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Pak J Pharm Sci ; 31(4): 1301-1310, 2018 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-30033414

RESUMO

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.


Assuntos
Regulação da Expressão Gênica , Glutarredoxinas/química , Glutarredoxinas/genética , Ferro/metabolismo , Fígado/metabolismo , Sequência de Aminoácidos , Animais , Sítios de Ligação , Biologia Computacional , Simulação por Computador , Humanos , Ligantes , Masculino , Modelos Moleculares , Filogenia , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Ratos , Ratos Wistar
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