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Synthetic cell-permeable caveolin-1 scaffolding domain peptide activates phagocytosis of Escherichia coli by regulating Rab5 activity
Zeitschrift für Naturforschung C ( IF 2 ) Pub Date : 2020-05-26 , DOI: 10.1515/znc-2020-0023
Makoto Hagiwara 1, 2 , Kenji Matsushita 1
Affiliation  

Abstract Caveolae are defined as 50–100 nm wide pits in the plasma membrane containing oligomeric caveolin proteins. They have been implicated in endocytosis (including phagocytosis), transcytosis, calcium signalling, and numerous other signal transduction events. Caveolin-1, a major structural component of caveolae, enhances Rab5 activity. In this study, we examined the effect of a synthetic cell-permeable peptide of the caveolin-1 scaffolding domain (CSD) on phagocytosis. Treatment with the CSD peptide increased Rab5 activity, Rab5-early endosome antigen 1 (EEA1) interaction, and phagocytosis of Escherichia coli. The results suggest that the synthetic cell-permeable CSD peptide is an activator of phagocytosis.

中文翻译:

合成细胞渗透性caveolin-1支架结构域肽通过调节Rab5活性激活大肠杆菌的吞噬作用

摘要 Caveolae 被定义为质膜中含有寡聚小窝蛋白的 50-100 nm 宽的凹坑。它们与内吞作用(包括吞噬作用)、胞吞作用、钙信号传导和许多其他信号转导事件有关。Caveolin-1 是小窝的主要结构成分,可增强 Rab5 的活性。在这项研究中,我们检查了caveolin-1 支架结构域(CSD) 的合成细胞渗透性肽对吞噬作用的影响。用 CSD 肽处理增加了 Rab5 活性、Rab5 早期内体抗原 1 (EEA1) 相互作用和大肠杆菌的吞噬作用。结果表明合成的细胞渗透性 CSD 肽是吞噬作用的激活剂。
更新日期:2020-05-26
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