Modulation of the mitochondrial voltage-dependent anion channel (VDAC) by hydrogen peroxide and its recovery by curcumin

Malik, C. P.; Ghosh, Subhendu

doi:10.1007/s00249-020-01469-2

Cited by 12 publications

(8 citation statements)

References 63 publications

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“…Mitochondria are the sites where H 2 O 2 is produced, 26 which has been fully confirmed. Excessive production of H 2 O 2 is toxic to cells and causes oxidative stress 27 . In this study, the H 2 O 2 content was increased in the OSO‐exposed lactating rats.…”

Section: Discussionmentioning

confidence: 50%

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Maternal oxidized soybean oil exposure in rats during lactation damages offspring kidneys via Nrf2/HO‐1 and NF‐κB signaling pathway

Gao

Wang

et al. 2021

J Sci Food Agric

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BACKGROUND Cooking oil is an indispensable component of the human diet. However, oils usually undergo thermal oxidation. Oxidized soybean oil (OSO) has been shown to have detrimental effects on humans and has emerged as a root cause of many chronic diseases. The objective of this work was to evaluate the effects of puerpera exposure to OSO on kidney damage in the mother and offspring using lactating rats as an experimental model. RESULTS Pathological sections and ultrastructure showed that OSO exposure resulted in various levels of damage to lactating rats and their offspring. OSO induced oxidative stress in the kidneys of lactating rats, as evidenced by increased levels of hydrogen peroxide, interleukin (IL)‐1β, and IL‐8. OSO increased the activities of glutathione peroxidase and superoxide dismutase. OSO upregulated the expression of apoptosis‐related genes, nuclear factor‐erythroid 2‐related factor 2 (Nrf2), and nuclear factor κB‐related inflammatory factor genes. In the offspring of the OSO‐exposed mothers, hydrogen peroxide, malondialdehyde, IL‐6, and tumor necrosis factor‐alpha contents were increased. Furthermore, OSO enhanced the levels of Nrf2, NAD(P)H quinone oxidoreductase 1, heme oxygenase 1, and p65 and decreased B‐cell lymphoma 2. CONCLUSION These findings indicated that the kidneys of two generations of rats were compromised by oxidative damage when fed OSO during lactation. This study provides evidence for increasing the genes expression of the Nrf2/heme oxygenase 1 pathway to alleviate the kidney damage caused by OSO in the mother and offspring. © 2021 Society of Chemical Industry.

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Section: Discussionmentioning

confidence: 50%

“…Excessive production of H 2 O 2 is toxic to cells and causes oxidative stress. 27 In this study, the H 2 O 2 content was increased in the OSO-exposed lactating rats. Therefore, we suspected that excessive H 2 O 2 production might be associated with mitochondrial damage.…”

Section: Wileyonlinelibrarycom/jsfamentioning

confidence: 49%

Maternal oxidized soybean oil exposure in rats during lactation damages offspring kidneys via Nrf2/HO‐1 and NF‐κB signaling pathway

Gao

Wang

et al. 2021

J Sci Food Agric

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“…On the contrary, recombinant hVDAC3 has been reported to form a relatively small conductance channel in the bilayer lipid membrane (BLM) . The gating properties of VDAC1 depend on the membrane potential, interaction with various metabolites, and ligands, such as Bax and Bid, , plasminogen, mercuric chloride, quinidine, and hydrogen peroxide, and post-translational modifications by enzymes, − e.g., protein kinase A , and mitogen-activated protein (MAP) kinases. ,,, Moreover, VDAC1 is one of the primary regulators of OMM permeability, mediating cytochrome c release, where critical mitochondrial Ca 2+ concentration is an essential determinant of a cell’s response to apoptotic signals …”

Section: Introductionmentioning

confidence: 99%

Calmodulin Modulates the Gating Properties of Voltage-Dependent Anion Channel from Rat Brain Mitochondria

et al. 2022

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Calmodulin (CaM) is a key signaling protein that plays a decisive role in mitochondrial Ca2+ homeostasis and signaling and modulates the mitochondrial membrane properties. We propose that voltage-dependent anion channel 1 (VDAC1), one of the most abundant outer mitochondrial membrane (OMM) proteins, could be its possible target or site of action. VDAC1 is known to play a crucial role in the mitochondrial Ca2+ signaling mechanism. Bilayer electrophysiology experiments show that CaM significantly reduces VDAC1’s conductivity and modulates its gating as well as permeability properties. Also, spectrofluorimetric analysis indicates the possibility of binding CaM with VDAC1. Theoretical analysis of fluorescence data shows that the aforementioned protein–protein interaction is not linear, but rather it is a complex nonlinear process. In VDAC1, CaM binding site has been predicted using various bioinformatics tools. It is proposed that CaM could interact with VDAC1’s outer-loop region and regulate its gating properties. Our findings suggest that VDAC1–CaM interaction could play a crucial role in the transport of ions and metabolites through the OMM and the regulation of the mitochondrial Ca2+ signaling mechanism through alteration of VDAC1’s gating and conductive properties.

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“…The conductance of VDAC was shown to increase upon H 2 O 2 treatment, and its activity was restored by curcumin. The binding site of H 2 O 2 on the channel identified through in silico molecular docking indicates a possibility of direct interaction between VDAC and H 2 O 2 ( Malik and Ghosh, 2020 ). Leaf extracts (aqueous-methanolic) from Centella asiatica (CA) quench ROS during ischemia-reperfusion injury by protecting N2a cells due to antioxidant property.…”

Section: Chemical Compounds: Interactional Influences Imentioning

confidence: 99%

VDACs: An Outlook on Biochemical Regulation and Function in Animal and Plant Systems

et al. 2021

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The voltage-dependent anion channels (VDACs) are the most abundant proteins present on the outer mitochondrial membrane. They serve a myriad of functions ranging from energy and metabolite exchange to highly debatable roles in apoptosis. Their role in molecular transport puts them on the center stage as communicators between cytoplasmic and mitochondrial signaling events. Beyond their general role as interchangeable pores, members of this family may exhibit specific functions. Even after nearly five decades of their discovery, their role in plant systems is still a new and rapidly emerging field. The information on biochemical regulation of VDACs is limited. Various interacting proteins and post-translational modifications (PTMs) modulate VDAC functions, amongst these, phosphorylation is quite noticeable. In this review, we have tried to give a glimpse of the recent advancements in the biochemical/interactional regulation of plant VDACs. We also cover a critical analysis on the importance of PTMs in the functional regulation of VDACs. Besides, the review also encompasses numerous studies which can identify VDACs as a connecting link between Ca2+ and reactive oxygen species signaling in special reference to the plant systems.

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Modulation of the mitochondrial voltage-dependent anion channel (VDAC) by hydrogen peroxide and its recovery by curcumin

Cited by 12 publications

References 63 publications

Maternal oxidized soybean oil exposure in rats during lactation damages offspring kidneys via Nrf2/HO‐1 and NF‐κB signaling pathway

Maternal oxidized soybean oil exposure in rats during lactation damages offspring kidneys via Nrf2/HO‐1 and NF‐κB signaling pathway

Calmodulin Modulates the Gating Properties of Voltage-Dependent Anion Channel from Rat Brain Mitochondria

VDACs: An Outlook on Biochemical Regulation and Function in Animal and Plant Systems

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