Rat as an animal model for studying glutaredoxin-5 gene.
Identifieur interne : 000227 ( Main/Exploration ); précédent : 000226; suivant : 000228Rat as an animal model for studying glutaredoxin-5 gene.
Auteurs : Ateeq Ashraf [Pakistan] ; Najeeb Ullah [Pakistan] ; Ghayyor Ahmad [Pakistan]Source :
- Pakistan journal of pharmaceutical sciences [ 1011-601X ] ; 2018.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Biologie informatique (MeSH), Fer (métabolisme), Foie (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Humains (MeSH), Ligands (MeSH), Modèles moléculaires (MeSH), Mâle (MeSH), Phylogenèse (MeSH), Rat Wistar (MeSH), Rats (MeSH), Régulation de l'expression des gènes (MeSH), Simulation numérique (MeSH), Sites de fixation (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines.
- génétique : Glutarédoxines.
- métabolisme : Fer, Foie.
- Animaux, Biologie informatique, Humains, Ligands, Modèles moléculaires, Mâle, Phylogenèse, Rat Wistar, Rats, Régulation de l'expression des gènes, Simulation numérique, Sites de fixation, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Binding Sites (MeSH), Computational Biology (MeSH), Computer Simulation (MeSH), Gene Expression Regulation (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Humans (MeSH), Iron (metabolism), Ligands (MeSH), Liver (metabolism), Male (MeSH), Models, Molecular (MeSH), Phylogeny (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Rats (MeSH), Rats, Wistar (MeSH).
- MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Iron.
- metabolism : Liver.
- Amino Acid Sequence, Animals, Binding Sites, Computational Biology, Computer Simulation, Gene Expression Regulation, Humans, Ligands, Male, Models, Molecular, Phylogeny, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Rats, Wistar.
Abstract
Glutaredoxin-5 (Grx5) is a mitochondrial monothiol, participating in iron-sulfur clusters' biogenesis. It directly maintains normal cytosolic and mitochondrial iron homeostasis, participates in erythropoiesis and oxidative stress sensing, and regulates the oxidative-stress-induced apoptosis. The current investigation involved various techniques to associate rat- and human-Grx5 genes. The rat Grx5 protein's 3D structure was predicted (C-score = _1.10) and its stereochemical qualities were validated, with 88.2% of amino-acid-residues in the favoured regions of "Ramachandran plot". Z-score (-5.93) also confirmed reliability of the model. Superimposition results demonstrated 93% resemblance, and COFACTOR server predicted 10 conserved ligand-binding-sites in rat- and human-Grx5. Upstream the ATG start site, 26 conserved and 26 aligned transcription factors' binding sites were identified, indicating resemblances in transcriptional regulation of the gene in two organisms. Rat liver also expressed Grx5, indicating Grx5's possible involvement in hepatic iron metabolism not only in housekeeping but in pathophysiological conditions as well. The investigation concluded that rat could logically be used to study the role of Grx5 during health and disease conditions, understanding of which might prove crucial for targeting Grx5 for managing various acute or chronic ironinduced oxidative stress conditions.
PubMed: 30033414
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Ashraf, Ateeq" sort="Ashraf, Ateeq" uniqKey="Ashraf A" first="Ateeq" last="Ashraf">Ateeq Ashraf</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Human Genetics & Molecular Biology, Division of Basic Medical Sciences, University of Health Sciences, Lahore, Pakistan.</nlm:affiliation>
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<term>Animals (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Computational Biology (MeSH)</term>
<term>Computer Simulation (MeSH)</term>
<term>Gene Expression Regulation (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Humans (MeSH)</term>
<term>Iron (metabolism)</term>
<term>Ligands (MeSH)</term>
<term>Liver (metabolism)</term>
<term>Male (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Rats (MeSH)</term>
<term>Rats, Wistar (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Biologie informatique (MeSH)</term>
<term>Fer (métabolisme)</term>
<term>Foie (métabolisme)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Humains (MeSH)</term>
<term>Ligands (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mâle (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Rat Wistar (MeSH)</term>
<term>Rats (MeSH)</term>
<term>Régulation de l'expression des gènes (MeSH)</term>
<term>Simulation numérique (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Liver</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term>
<term>Foie</term>
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<term>Binding Sites</term>
<term>Computational Biology</term>
<term>Computer Simulation</term>
<term>Gene Expression Regulation</term>
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<term>Ligands</term>
<term>Male</term>
<term>Models, Molecular</term>
<term>Phylogeny</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>Rats</term>
<term>Rats, Wistar</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Biologie informatique</term>
<term>Humains</term>
<term>Ligands</term>
<term>Modèles moléculaires</term>
<term>Mâle</term>
<term>Phylogenèse</term>
<term>Rat Wistar</term>
<term>Rats</term>
<term>Régulation de l'expression des gènes</term>
<term>Simulation numérique</term>
<term>Sites de fixation</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxin-5 (Grx5) is a mitochondrial monothiol, participating in iron-sulfur clusters' biogenesis. It directly maintains normal cytosolic and mitochondrial iron homeostasis, participates in erythropoiesis and oxidative stress sensing, and regulates the oxidative-stress-induced apoptosis. The current investigation involved various techniques to associate rat- and human-Grx5 genes. The rat Grx5 protein's 3D structure was predicted (C-score = _1.10) and its stereochemical qualities were validated, with 88.2% of amino-acid-residues in the favoured regions of "Ramachandran plot". Z-score (-5.93) also confirmed reliability of the model. Superimposition results demonstrated 93% resemblance, and COFACTOR server predicted 10 conserved ligand-binding-sites in rat- and human-Grx5. Upstream the ATG start site, 26 conserved and 26 aligned transcription factors' binding sites were identified, indicating resemblances in transcriptional regulation of the gene in two organisms. Rat liver also expressed Grx5, indicating Grx5's possible involvement in hepatic iron metabolism not only in housekeeping but in pathophysiological conditions as well. The investigation concluded that rat could logically be used to study the role of Grx5 during health and disease conditions, understanding of which might prove crucial for targeting Grx5 for managing various acute or chronic ironinduced oxidative stress conditions.</div>
</front>
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<Title>Pakistan journal of pharmaceutical sciences</Title>
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<ArticleTitle>Rat as an animal model for studying glutaredoxin-5 gene.</ArticleTitle>
<Pagination><MedlinePgn>1301-1310</MedlinePgn>
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<Abstract><AbstractText>Glutaredoxin-5 (Grx5) is a mitochondrial monothiol, participating in iron-sulfur clusters' biogenesis. It directly maintains normal cytosolic and mitochondrial iron homeostasis, participates in erythropoiesis and oxidative stress sensing, and regulates the oxidative-stress-induced apoptosis. The current investigation involved various techniques to associate rat- and human-Grx5 genes. The rat Grx5 protein's 3D structure was predicted (C-score = _1.10) and its stereochemical qualities were validated, with 88.2% of amino-acid-residues in the favoured regions of "Ramachandran plot". Z-score (-5.93) also confirmed reliability of the model. Superimposition results demonstrated 93% resemblance, and COFACTOR server predicted 10 conserved ligand-binding-sites in rat- and human-Grx5. Upstream the ATG start site, 26 conserved and 26 aligned transcription factors' binding sites were identified, indicating resemblances in transcriptional regulation of the gene in two organisms. Rat liver also expressed Grx5, indicating Grx5's possible involvement in hepatic iron metabolism not only in housekeeping but in pathophysiological conditions as well. The investigation concluded that rat could logically be used to study the role of Grx5 during health and disease conditions, understanding of which might prove crucial for targeting Grx5 for managing various acute or chronic ironinduced oxidative stress conditions.</AbstractText>
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