Serveur d'exploration sur la glutarédoxine

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PEP‑1‑glutaredoxin 1 protects against hippocampal neuronal cell damage from oxidative stress via regulation of MAPK and apoptotic signaling pathways.

Identifieur interne : 000238 ( Main/Exploration ); précédent : 000237; suivant : 000239

PEP‑1‑glutaredoxin 1 protects against hippocampal neuronal cell damage from oxidative stress via regulation of MAPK and apoptotic signaling pathways.

Auteurs : Eun Ji Ryu ; Dae Won Kim ; Min Jea Shin ; Hyo Sang Jo ; Jung Hwan Park ; Su Bin Cho ; Chi Hern Lee ; Hyeon Ji Yeo ; Eun Ji Yeo ; Yeon Joo Choi ; Duk-Soo Kim ; Sung-Woo Cho ; Yong-Jun Cho ; Eun Jeong Sohn ; Ora Son ; Keun Wook Lee ; Kyu Hyung Han ; Jinseu Park ; Won Sik Eum ; Soo Young Choi

Source :

RBID : pubmed:29916538

Descripteurs français

English descriptors

Abstract

Oxidative stress is known to be a primary risk factor for neuronal diseases. Glutaredoxin (GLRX)‑1, a redox‑regulator of the thioredoxin superfamily, is known to exhibit an important role in cell survival via various cellular functions. However, the precise roles of GLRX1 in brain ischemia are still not fully understood. The present study investigated whether transduced PEP‑1‑GLRX1 protein has protective effects against oxidative stress in cells and in an animal model. Transduced PEP‑1‑GLRX1 protein increased HT‑22 cell viability under oxidative stress and this fusion protein significantly reduced intracellular reactive oxygen species and levels of DNA damage. In addition, PEP‑1‑GLRX1 protein regulated RAC‑a serine/threonine‑protein kinase and mitogen‑activated protein kinase signaling, in addition to apoptotic signaling including B cell lymphoma (Bcl)‑2, Bcl‑2 associated X, apoptosis regulator, pro‑caspase‑9 and p53 expression levels. In an ischemic animal model, it was verified that PEP‑1‑GLRX1 transduced into the Cornu Ammonis 1 region of the animal brain, where it markedly protected against ischemic injury. These results indicate that PEP‑1‑GLRX1 attenuates neuronal cell death resulting from oxidative stress in vitro and in vivo. Therefore, PEP‑1‑GLRX1 may exhibit a beneficial role in the treatment of neuronal disorders, including ischemic injury.

DOI: 10.3892/mmr.2018.9176
PubMed: 29916538


Affiliations:


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Le document en format XML

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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Kim, Dae Won" sort="Kim, Dae Won" uniqKey="Kim D" first="Dae Won" last="Kim">Dae Won Kim</name>
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<nlm:affiliation>Department of Biochemistry and Molecular Biology, Research Institute of Oral Sciences, College of Dentistry, Gangneung‑Wonju National University, Gangneung, Gangwon 25457, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
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<name sortKey="Shin, Min Jea" sort="Shin, Min Jea" uniqKey="Shin M" first="Min Jea" last="Shin">Min Jea Shin</name>
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<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
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<name sortKey="Jo, Hyo Sang" sort="Jo, Hyo Sang" uniqKey="Jo H" first="Hyo Sang" last="Jo">Hyo Sang Jo</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
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<name sortKey="Park, Jung Hwan" sort="Park, Jung Hwan" uniqKey="Park J" first="Jung Hwan" last="Park">Jung Hwan Park</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
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<name sortKey="Cho, Su Bin" sort="Cho, Su Bin" uniqKey="Cho S" first="Su Bin" last="Cho">Su Bin Cho</name>
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<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Lee, Chi Hern" sort="Lee, Chi Hern" uniqKey="Lee C" first="Chi Hern" last="Lee">Chi Hern Lee</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Yeo, Eun Ji" sort="Yeo, Eun Ji" uniqKey="Yeo E" first="Eun Ji" last="Yeo">Eun Ji Yeo</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Choi, Yeon Joo" sort="Choi, Yeon Joo" uniqKey="Choi Y" first="Yeon Joo" last="Choi">Yeon Joo Choi</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Kim, Duk Soo" sort="Kim, Duk Soo" uniqKey="Kim D" first="Duk-Soo" last="Kim">Duk-Soo Kim</name>
<affiliation>
<nlm:affiliation>Department of Anatomy, College of Medicine, Soonchunhyang University, Cheonan‑Si, South Chungcheong 31538, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Cho, Sung Woo" sort="Cho, Sung Woo" uniqKey="Cho S" first="Sung-Woo" last="Cho">Sung-Woo Cho</name>
<affiliation>
<nlm:affiliation>Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine, Seoul 05505, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Cho, Yong Jun" sort="Cho, Yong Jun" uniqKey="Cho Y" first="Yong-Jun" last="Cho">Yong-Jun Cho</name>
<affiliation>
<nlm:affiliation>Department of Neurosurgery, Hallym University Medical Center, Chuncheon, Gangwon 24253, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Sohn, Eun Jeong" sort="Sohn, Eun Jeong" uniqKey="Sohn E" first="Eun Jeong" last="Sohn">Eun Jeong Sohn</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Son, Ora" sort="Son, Ora" uniqKey="Son O" first="Ora" last="Son">Ora Son</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<author>
<name sortKey="Lee, Keun Wook" sort="Lee, Keun Wook" uniqKey="Lee K" first="Keun Wook" last="Lee">Keun Wook Lee</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Han, Kyu Hyung" sort="Han, Kyu Hyung" uniqKey="Han K" first="Kyu Hyung" last="Han">Kyu Hyung Han</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<author>
<name sortKey="Park, Jinseu" sort="Park, Jinseu" uniqKey="Park J" first="Jinseu" last="Park">Jinseu Park</name>
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<nlm:affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</nlm:affiliation>
<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<name sortKey="Eum, Won Sik" sort="Eum, Won Sik" uniqKey="Eum W" first="Won Sik" last="Eum">Won Sik Eum</name>
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<wicri:noCountry code="subField">Republic of South Korea</wicri:noCountry>
</affiliation>
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<term>Animals (MeSH)</term>
<term>Brain Ischemia (drug therapy)</term>
<term>Brain Ischemia (metabolism)</term>
<term>Brain Ischemia (pathology)</term>
<term>Cell Line (MeSH)</term>
<term>Cysteamine (analogs & derivatives)</term>
<term>Cysteamine (pharmacology)</term>
<term>Glutaredoxins (pharmacology)</term>
<term>Hippocampus (metabolism)</term>
<term>Hippocampus (pathology)</term>
<term>MAP Kinase Signaling System (drug effects)</term>
<term>Mice (MeSH)</term>
<term>Neurons (metabolism)</term>
<term>Neurons (pathology)</term>
<term>Oxidative Stress (drug effects)</term>
<term>Peptides (pharmacology)</term>
</keywords>
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<term>Animaux (MeSH)</term>
<term>Encéphalopathie ischémique (anatomopathologie)</term>
<term>Encéphalopathie ischémique (métabolisme)</term>
<term>Encéphalopathie ischémique (traitement médicamenteux)</term>
<term>Glutarédoxines (pharmacologie)</term>
<term>Hippocampe (anatomopathologie)</term>
<term>Hippocampe (métabolisme)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Mercaptamine (analogues et dérivés)</term>
<term>Mercaptamine (pharmacologie)</term>
<term>Neurones (anatomopathologie)</term>
<term>Neurones (métabolisme)</term>
<term>Peptides (pharmacologie)</term>
<term>Souris (MeSH)</term>
<term>Stress oxydatif (effets des médicaments et des substances chimiques)</term>
<term>Système de signalisation des MAP kinases (effets des médicaments et des substances chimiques)</term>
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<term>Stress oxydatif</term>
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<term>Brain Ischemia</term>
<term>Hippocampus</term>
<term>Neurons</term>
</keywords>
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<term>Encéphalopathie ischémique</term>
<term>Hippocampe</term>
<term>Neurones</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en">
<term>Brain Ischemia</term>
<term>Hippocampus</term>
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<term>Glutarédoxines</term>
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<term>Peptides</term>
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<term>Cell Line</term>
<term>Mice</term>
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<div type="abstract" xml:lang="en">Oxidative stress is known to be a primary risk factor for neuronal diseases. Glutaredoxin (GLRX)‑1, a redox‑regulator of the thioredoxin superfamily, is known to exhibit an important role in cell survival via various cellular functions. However, the precise roles of GLRX1 in brain ischemia are still not fully understood. The present study investigated whether transduced PEP‑1‑GLRX1 protein has protective effects against oxidative stress in cells and in an animal model. Transduced PEP‑1‑GLRX1 protein increased HT‑22 cell viability under oxidative stress and this fusion protein significantly reduced intracellular reactive oxygen species and levels of DNA damage. In addition, PEP‑1‑GLRX1 protein regulated RAC‑a serine/threonine‑protein kinase and mitogen‑activated protein kinase signaling, in addition to apoptotic signaling including B cell lymphoma (Bcl)‑2, Bcl‑2 associated X, apoptosis regulator, pro‑caspase‑9 and p53 expression levels. In an ischemic animal model, it was verified that PEP‑1‑GLRX1 transduced into the Cornu Ammonis 1 region of the animal brain, where it markedly protected against ischemic injury. These results indicate that PEP‑1‑GLRX1 attenuates neuronal cell death resulting from oxidative stress in vitro and in vivo. Therefore, PEP‑1‑GLRX1 may exhibit a beneficial role in the treatment of neuronal disorders, including ischemic injury.</div>
</front>
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<DateCompleted>
<Year>2018</Year>
<Month>10</Month>
<Day>19</Day>
</DateCompleted>
<DateRevised>
<Year>2018</Year>
<Month>10</Month>
<Day>19</Day>
</DateRevised>
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<Journal>
<ISSN IssnType="Electronic">1791-3004</ISSN>
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<Volume>18</Volume>
<Issue>2</Issue>
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<Year>2018</Year>
<Month>Aug</Month>
</PubDate>
</JournalIssue>
<Title>Molecular medicine reports</Title>
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<ArticleTitle>PEP‑1‑glutaredoxin 1 protects against hippocampal neuronal cell damage from oxidative stress via regulation of MAPK and apoptotic signaling pathways.</ArticleTitle>
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<Abstract>
<AbstractText>Oxidative stress is known to be a primary risk factor for neuronal diseases. Glutaredoxin (GLRX)‑1, a redox‑regulator of the thioredoxin superfamily, is known to exhibit an important role in cell survival via various cellular functions. However, the precise roles of GLRX1 in brain ischemia are still not fully understood. The present study investigated whether transduced PEP‑1‑GLRX1 protein has protective effects against oxidative stress in cells and in an animal model. Transduced PEP‑1‑GLRX1 protein increased HT‑22 cell viability under oxidative stress and this fusion protein significantly reduced intracellular reactive oxygen species and levels of DNA damage. In addition, PEP‑1‑GLRX1 protein regulated RAC‑a serine/threonine‑protein kinase and mitogen‑activated protein kinase signaling, in addition to apoptotic signaling including B cell lymphoma (Bcl)‑2, Bcl‑2 associated X, apoptosis regulator, pro‑caspase‑9 and p53 expression levels. In an ischemic animal model, it was verified that PEP‑1‑GLRX1 transduced into the Cornu Ammonis 1 region of the animal brain, where it markedly protected against ischemic injury. These results indicate that PEP‑1‑GLRX1 attenuates neuronal cell death resulting from oxidative stress in vitro and in vivo. Therefore, PEP‑1‑GLRX1 may exhibit a beneficial role in the treatment of neuronal disorders, including ischemic injury.</AbstractText>
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<LastName>Ryu</LastName>
<ForeName>Eun Ji</ForeName>
<Initials>EJ</Initials>
<AffiliationInfo>
<Affiliation>Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chuncheon, Gangwon 24252, Republic of South Korea.</Affiliation>
</AffiliationInfo>
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<LastName>Kim</LastName>
<ForeName>Dae Won</ForeName>
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<Affiliation>Department of Biochemistry and Molecular Biology, Research Institute of Oral Sciences, College of Dentistry, Gangneung‑Wonju National University, Gangneung, Gangwon 25457, Republic of South Korea.</Affiliation>
</AffiliationInfo>
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<name sortKey="Lee, Chi Hern" sort="Lee, Chi Hern" uniqKey="Lee C" first="Chi Hern" last="Lee">Chi Hern Lee</name>
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<name sortKey="Park, Jung Hwan" sort="Park, Jung Hwan" uniqKey="Park J" first="Jung Hwan" last="Park">Jung Hwan Park</name>
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