Mechanism of Oxidative Damage of Dog Kidney Na/K–ATPase

Boldyrev, Alexander A.; Kurella, Ekaterina G.

doi:10.1006/bbrc.1996.0770

Cited by 41 publications

(20 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In opossum kidney cells Na + ,K + -ATPase activity is inhibited by acute incubation with 500 mM of hydrogen peroxide (unpublished results). This finding is in accordance with the works performed by Boldyrev et al (Boldyrev & Kurella, 1996) addressed at studying the kinetic parameters of the Na + ,K + -ATPase after its partial inhibition by hydrogen peroxide. They used hydrogen peroxide in the mM concentration range and suggest that oxidized SH-groups of Na + ,K + -ATPase interfered with the capacity of the enzyme to form active oligomers which are essential for higher Na + ,K + -ATPase activity ( Figure 5).…”

Section: Redox Balance and Renal Nasupporting

confidence: 93%

Renal Redox Balance and Na+, K+-ATPase Regulation: Role in Physiology and Pathophysiology

Silva¹,

Soares‐da‐Silva²

2012

Oxidative Stress - Molecular Mechanisms and Biological Effects

View full text Add to dashboard Cite

Section: Redox Balance and Renal Nasupporting

confidence: 93%

Renal Redox Balance and Na+, K+-ATPase Regulation: Role in Physiology and Pathophysiology

Silva¹,

Soares‐da‐Silva²

2012

Oxidative Stress - Molecular Mechanisms and Biological Effects

View full text Add to dashboard Cite

“…One of the targets of ROS accumulated in neuronal cells is the Na + /K + -activated ATPase (Huang et al, 1992;Boldyrev and Kurella, 1996;Boldyrev et al, 2003) which generates ionic asymmetry across the plasma cell membrane, a feature which is especially important for excitable cells. Under normal conditions, the neuronal Na + /K + -pump consumes from 15% to 40% of cell energy to support ionic gradients.…”

mentioning

confidence: 99%

Glutamate receptors modulate oxidative stress in neuronal cells. A mini-review

2004

View full text Add to dashboard Cite

Multiple lines of evidence demonstrate that reactive oxygen species (ROS) are involved in regulation of normal cell metabolism as second messengers. Under extreme conditions, these molecules induce oxidative stress, which may stimulate (or accompany) a number of neurodegenerative processes. In the glutamatergic system, ROS levels are under control of ionotropic and metabotropic glutamate receptors, which modulate ion fluxes through the neuronal membrane. The Na+/K(+)-pump is also one of the important participants affecting stationary ROS levels through several distinct mechanisms. This review describes the involvement of the Na+/K(+)-pump in intracellular signaling mechanisms via cross-talk between the pump and glutamate receptors in cerebellum granule cells. Selective dysfunction of mGlu II receptors may also lead to abnormal protein phosphorylation (i.e., tau phosphorylation), culminating in neurodegenerative disorders (i.e., Alzheimer disease). Also, unregulated production of intracellular ROS resulting from an imbalance of ionotropic and metabotropic receptors may activate one or more protein kinases. In summary, Glu receptor dysfunction, leading to a deficit in glutamate-mediated signal transduction may represent one of the earliest stages of neurodegenerative disorders. The Na+/K(+)-pump is able to prevent over-production of intracellular ROS, thus increasing oxidative stability of neuronal cells.

show abstract

“…Apart from the photodynamic generation of singlet oxygen (Vinnikova, Kukreja & Hess, 1992, Penning et al, 1994Ishibashi, Lee & Okabe 1996), Fenton or Fenton-like reactions were frequently used (Mishra et al, 1989;Thomas & Reed, 1990;Chen et al, 1992;Rohn, Hinds & Vincenzi, 1993Huang et al, 1994;Shao et al, 1995). Alternatively, the enzymes were exposed to various reactive oxygen species such as the superoxide anion generated by xanthine oxidase (Elmoselhi et al, 1994), to hydrogen peroxide (Boldyrev & Kurella, 1996), to hypochlorous acid (Kato et al, 1998) or to free radicals of water radiolysis (Hitschke et al, 1994;Mense, Stark & Apell, 1997).…”

Section: Introductionmentioning

confidence: 99%

Photodynamic Inactivation of the Na,K-ATPase Occurs via Different Pathways

2004

View full text Add to dashboard Cite

Abstract. The photodynamic, i.e., the light-induced, inactivation of the Na,K-ATPase in the presence of the sensitizer rose bengal was studied under different conditions. The shape of inactivation curves of the enzyme activity was analyzed as well as partial reactions of the pump cycle. Both experimental approaches showed the existence of two different time constants of inactivation of the ion pump, which reflect two pathways of a photodynamic modification. This is supported by the following observations: (1) The amplitude of the initial fast decay of enzyme activity was enhanced in the presence of D 2 O and reduced in the presence of the singlet oxygen scavenger imidazole. (Similar results were found for the SR Ca-ATPase.) (2) Contrary to the fast enzyme inactivation the slow process shows an inverse doserate behavior. (3) Inactivation of the partial reactions of Na + -binding and of K + -binding to the membrane domain of the Na,K-ATPase showed only a single time constant, which corresponded to the slower time constant of enzyme inactivation. In the presence of high concentrations of singlet oxygen the fast time constant dominated the inactivation of the ATP-induced partial reaction for which the cytoplasmic domains of the enzyme play an important role. The data support the conclusion that fast inactivation is due to modification of the cytoplasmic domains and slow inactivation due to modifications of the membrane domain of the ion pumps.

show abstract

Mechanism of Oxidative Damage of Dog Kidney Na/K–ATPase

Cited by 41 publications

References 0 publications

Renal Redox Balance and Na+, K+-ATPase Regulation: Role in Physiology and Pathophysiology

Renal Redox Balance and Na+, K+-ATPase Regulation: Role in Physiology and Pathophysiology

Glutamate receptors modulate oxidative stress in neuronal cells. A mini-review

Photodynamic Inactivation of the Na,K-ATPase Occurs via Different Pathways

Contact Info

Product

Resources

About