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翻译:化学趋化因子活性的体内调节:翻译后修饰。

In vivo regulation of chemokine activity by post-translational modification.

机构信息

Laboratory of Molecular Immunology, Department of Microbiology and Immunology, Rega Institute for Medical Research, KU Leuven, Leuven, Belgium.

出版信息

Immunol Cell Biol. 2013 Jul;91(6):402-7. doi: 10.1038/icb.2013.16. Epub 2013 Apr 30.

DOI:10.1038/icb.2013.16
PMID:23628804
Abstract

Cytokines and chemokines represent two important groups of proteins that control the immune system. Dysregulation of the network in which these immunomodulators function can result in uncontrolled inflammation leading to various diseases, including rheumatoid arthritis, characterized by chronic inflammation and bone erosion. Chemokine activity is regulated at multiple levels, such as post-translational modification (PTM) of chemokines and their receptors by specific enzymes including proteases and peptidylarginine deiminases. Many in vitro experiments underscore the importance of post-translational processing of human chemokines. PTMs may enhance or reduce chemokine activity or may alter the receptor specificity of chemokine ligands. However, identification of chemokine isoforms in physiological in vivo settings forms the ultimate proof that PTM of chemokines is relevant in regulating the biological activity of these molecules. This review summarizes current knowledge on the in vivo role for PTMs in the regulation of chemokine activity.

摘要

细胞因子和趋化因子是控制免疫系统的两类重要蛋白质。这些免疫调节剂功能网络的失调可导致不受控制的炎症,从而导致各种疾病,包括类风湿关节炎,其特征为慢性炎症和骨质侵蚀。趋化因子的活性在多个层面受到调节,如趋化因子及其受体的翻译后修饰(PTM),这是由包括蛋白酶和肽基精氨酸脱亚氨酶在内的特定酶完成的。许多体外实验强调了人趋化因子翻译后加工的重要性。PTMs 可能增强或降低趋化因子的活性,或者改变趋化因子配体的受体特异性。然而,在生理的体内环境中鉴定趋化因子同工型是 PTM 调节这些分子的生物学活性的最终证明。这篇综述总结了 PTM 在调节趋化因子活性中的体内作用的最新知识。

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