炎症反应S100蛋白:新的机制,调节功能。
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Goyette J, Geczy CL
炎症反应S100蛋白:新的机制,调节功能。
氨基酸。2011年10月,41 (4):821 - 42。doi: 10.1007 / s00726 - 010 - 0528 - 0。Epub 2010年3月6日。
- PubMed ID
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20213444 (在PubMed]
- 文摘
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本文着重于细胞外的新方面calgranulins的角色。S100A8, S100A9 S100A12中性粒细胞持续表达,诱导多种细胞类型。S100A8和S100A9基因是由pro -抗炎介质及其功能可能取决于细胞类型,在一个特定的炎性介质环境,受体参与识别和翻译修饰。S100A8基因诱导巨噬细胞是依赖于il - 10和强免疫抑制药物。S100A8和S100A9被过氧化氢氧化,次氯酸盐和一氧化氮(NO)。HOCl生成intra-chain sulfinamide债券;强氧化促进交联形式在人类动脉粥样化。S100A8 > 200倍更敏感比低密度脂蛋白氧化交联,可以减少氧化损伤。S100A8和S100A9 S-nitrosylated。S100A8-SNO抑制肥大细胞激活和炎症的微循环,并可能作为一个没有转运蛋白调节船语气炎性病变。 S100A12 activates mast cells and is a monocyte and mast cell chemoattractant; a G-protein-coupled mechanism may be involved. Structure-function studies are discussed in relation to conservation and divergence of functions in S100A8. S100A12 induces cytokines in mast cells, but not monocytes/macrophages. It forms complexes with Zn(2+) and, by chelating Zn(2+), S100A12 significantly inhibits MMPs. Zn(2+) in S100A12 complexes co-localize with MMP-9 in foam cells in atheroma. In summary, S100A12 has pro-inflammatory properties that are likely to be stable in an oxidative environment, because it lacks Cys and Met residues. Conversely, S100A8 and S100A9 oxidation and S-nitrosylation may have important protective mechanisms in inflammation.