GRP78 inhibits macrophage adhesion via SR-A | Zendy

Hui Bai | Zendy; Nan Li | Zendy; Zhou Xiaodan | Zendy; Chenchen Wang | Zendy; Yan Zhang | Zendy; Xudong Zhu | Zendy; Min Huang | Zendy; Yaoyu Chen | Zendy; Xiaoyü Li | Zendy; Yang Qing | Zendy; Chaojun Li | Zendy; Ben Jingjing | Zendy; Qi Chen | Zendy

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GRP78 inhibits macrophage adhesion via SR-A

Author(s) -

Hui Bai,

Nan Li,

Zhou Xiaodan,

Chenchen Wang,

Yan Zhang,

Xudong Zhu,

Min Huang,

Yaoyu Chen,

Xiaoyü Li,

Yang Qing,

Chaojun Li,

Ben Jingjing,

Qi Chen

Publication year - 2014

Publication title -

journal of biomedical research

Language(s) - Uncategorized

Resource type - Journals

eISSN - 2352-4685

pISSN - 1674-8301

DOI - 10.7555/jbr.28.20130054

Subject(s) - internalization , förster resonance energy transfer , macrophage , adhesion , scavenger receptor , chemistry , microbiology and biotechnology , cell adhesion , receptor , ligand (biochemistry) , biophysics , biochemistry , biology , fluorescence , in vitro , lipoprotein , physics , organic chemistry , quantum mechanics , cholesterol

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.

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