Abstract:
:Plasma membranes isolated from K562 cells contain an NADH-ascorbate free radical reductase activity and intact cells show the capacity to reduce the rate of chemical oxidation of ascorbate leading to its stabilization at the extracellular space. Both activities are stimulated by CoQ10 and inhibited by capsaicin and dicumarol. A 34-kDa protein (p34) isolated from pig liver plasma membrane, displaying NADH-CoQ10 reductase activity and its internal sequence being identical to cytochrome b5 reductase, increases the NADH-ascorbate free radical reductase activity of K562 cells plasma membranes. Also, the incorporation of this protein into K562 cells by p34-reconstituted liposomes also increased the stabilization of ascorbate by these cells. TPA-induced differentiation of K562 cells increases ascorbate stabilization by whole cells and both NADH-ascorbate free radical reductase and CoQ10 content in isolated plasma membranes. We show here the role of CoQ10 and its NADH-dependent reductase in both plasma membrane NADH-ascorbate free radical reductase and ascorbate stabilization by K562 cells. These data support the idea that besides intracellular cytochrome b5-dependent ascorbate regeneration, the extracellular stabilization of ascorbate is mediated by CoQ10 and its NADH-dependent reductase.
journal_name
J Bioenerg Biomembrjournal_title
Journal of bioenergetics and biomembranesauthors
Gómez-Díaz C,Rodríguez-Aguilera JC,Barroso MP,Villalba JM,Navarro F,Crane FL,Navas Pdoi
10.1023/a:1022410127104subject
Has Abstractpub_date
1997-06-01 00:00:00pages
251-7issue
3eissn
0145-479Xissn
1573-6881journal_volume
29pub_type
杂志文章abstract::We have studied a mutant strain of Drosophila in which 80% of the mitochondrial DNA molecules have lost over 30% of their coding region through deletion. This deletion affects genes encoding five subunits of complex I of the respiratory chain (NADH:ubiquinone oxidoreductase). The enzymatic activity of complex I in the...
journal_title:Journal of bioenergetics and biomembranes
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abstract::Absorbance changes at 446 nm in purified cytochrome oxidase following flash photolysis of carboxy-oxidase poised in the mixed valance state at +220 mV show biphasic kinetics. One phase corresponds to CO recombination to ferrous cytochrome a3 with an energy of activation of 9 kcal/mol; the second phase is 3-5 times fas...
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abstract::Reaction of a dog kidney (Na + K)-ATPase with pyridoxal phosphate, followed by borohydride reduction, reduced the catalytic activity when measured subsequently. The time course of inactivation did not follow a first-order process, and certain characteristics of the residual enzymatic activity were modified. Moreover, ...
journal_title:Journal of bioenergetics and biomembranes
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