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着眼于糖尿病的硫醇信号网络。

Thiol signalling network with an eye to diabetes.

机构信息

Department of Internal Medicine, University of Pisa, Pisa, Italy.

出版信息

Molecules. 2010 Dec 6;15(12):8890-903. doi: 10.3390/molecules15128890.

DOI:10.3390/molecules15128890
PMID:21135801
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6259199/
Abstract

Redox regulatory system controls normal cellular functions. Controlled changes in redox couples potential serve as components for signal transduction, similarly to the phosphorylation cascade. Cellular redox biology requires both compartimentalisation and communication of redox systems: the thermodynamic disequilibrium of the major redox switches allows rapid and sensitive responses to perturbations in redox environments. The many oxidation states of sulphur are found in numerous sulphur species with distinct functional groups (thiols, disulphides, polysulphides, sulphenic, sulphinic and sulphonic acids, etc.), which participate in a complicated network of sulphur-based redox events. Human diseases such as diabetes mellitus and its cardiovascular complications have been associated with increased production of reactive oxygen species and perturbations of thiol redox homeostasis. The review surveys literature related to some etiopathogenic aspects and therapeutic perspectives. The dual toxic-protective property of sulphydryl-donor molecules in experimental settings proposes the general problem of designing antioxidants for therapeutic use.

摘要

氧化还原调控系统控制着正常的细胞功能。氧化还原对电位的可控变化可作为信号转导的组成部分,类似于磷酸化级联。细胞氧化还原生物学需要氧化还原系统的区室化和通讯:主要氧化还原开关的热力学不平衡允许对氧化还原环境的干扰做出快速和敏感的反应。许多硫的氧化态存在于具有不同功能基团的许多硫物种中(硫醇、二硫化物、多硫化物、亚磺酸、亚硫酸和磺酸等),这些物质参与了一个复杂的基于硫的氧化还原事件网络。糖尿病及其心血管并发症等人类疾病与活性氧的产生增加和巯基氧化还原稳态的紊乱有关。综述调查了与一些病因发病和治疗相关的文献。实验环境中巯基供体分子的双重毒性保护特性提出了为治疗用途设计抗氧化剂的一般问题。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdc/6259199/57bd5a6f372c/molecules-15-08890-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdc/6259199/57bd5a6f372c/molecules-15-08890-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdc/6259199/57bd5a6f372c/molecules-15-08890-g001.jpg

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Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease.
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