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GRP78 inhibits macrophage adhesion via SR-A 被引量:2
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作者 Hui Bai Nan Li +10 位作者 Xiaodan Zhou Chenchen Wang Yan Zhang Xudong Zhu Min Huang Yaoyu Chen Xiaoyu Li Qing Yang Chaojun Li Jingjing Ben Qi Chen 《The Journal of Biomedical Research》 CAS 2014年第4期269-274,共6页
Class A scavenger receptor (SR-A) plays an important role in macrophage adhesion. However, the underlying mechanism remains unclear. We previously found that 78 kDa glucose-regulated protein (GRP78) inhibited SR- ... Class A scavenger receptor (SR-A) plays an important role in macrophage adhesion. However, the underlying mechanism remains unclear. We previously found that 78 kDa glucose-regulated protein (GRP78) inhibited SR- A-mediated ligand internalization into macrophage by binding to SR-A. The aim of the study was to investigate whether GRP78 could regulate SR-A-mediated cell adhesion. We demonstrated that GRP78 bound directly to SR-A by fluorescence resonance energy transfer (FRET) assay. Overexpression of GRP78 inhibited macrophage adhesion via SR-A. These results suggest that GRP78 may act as an inhibitor of macrophage adhesion via SR-A. 展开更多
关键词 class A scavenger receptor glucose-regulated protein 78 (GRP78) macrophage adhesion fluorescenceresonance energy transfer 6-aminonicotinamide
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