Identification and characterisation of the anti-oxidative stress properties of the lamprey prohibitin 2 gene
The highly conserved protein prohibitin 2 (PHB2) has been implicated as a cell-surface receptor in the regulation of proliferation, apoptosis, transcription, and mitochondrial protein folding. In the present study, we identified a Lampetra morii homologue of PHB2, Lm-PHB2, showing greater than 61.8% sequence identity with its homologues. Phylogenetic analysis indicated that the position of Lm-PHB2 is consistent with lamprey phylogeny. Expression of the Lm-PHB2 protein was nearly equivalent in the heart, liver, kidneys, intestines, and muscles of normal lampreys. However, the Lm-PHB2 protein was down-regulated in the myocardia of lampreys challenged for 5 days with adriamycin (Adr), followed by a significant up-regulation 10 days after treatment. In vitro, recombinant Lm-PHB2 (rLm-PHB2) protein could significantly enhance the H2O2-induced oxidative stress tolerance in Chang liver (CHL) cells. Further mechanism studies indicated that the nucleus-to-mitochondria translocation of Lm-PHB2 was closely involved in the oxidative stress protection. Our results suggests that the strategies to modulate Lm-PHB2 levels may constitute a novel therapeutic approach for myocardial injury and liver inflammatory diseases, conditions in which oxidative stress plays a critical role in tissue injury and inflammation..
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Artikel |
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Erscheinungsjahr: |
2015 |
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Erschienen: |
2015 |
Enthalten in: |
Zur Gesamtaufnahme - volume:42 |
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Enthalten in: |
Fish & shellfish immunology - 42(2015), 2, Seite 447-456 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Li, Tiesong [VerfasserIn] |
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Links: |
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doi: |
10.1016/j.fsi.2014.11.016 |
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funding: |
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PPN (Katalog-ID): |
OLC1958885169 |
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520 | |a The highly conserved protein prohibitin 2 (PHB2) has been implicated as a cell-surface receptor in the regulation of proliferation, apoptosis, transcription, and mitochondrial protein folding. In the present study, we identified a Lampetra morii homologue of PHB2, Lm-PHB2, showing greater than 61.8% sequence identity with its homologues. Phylogenetic analysis indicated that the position of Lm-PHB2 is consistent with lamprey phylogeny. Expression of the Lm-PHB2 protein was nearly equivalent in the heart, liver, kidneys, intestines, and muscles of normal lampreys. However, the Lm-PHB2 protein was down-regulated in the myocardia of lampreys challenged for 5 days with adriamycin (Adr), followed by a significant up-regulation 10 days after treatment. In vitro, recombinant Lm-PHB2 (rLm-PHB2) protein could significantly enhance the H2O2-induced oxidative stress tolerance in Chang liver (CHL) cells. Further mechanism studies indicated that the nucleus-to-mitochondria translocation of Lm-PHB2 was closely involved in the oxidative stress protection. Our results suggests that the strategies to modulate Lm-PHB2 levels may constitute a novel therapeutic approach for myocardial injury and liver inflammatory diseases, conditions in which oxidative stress plays a critical role in tissue injury and inflammation. | ||
540 | |a Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. | ||
650 | 4 | |a DNA, Complementary - metabolism | |
650 | 4 | |a Fish Proteins - metabolism | |
650 | 4 | |a Sequence Alignment - veterinary | |
650 | 4 | |a Repressor Proteins - metabolism | |
650 | 4 | |a Fish Proteins - genetics | |
650 | 4 | |a Lampreys - genetics | |
650 | 4 | |a Repressor Proteins - genetics | |
650 | 4 | |a Lampreys - metabolism | |
650 | 4 | |a Hydrogen Peroxide - pharmacology | |
650 | 4 | |a Gene Expression Regulation - drug effects | |
650 | 4 | |a Lampreys - immunology | |
650 | 4 | |a RNA, Messenger - metabolism | |
650 | 4 | |a Real-Time Polymerase Chain Reaction - veterinary | |
650 | 4 | |a Oxidative Stress - drug effects | |
650 | 4 | |a RNA, Messenger - genetics | |
650 | 4 | |a DNA, Complementary - genetics | |
700 | 1 | |a Wang, Ying |4 oth | |
700 | 1 | |a Gao, Yang |4 oth | |
700 | 1 | |a Li, Qingwei |4 oth | |
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