Abstract:
:Protein thiolation is elicited by oxidation by different mechanisms and is involved in a variety of biological processes. Thiols, protein SH (PSH) and non-protein SH groups (NPSH, namely GSH), are in competition in all biological environments in the regulation of oxidant homeostasis because oxidants thiolate proteins, whereas GSH dethiolates them (e.g., GSSG + PSH --> GSSP + GSH). Although poorly investigated, the elimination of disulfides from thiolated proteins to regenerate critical PSH is important. These aspects are poorly known in cells, where glutaredoxin and peroxiredoxin operate as enzymes or potential chaperones to accelerate dethiolation. On the contrary, studies with plasma or albumin have highlighted the importance of protein conformation in dethiolation processes and have clarified the reason why homocysteine (thiol with potential toxicity) is preferentially bound to albumin as protein-thiol mixed disulfide with respect to other NPSH. Here we provide an overview of protein thiolation/dethiolation processes, with an emphasis on recent developments and future perspectives in this field.
journal_name
Antioxid Redox Signaljournal_title
Antioxidants & redox signalingauthors
Di Simplicio P,Frosali S,Priora R,Summa D,Cherubini Di Simplicio F,Di Giuseppe D,Di Stefano Adoi
10.1089/ars.2005.7.951keywords:
subject
Has Abstractpub_date
2005-07-01 00:00:00pages
951-63issue
7-8eissn
1523-0864issn
1557-7716journal_volume
7pub_type
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