Abstract:
:Glutathione (GSH or reduced glutathione) is a tripeptide of gamma-Glutamyl-cysteinylglycine and the predominant intracellular antioxidant in many organisms including humans. GSH and associated enzymes are controlled by a transcription factor-nuclear factor-2 related erythroid factor-2 (Nrf2). In cellular milieu, GSH protects the cells essentially against a wide variety of free radicals including reactive oxygen species, lipid hydroperoxides, xenobiotic toxicants, and heavy metals. It has two forms, the reduced form or reduced glutathione (GSH) and oxidized form (GSSG), where two GSH moieties combine by sulfhydryl bonds. Glutathione peroxidase (GPx) and glutathione-s-transferase (GST) essentially perform the detoxification reactions using GSH, converting it into GSSG. Glutathione reductase (GR) operates the salvage pathway by converting GSSG to GSH with the expense of NADPH and restores the cellular GSH pool. Hence, GSH and GSH-dependent enzymes are necessary for maintaining the normal redox balance in the body and help in cell survival under stress conditions. In addition, GST removes various carcinogenic compounds offering a chemopreventive property, whereas the GSH system plays a significant role in regulating the cellular survival by offering redox stability in a variety of cancers including prostate, lung, breast, and colon cancer. Studies have also indicated that GSH inhibitors, such as buthionine sulfoximine, improve the chemo-sensitivity in cancer cells. In addition, GSH and dependent enzymes provide a survival advantage for cancer cells against chemotherapeutic drugs and radiotherapy.
journal_name
Curr Protein Pept Scijournal_title
Current protein & peptide scienceauthors
Narayanankutty A,Job JT,Narayanankutty Vdoi
10.2174/1389203720666190206130003subject
Has Abstractpub_date
2019-01-01 00:00:00pages
907-917issue
9eissn
1389-2037issn
1875-5550pii
CPPS-EPUB-96394journal_volume
20pub_type
杂志文章abstract::While the crucial role of intrinsically disordered proteins (IDPs) in the cell cycle is now recognized, deciphering their molecular mode of action at the structural level still remains highly challenging and requires a combination of many biophysical approaches. Among them, small angle X-ray scattering (SAXS) has been...
journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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abstract::The majority of tRNA studies has focused on tRNA molecules as pivotal player in the fundamental process of protein synthesis. Mounting studies have unveiled further functions for tRNA beyond protein synthesis, including non-ribosomal amino acid transfer, and regulation of targeted proteolysis. Post-translational N-ter...
journal_title:Current protein & peptide science
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abstract::Tribbles homolog 3 (TRIB3) is a mammalian gene that is upregulated in response to several types of cell death-inducing cellular stress. The TRIB3 protein is a pseudokinase, a protein kinase-like scaffold with impaired catalytic activity. However, research has revealed it to be prolific at forming protein- protein inte...
journal_title:Current protein & peptide science
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