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

Biochemical and biological aspects of protein thiolation in cells and plasma.
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细胞和血浆中蛋白质硫醇化的生化和生物学方面。

DOI:
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发表时间:
2005
影响因子:
6.6
通讯作者:
A. Di Stefano
A. Di Stefano
中科院分区:
生物学2区
文献类型:
--
作者:
P. di Simplicio;Simona Frosali;R. Priora;D. Summa;F. Cherubini Di Simplicio;D. Di Giuseppe;A. Di Stefano

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蛋白质巯基化是由不同机制的氧化引起的,并参与各种生物过程。硫醇,蛋白质SH(PSH)和非蛋白质SH基团(NPSH,即GSH),在所有生物环境中在氧化剂稳态的调节中竞争,因为氧化剂使蛋白质硫醇化,而GSH使它们脱硫醇(例如,GSSG + PSH-GSSP + GSH)。虽然研究不足,但从巯基化蛋白质中消除二硫化物以再生关键的PSH是重要的。这些方面在细胞中知之甚少,其中谷氧还蛋白和过氧化物氧还蛋白作为酶或潜在的伴侣蛋白起作用以加速去巯基化。相反,血浆或白蛋白的研究强调了蛋白质构象在脱巯基过程中的重要性,并阐明了相对于其他NPSH,高半胱氨酸(具有潜在毒性的巯基)优先与白蛋白结合为蛋白质-巯基混合二硫化物的原因。在这里,我们提供了一个蛋白质硫醇化/脱硫醇化过程的概述,重点是在这一领域的最新发展和未来的前景。
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.
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