Modulation of cytosolic protein kinase C activity by ferricyanide: priming event seems transmembrane redox signalling

Malviya, Anant N.; Anglard, Patrick

doi:10.1016/0014-5793(86)81149-8

Cited by 17 publications

(5 citation statements)

References 18 publications

(9 reference statements)

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“…Induction of differentiation in HL-60 cells has been associated with transient changes in reductase activity (7). In other cells, activation of the redox system has been shown to modulate protein kinase C activity (8). These findings raise an interest in the role of the plasma membrane reductase in these cells and the mechanisms through which it operates.…”

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confidence: 99%

Ascorbate Stimulates Ferricyanide Reduction in HL-60 Cells through a Mechanism Distinct from the NADH-dependent Plasma Membrane Reductase

VanDuijn

Zee

VanSteveninck

et al. 1998

Journal of Biological Chemistry

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The impermeable oxidant ferricyanide is reduced by the plasma membrane redox system of HL-60 cells. The rate of reduction is strongly enhanced by ascorbate or dehydroascorbate. The aim of this study was to determine the mechanism by which ascorbate and dehydroascorbate accelerate ferricyanide reduction in HL-60 cells. Addition of ascorbate or dehydroascorbate to cells in the presence of ferricyanide led to the intracellular accumulation of ascorbate. Control experiments showed that extracellular ascorbate was rapidly converted to dehydroascorbate in the presence of ferricyanide. These data suggest that intracellular ascorbate originates from extracellular dehydroascorbate. Accumulation of ascorbate was prevented by inhibitors of dehydroascorbate transport into the cell. These compounds also strongly inhibited ascorbate-stimulated ferricyanide reduction in HL-60 cells. Thus, it is concluded that the stimulation of ferricyanide reduction is dependent on intracellular accumulation of ascorbate. Changing the ␣-tocopherol content of the cells had no effect on the ascorbate-stimulated ferricyanide reduction, showing that a nonenzymatic redox system utilizing ␣-tocopherol was not involved. p-Chloromercuribenzenesulfonic acid strongly affected ferricyanide reduction in the absence of ascorbate, whereas the stimulated reaction was much less responsive to this compound. Thus, it appears that at least two different membrane redox systems are operative in HL-60 cells, both capable of reducing ferricyanide, but through different mechanisms. The first system is the ferricyanide reductase, which uses NADH as its source for electrons, whereas the novel system proposed in this paper relies on ascorbate.

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confidence: 99%

Ascorbate Stimulates Ferricyanide Reduction in HL-60 Cells through a Mechanism Distinct from the NADH-dependent Plasma Membrane Reductase

VanDuijn

Zee

VanSteveninck

et al. 1998

Journal of Biological Chemistry

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“…Reactive oxygen species are involved in the induction of c-fos and c-myc expression (Shibanuma et al, 1988;Amstad et al, 1990;Cerutti, 1985) and in the regulation of nuclear factors and protein phosphorylation (Rao et al, 1993a;Malviya and Anglard, 1986;Abate et al, 1990;Toledano et al, 1993;Toledano and Leonard, 1991;Staal et al, 1990;Bauskin et al, 1991;Dartsch et al, 1990a;Dartsch et al, 1990b). Activation of NF-KB may be achieved not only by phosphorylation (Baeuerle et al, 1988;Henkel et al, 1993;Li and Sedivy, 1993) but also by H,O, treatment of cells (Schreck et al, 1992).…”

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confidence: 99%

Modulation of Activator Protein‐1 (AP‐1) Transcription Factor and Protein Kinase C by Hydrogen Peroxide and d‐α‐Tocopherol in Vascular Smooth Muscle Cells

Stäuble

Boscoboinik

Tasinato

et al. 1994

European Journal of Biochemistry

106

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The effects of hydrogen peroxide, D-a-tocopherol and of D-P-tocopherol on proliferation, protein kinase C and activator protein-1 (AP-1) activation have been studied in vascular smooth muscle cells. Cell proliferation, when activated by foetal calf serum, was inhibited by D-a-tocopherol. Protein kinase C activity was stimulated by hydrogen peroxide in a manner similar to phorbol myristate acetate; in the latter case, but not in the former, D-a-tocopherol inhibited the reaction. Hydrogen peroxide prevented phorbol-myristate-acetate-stimulated AP-1 binding to DNA but stimulated it if protein kinase C was down-regulated or inhibited. D-a-Tocopherol promoted AP-1 activation in quiescent cells but prevented its activation by phorbol myristate acetate.None of the described effects of D-a-tocopherol were shared by D-P-tocopherol, suggesting a non-antioxidant mechanism as the basis of its action. The data show that hydrogen peroxide and Da-tocopherol affect more than one element in the cell signal-transduction cascade.

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“…A regulatory role of intracellular pH has been found in procariotic cells, unrelated to the energetic function of the transtnetnbrane proton gtadient (Padan & Shuldiner, 1987 The network of interlinked processes underlaying the action of honnones at the cellular level also involves protein phosphotylation, as a mechanistn of signal atnplification, modulation and transfer (teviewed by . Data in anitnal cells suggest that cytosolic protein kinase C is modulated by intracellular pH (Malviya & Anglard 1986).…”

Section: Introductionmentioning

confidence: 99%

Microsome protein phosphorylation in Acer pseudoplatanus cells as influenced by intracellular alkalinization

Basso¹,

Rosa²,

Tognoli³

1989

Plant Cell & Environment

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Abstract. The authors have previously shown that cell treatments causing intra‐cellular alkalinization stimulate the in vivo phosphorylation of a 33‐K Dalton polypeptide (33 KP) (Tognoli & Basso, 1987). Here, the authors report that this polypeptide belongs to a protein associated with the microsomal membranes. They show that treatment of cells which induce intracellular alkalinization stimulate 33‐KP phosphorylation, whether the phosphorylation is performed in vivo (cells loaded with 32Pi before treatments) or in vitro (microsomes from control and treated cells, incubated with γ32P ATP). In both cases, 33 KP is phosphorylated on a serine residue. Microsomes do not show any phosphatase activity towards this phosphorylated protein, indicating involvement of a protein kinase reaction as an effector of changes induced by intracellular alkalinization. The number of phosphorylated sites or molecules of this protein increases as a result of intracellular alkalinization, suggesting that intracellular alkalinization causes topological or conformational modifications to a protein kinase or its substrate protein. The in vitro phosphorylation is not specifically influenced by the pH of the in vitro phosphorylation medium, suggesting that protein phosphorylation is not directly controlled by cytoplasmic pH.

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Modulation of cytosolic protein kinase C activity by ferricyanide: priming event seems transmembrane redox signalling

Cited by 17 publications

References 18 publications

Ascorbate Stimulates Ferricyanide Reduction in HL-60 Cells through a Mechanism Distinct from the NADH-dependent Plasma Membrane Reductase

Ascorbate Stimulates Ferricyanide Reduction in HL-60 Cells through a Mechanism Distinct from the NADH-dependent Plasma Membrane Reductase

Modulation of Activator Protein‐1 (AP‐1) Transcription Factor and Protein Kinase C by Hydrogen Peroxide and d‐α‐Tocopherol in Vascular Smooth Muscle Cells

Microsome protein phosphorylation in Acer pseudoplatanus cells as influenced by intracellular alkalinization

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