Oxidative damage and reduction of redox factor-1 expression after transient spinal cord ischemia in rabbits

Sakurai, Masahiro; Nagata, Tetsuya; Abe, Kōji; Horinouchi, Takashi; Itoyama, Yasuto; Tabayashi, Koichi

doi:10.1067/mva.2003.100

Cited by 46 publications

(32 citation statements)

References 32 publications

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“…APE1 is highly expressed in selected regions of the central nervous system (99,100,142). A reduction in APE1 expression, followed by an increase in the apoptotic rate, occurs in the hippocampus after a hypoxic-ischemic injury (41), in the cortex after compression injury (79), and in the spinal cord after ischemia (116). The hippocampus of patients with Alzheimer shows an increased expression of APE1 levels in senile plaques and plaque-like structures (123).…”

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confidence: 99%

The Many Functions of APE1/Ref-1: Not Only a DNA Repair Enzyme

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Quadrifoglio

Tiribelli

et al. 2009

Antioxidants & Redox Signaling

442

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APE1/Ref-1 (APE1), the mammalian ortholog of Escherichia coli Xth, and a multifunctional protein possessing both DNA repair and transcriptional regulatory activities, has a pleiotropic role in controlling cellular response to oxidative stress. APE1 is the main apurinic/apyrimidinic endonuclease in eukaryotic cells, playing a central role in the DNA base excision repair pathway of all DNA lesions (uracil, alkylated and oxidized, and abasic sites), including single-strand breaks, and has also cotranscriptional activity by modulating genes expression directly regulated by either ubiquitous (i.e., AP-1, Egr-1, NF-B, p53, and HIF) and tissue specific (i.e., PEBP-2, Pax-5 and -8, and TTF-1) transcription factors. In addition, it controls the intracellular redox state by inhibiting the reactive oxygen species (ROS) production. At present, information is still inadequate regarding the molecular mechanisms responsible for the coordinated control of its several activities. Both expression and/or subcellular localization are altered in several metabolic and proliferative disorders such as in tumors and aging. Here, we have attempted to coalesce the most relevant information concerning APE1's different functions in order to shed new light and to focus current and future studies to fully understand this unique molecule that is acquiring more and more interest and translational relevance in the field of molecular medicine. Antioxid. Redox Signal. 11,[601][602][603][604][605][606][607][608][609][610][611][612][613][614][615][616][617][618][619]

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confidence: 99%

The Many Functions of APE1/Ref-1: Not Only a DNA Repair Enzyme

Tell

Quadrifoglio

Tiribelli

et al. 2009

Antioxidants & Redox Signaling

442

412

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“…Free radicals can induce lipid peroxidation in neuronal and glial cell membranes resulting in the production of 4-hydroxy-2-nonenal (4-HNE; Chan et al 1985;Lee et al 2003). In addition, ROS can directly cause DNA damage in neuronal and glial cells resulting in the production of 8-hydroxy-2 0 -deoxyguanosine (8-OHdG; Won et al 2001;Sakurai et al 2003). These cascades in membrane peroxidation and DNA damage can induce apoptotic neuronal and glial cell death, which can be detected as immunopositive single-stranded DNA (ssDNA), and neuronal dysfunction (Chan et al 1985;Lee et al 2003).…”

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confidence: 98%

(−)-Epigallocatechin-3-gallate Protects Against Neuronal Cell Death and Improves Cerebral Function After Traumatic Brain Injury in Rats

et al. 2011

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A major component of green tea, a widely consumed beverage, is (-)-epigallocatechin gallate (EGCG), which has strong antioxidant properties. Our previous study has indicated that free radical production following rat traumatic brain injury (TBI) induces neural degeneration. In this study, we investigated the effects of EGCG on cerebral function and morphology following TBI. Six-week-old male Wistar rats that had access to normal drinking water, or water containing 0.1% (w/v) EGCG ad libitum, received TBI with a pneumatic controlled injury device at 10 weeks of age. Immunohistochemistry and lipid peroxidation studies revealed that at 1, 3 and 7 days post-TBI, the number of 8-hydroxy-2'-deoxyguanosine-, 4-hydroxy-2-nonenal- and single-stranded DNA (ssDNA)-positive cells, and the levels of malondialdehyde (MDA) around the damaged area after TBI, significantly decreased in the EGCG treatment group compared with the water group (P < 0.05). Most ssDNA-positive cells in the water group co-localized with neuronal cells. However, in the EGCG treatment group, few ssDNA-positive cells co-localized with neurons. In addition, there was a significant increase in the number of surviving neuronal cells and an improvement in cerebral dysfunction after TBI in the EGCG treatment group compared with the water group (P < 0.05). These results indicate that consumption of water containing EGCG pre- and post-TBI inhibits free radical-induced neuronal degeneration and apoptotic cell death around the damaged area, resulting in the improvement of cerebral function following TBI. In summary, consumption of green tea may be an effective therapy for TBI patients.

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“…Ape1/Ref-1 is highly expressed in selected regions of the central nervous system (68,95). A reduction in Ape1/ Ref-1 expression occurs in the hippocampus after hypoxicischemic injury (93), in the cortex after compression injury (49), and in the spinal cord after ischemia (76 (17,66,83). Thus, Ape1/Ref-1 has been implicated in tumor progression, and Ape1/Ref-1 dysfunction may contribute to development of neurodegenerative disease.…”

mentioning

confidence: 99%

Ape1/Ref-1 Induces Glial Cell-Derived Neurotropic Factor (GDNF) Responsiveness by Upregulating GDNF Receptor α1 Expression

Kim

Acharya

et al. 2009

Molecular and Cellular Biology

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The major human apurinic and apyrimidinic (AP) endonuclease 1 Ape1 (also known as Redox factor 1 [Ref-1]), which is homologous to Escherichia coli exonuclease III, plays a key role in both short-patch and long-patch base excision repair (20,40). It cleaves the AP sites in DNA and allows them to be repaired by other enzymes involved in base excision repair (16,23,24). The AP sites can be formed by chemical hydrolysis, the oxygen metabolism, ionizing radiation, UV irradiation, alkylating agents, or oxidizing agents (16,53). In addition, AP sites can also arise spontaneously, where it has been estimated that 20,000 purine samples and 500 pyrimidines are lost in each 24-h cell cycle in human cells (52). The presence of AP sites blocks DNA replication, leading to DNA breakage, mutagenicity, and cytotoxicity. Ape1/Ref-1 contributes to more than 95% of the total cellular AP site-specific activity (12), which is consistent with Ape1/Ref-1 being essential for maintaining the genomic stability. (32,35,73). Studies have reported elevated Ape1/Ref-1 levels or altered subcellular localization in various types of cancers, such as epithelial ovarian cancers, cervical cancers, prostate cell tumors, melanoma, gliomas, rhabdomyosarcoma, and germ cell tumors, which are associated with tumor resistance and progression (7,21,22,43,74,99,100). Ape1/Ref-1 is highly expressed in selected regions of the central nervous system (68,95). A reduction in Ape1/ Ref-1 expression occurs in the hippocampus after hypoxicischemic injury (93), in the cortex after compression injury (49), and in the spinal cord after ischemia (76). In addition,

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Oxidative damage and reduction of redox factor-1 expression after transient spinal cord ischemia in rabbits

Cited by 46 publications

References 32 publications

The Many Functions of APE1/Ref-1: Not Only a DNA Repair Enzyme

The Many Functions of APE1/Ref-1: Not Only a DNA Repair Enzyme

(−)-Epigallocatechin-3-gallate Protects Against Neuronal Cell Death and Improves Cerebral Function After Traumatic Brain Injury in Rats

Ape1/Ref-1 Induces Glial Cell-Derived Neurotropic Factor (GDNF) Responsiveness by Upregulating GDNF Receptor α1 Expression

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