, Effects of vanadium complexes with organic ligands on glucose metabolism: a comparison study in diabetic rats British Journal of Pharmacology. ,vol. 126, pp. 467- 477 ,(1999) , 10.1038/SJ.BJP.0702311