S100A8型
中性粒细胞胞外陷阱
钙蛋白酶
S100A9型
先天免疫系统
细胞外
炎症
细胞生物学
细胞内
细胞质
趋化性
下调和上调
化学
生物
免疫学
免疫系统
生物化学
医学
受体
基因
病理
疾病
炎症性肠病
作者
Evelien G. G. Sprenkeler,Judith Zandstra,Nadine D van Kleef,Ines Goetschalckx,Bibian Verstegen,Cathelijn E.M. Aarts,Hans Janssen,Anton T.J. Tool,Gerard van Mierlo,Robin van Bruggen,Ilse Jongerius,Taco W. Kuijpers
出处
期刊:Cells
[MDPI AG]
日期:2022-01-11
卷期号:11 (2): 236-236
被引量:30
标识
DOI:10.3390/cells11020236
摘要
Neutrophils are the most abundant innate immune cells in the circulation and they are the first cells recruited to sites of infection or inflammation. Almost half of the intracellular protein content in neutrophils consists of S100A8 and S100A9, though there has been controversy about their actual localization. Once released extracellularly, these proteins are thought to act as damage-associated molecular patterns (DAMPs), though their mechanism of action is not well understood. These S100 proteins mainly form heterodimers (S100A8/A9, also known as calprotectin) and this heterocomplex is recognized as a useful biomarker for several inflammatory diseases. We observed that S100A8/A9 is highly present in the cytoplasmic fraction of neutrophils and is not part of the granule content. Furthermore, we found that S100A8/A9 was not released in parallel with granular content but upon the formation of neutrophil extracellular traps (NETs). Accordingly, neutrophils of patients with chronic granulomatous disease, who are deficient in phorbol 12-myristate 13-acetate (PMA)-induced NETosis, did not release S100A8/A9 upon PMA stimulation. Moreover, we purified S100A8/A9 from the cytoplasmic fraction of neutrophils and found that S100A8/A9 could induce neutrophil activation, including adhesion and CD11b upregulation, indicating that this DAMP might amplify neutrophil activation.
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