Biochemical and biological aspects of protein thiolation in cells and plasma.

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 Signal

authors

Di Simplicio P,Frosali S,Priora R,Summa D,Cherubini Di Simplicio F,Di Giuseppe D,Di Stefano A

doi

10.1089/ars.2005.7.951

keywords:

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

951-63

issue

7-8

eissn

1523-0864

issn

1557-7716

journal_volume

7

pub_type

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