炎症
趋化因子
效力
化学
半乳糖凝集素-3
重组DNA
细胞因子
鼻息肉
肿瘤坏死因子α
细胞生物学
免疫学
体外
生物化学
生物
基因
作者
Yan Zhao,Shanshan Mo,Lanlan Yu,Xiaolu Li,Yun Hao,Wenbo Zhang,Qi Zhang,Ping Wang,Xiangdong Wang,Chenxuan Wang,Luo Zhang
出处
期刊:Nano Letters
[American Chemical Society]
日期:2022-03-11
卷期号:22 (6): 2350-2357
被引量:6
标识
DOI:10.1021/acs.nanolett.1c04817
摘要
Protein crystallization is a prevalent phenomenon existing in the formation of intricate protein-assembled structures in living cells. Whether the crystallization of a protein would exert a specific biological function, however, remains poorly understood. Here, we reconstructed a recombinant galectin-10 (gal-10) protein and artificially engineered a gal-10 protein assembly in two distinguishable states: i.e., an insoluble crystalline state and a soluble state. The potency of the gal-10 protein in either the crystalline state or the soluble state to induce chemokine or cytokine release in the primary human nasal epithelial cells and nasal polyps derived from chronic rhinosinusitis patients with nasal polyps was investigated. The crystalline gal-10 upregulated the gene expression of chemokines or cytokines, including IL-1β, IL-6, IL-8, TNF-α, and GM-CSF, in patient-derived primary cells and nasal polyps. In contrast, soluble gal-10 displayed a diminished potency to induce inflammation. Our results demonstrate that the gal-10 protein potency of activating inflammation is correlated with its crystalline state.
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