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糖皮质激素对白细胞中膜联蛋白A1受体的上调作用。

Glucocorticoid upregulation of the annexin-A1 receptor in leukocytes.

作者信息

Sawmynaden Prescilla, Perretti Mauro

机构信息

The William Harvey Research Institute, Bart's and the London, Charterhouse Square, London EC1M 6BQ, UK.

出版信息

Biochem Biophys Res Commun. 2006 Nov 3;349(4):1351-5. doi: 10.1016/j.bbrc.2006.08.179. Epub 2006 Sep 7.

Abstract

We tested here whether glucocorticoids modulated myeloid cell expression of a specific G-coupled receptor, termed formyl-peptide receptor like-1 (FPRL-1), recently shown to mediate the anti-inflammatory actions of annexin-A1. Real-time PCR and flow cytometry demonstrated rapid up-regulation of mRNA followed by the protein in HL-60 cells incubated with dexamethasone, with peaks at 2 and 24h, respectively. This effect was not restricted to dexamethasone, since reproduced by glucocorticoids. In addition, it was not restricted to the cell line, since replicated with human peripheral blood monocytes. Glucocorticoid ability to upregulate cell surface expression of FPRL-1 was specific, since no effects upon the related receptor FPR or the integrin CD11b could be detected. In view of the wide range of endogenous ligands known to interact with FPRL-1, including the anti-inflammatory protein annexin-A1, we speculate that the novel effect here described may impact on the clinical immunosuppressive and anti-inflammatory properties of glucocorticoids.

摘要

我们在此测试了糖皮质激素是否调节一种特定的G蛋白偶联受体(称为甲酰肽受体样1,FPRL-1)的髓样细胞表达,最近研究表明该受体介导膜联蛋白A1的抗炎作用。实时PCR和流式细胞术显示,在用地塞米松孵育的HL-60细胞中,mRNA迅速上调,随后蛋白质也上调,峰值分别出现在2小时和24小时。这种效应不仅限于地塞米松,因为其他糖皮质激素也能重现这种效应。此外,这种效应不仅限于该细胞系,因为在人外周血单核细胞中也能复制。糖皮质激素上调FPRL-1细胞表面表达的能力是特异性的,因为未检测到对相关受体FPR或整合素CD11b有任何影响。鉴于已知有多种内源性配体与FPRL-1相互作用,包括抗炎蛋白膜联蛋白A1,我们推测此处描述的新效应可能会影响糖皮质激素的临床免疫抑制和抗炎特性。

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