Characterization of the binding, kinetics, and redox stability of vanadium(IV) and vanadium(V) protein complexes in serum

Chasteen, N. Dennis; Grady, John K.; Holloway, Clive Ε.

doi:10.1021/ic00236a021

Cited by 163 publications

(152 citation statements)

References 4 publications

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“…Capillary electrophoresis confirmed the existence of two major binding sites for the oxovanadium(IV) cation, whereas VO 3 -has only a very weak binding affinity 41 , consistent with previous studies. 42 IR spectroscopic analysis showed that, as a consequence of the VO 2+ /HAS interaction, major structural changes are produced at the protein secondary structure. 41 In a recent comparative study of the binding of vanadate to HSA, human fresh frozen plasma and human transferrin, it was demonstrated that the binding capacity of HSA is about one thousandth of those of the other two systems.…”

Section: Transferrin and Serum Albumin Complexesmentioning

confidence: 99%

Model studies related to vanadium biochemistry: recent advances and perspectives

Baran¹

2003

J. Braz. Chem. Soc.

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Nos ultimos anos, vêm se acumulando as evidências sobre a necessidade de vanádio dos organismos mais evoluídos. Estudos de compostos modelos constituem-se numa importante ferramenta para o entendimento dos diferentes aspectos da bioquímica deste bioelemento. Neste artigo, apresentamos os resultados dos nossos estudos, assim como os de outros grupos de pesquisa, sobre compostos modelos relacionados a vários aspectos do metabolismo e detoxificação do vanádio e a haloperoxidasas dependentes do vanádio. São também apresentadas informações sobre as interações do cátion oxovanádio(IV), relevante do ponto de vista biológico, com bioligantes importantes, tais como nucleotideos, carboidratos, fosfatos e outros sistemas correlatos.Increasing evidence on the need of the higher forms of life for vanadium has accumulated during recent years. Model studies have become a very important tool to attain a better understanding of different aspects of the biochemistry of this bioelement. In this account we present the results of our own studies, as well as those of other research groups, on models related to different aspects of its metabolism and detoxification and to vanadium dependent haloperoxidases. Additional information about the interaction of the biologically relevant oxovanadium(IV) cation with important bioligands, such as nucleotides, carbohydrates, phosphates and related systems are also presented.

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Section: Transferrin and Serum Albumin Complexesmentioning

confidence: 99%

Model studies related to vanadium biochemistry: recent advances and perspectives

Baran¹

2003

J. Braz. Chem. Soc.

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“…The physiological effects of vanadium are commonly attributed to the vanadyl cation. However, some evidence suggests that vanadate may also exist intracellularly [38]. Since we have demonstrated that vanadate, in the monomeric, dimeric, tetrameric and pentameric oxoanions, has no effect on the activity of PKA, any direct in i o effects of vanadate on this enzyme would be mediated via the formation of VO# + .…”

Section: Figure 6 Molecular Structures Of Decavanadate (Top) and Vanamentioning

confidence: 80%

“…of 366p10 µM. However, in the light of the solution chemistry of vanadium(IV) in the neutral pH range [29,38], the concentration of free hydrated VO# + is significantly less than 366 µM, corresponding to a low micromolar or submicromolar affinity of this cation for PKA.…”

Section: Figure 6 Molecular Structures Of Decavanadate (Top) and Vanamentioning

confidence: 99%

Vanadium oxoanions and cAMP-dependent protein kinase: an anti-substrate inhibitor

Pluskey

Mahroof-Tahir

Crans

et al. 1997

Biochemical Journal

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Vanadium oxoions have been shown to elicit a wide range of effects in biological systems, including an increase in the quantity of phosphorylated proteins. This response has been attributed to the inhibition of protein phosphatases, the indirect activation of protein kinases via stimulation of enzymes at early steps in signal transduction pathways and/or the direct activation of protein kinases. We have evaluated the latter possibility by exploring the effects of vanadate, decavanadate and vanadyl cation species on the activity of the cAMP-dependent protein kinase (PKA), a serine/threonine kinase. Vanadate, in the form of monomer, dimer, tetramer and pentamer species, neither inhibits nor activates PKA. In marked contrast, decavanadate is a competitive inhibitor (Ki = 1.8ŷ0.1 mM) of kemptide (Leu-Arg-Arg-Ala-Ser-Leu-Gly), a peptide-based substrate. This inhibition pattern is especially surprising, since the negatively charged decavanadate would not be predicted to bind to the region of the active site of the enzyme that accommodates the positively charged kemptide substrate. Our studies suggest that decavanadate can associate with kemptide in solution, which would prevent kemptide from interacting with the enzyme. Vanadium(IV) also inhibits the PKA-catalysed phosphorylation of kemptide, but with an IC50 of 366ŷ10 ƁM. However, in this case V4+ appears to bind to the Mg2+-binding site, since it can substitute for Mg2+. In the absence of Mg2+, the optimal concentration of vanadium(IV) for the PKA-catalysed phosphorylation of kemptide is 100 ƁM, with concentrations above 100 ƁM being markedly inhibitory. However, even at the optimal 100 ƁM V4+ concentration, the Vmax and Km values (for kemptide) are significantly less favourable than those obtained in the presence of 100 ƁM Mg2+. In summary, we have found that oxovanadium ions can directly alter the activity of the serine/threonine-specific PKA.

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“…The concentrations of the protein solutions were estimated from their UV absorption: e 280nm (HSA) = 36850 M −1 cm −1 and e 280nm (apoTf) = 92300 M −1 cm −1 [28,29]. 2-(Nmorpholino)ethanesulfonic acid (MES), 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), Tris, N-cyclohexyl-2-aminoethanesulfonic acid (CHES) buffers and n-octanol were obtained from Sigma-Aldrich.…”

Section: Chemicalsmentioning

confidence: 99%

Interaction of folic acid and some matrix metalloproteinase (MMP) inhibitor folate-γ-hydroxamate derivatives with Zn(II) and human serum albumin

Enyedy

Farkas

Dömötör

et al. 2011

Journal of Inorganic Biochemistry

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Characterization of the binding, kinetics, and redox stability of vanadium(IV) and vanadium(V) protein complexes in serum

Cited by 163 publications

References 4 publications

Model studies related to vanadium biochemistry: recent advances and perspectives

Model studies related to vanadium biochemistry: recent advances and perspectives

Vanadium oxoanions and cAMP-dependent protein kinase: an anti-substrate inhibitor

Interaction of folic acid and some matrix metalloproteinase (MMP) inhibitor folate-γ-hydroxamate derivatives with Zn(II) and human serum albumin

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