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首页> 外文期刊>Journal of diabetes research. >The Autoantigenic Proinsulin B-Chain Peptide B11-23 Synergises with the 70 kDa Heat Shock Protein DnaK in Macrophage Stimulation
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The Autoantigenic Proinsulin B-Chain Peptide B11-23 Synergises with the 70 kDa Heat Shock Protein DnaK in Macrophage Stimulation

机译：自身抗原原胰岛素B链肽B11-23与巨噬细胞刺激中的70 kDa热激蛋白DnaK协同作用。

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Background. Heat shock proteins (Hsp) act as intracellular chaperones and in addition are used as adjuvant in vaccines of peptides complexed with recombinant Hsp. By interacting with autologous peptides, Hsp may promote the induction of autoimmune reactivity. Objective. Here, we analysed whether the effect of Hsp on macrophages is modulated by insulin peptides known to interact with Hsp. Results. Combinations of the 70 kDa Hsp DnaK with peptide B11-23 from the core region of the proinsulin B-chain induced the release of the inflammatory mediators interleukin-6, tumor necrosis factor α, and interleukin-1β from cells of human and murine macrophage lines. In parallel, there was high-affinity binding of B11-23 to DnaK. DnaK mixed with peptides from other regions of the insulin molecule did not stimulate cytokine secretion. DnaK alone induced little cytokine production, and peptides alone induced none. Conclusion. The macrophage-stimulating potential of Hsp70 family proteins when combined with the proinsulin B-chain peptide B11-23 may contribute to the immunodominance of this peptide in the development of beta cell-directed autoimmunity in type 1 diabetes.
机译：背景。热休克蛋白（Hsp）充当细胞内伴侣，并在与重组Hsp复合的肽疫苗中用作佐剂。通过与自体肽相互作用，Hsp可以促进自体免疫反应性的诱导。目的。在这里，我们分析了Hsp对巨噬细胞的作用是否被已知与Hsp相互作用的胰岛素肽调节。结果。 70 kDa Hsp DnaK与来自胰岛素原B链核心区域的肽B11-23的结合诱导人和鼠巨噬细胞系细胞释放炎性介质白介素6，肿瘤坏死因子α和白介素1β。 。同时，B11-23与DnaK具有高亲和力结合。与来自胰岛素分子其他区域的肽混合的DnaK不会刺激细胞因子的分泌。单独的DnaK几乎不诱导细胞因子的产生，而单独的肽则不诱导任何细胞因子的产生。结论。 Hsp70家族蛋白与胰岛素原B链肽B11-23结合时，具有刺激巨噬细胞的潜能，可能会促进该肽在1型糖尿病的β细胞定向自身免疫发展中的免疫优势。

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