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人C5a过敏毒素的趋化受体。

The chemotactic receptor for human C5a anaphylatoxin.

作者信息

Gerard N P, Gerard C

机构信息

Ina Sue Perlmutter Research Laboratory, Childrens' Hospital, Boston, Massachusetts.

出版信息

Nature. 1991 Feb 14;349(6310):614-7. doi: 10.1038/349614a0.

Abstract

Host defence and inflammatory responses are controlled and amplified by receptor-mediated events often initiated by a chemotactic factor that directs the approach of phagocytic cells. Complement receptors CR1 and CR3 are responsible for the phagocytic and adhesive properties of neutrophils, whereas the C5a receptor mediates the pro-inflammatory and chemotactic actions of the complement anaphylatoxin C5a. In addition to stimulating chemotaxis, granule enzyme release and superoxide anion production, this receptor stimulates upregulation of expression and activity of the adhesion molecule MAC-1, and of CR1, and a decrease in cell-surface glycoprotein 100MEL-14 on neutrophils. In vivo, the C5a receptor may participate in anaphylactoid and septic shock. The human C5a receptor was cloned from U937 and HL-60 cells and identified by high affinity binding when expressed in COS-7 cells. The deduced amino-acid sequence of the receptor reveals the expected motifs befitting its interaction with cellular GTP-binding proteins.

摘要

宿主防御和炎症反应由受体介导的事件控制和放大,这些事件通常由引导吞噬细胞靠近的趋化因子引发。补体受体CR1和CR3负责中性粒细胞的吞噬和黏附特性,而C5a受体介导补体过敏毒素C5a的促炎和趋化作用。除了刺激趋化作用、颗粒酶释放和超氧阴离子产生外,该受体还刺激中性粒细胞上黏附分子MAC-1、CR1的表达和活性上调,以及细胞表面糖蛋白100MEL-14减少。在体内,C5a受体可能参与类过敏反应和败血性休克。人C5a受体从U937和HL-60细胞中克隆出来,并在COS-7细胞中表达时通过高亲和力结合得以鉴定。该受体推导的氨基酸序列揭示了符合其与细胞GTP结合蛋白相互作用的预期基序。

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