Open AccessGRP78 inhibits macrophage adhesion via SR-A
Author(s) -
Hui Bai,
Nan Li,
Xiaosi Zhou,
Chenchen Wang,
Yan Zhang,
Xudong Zhu,
Min Huang,
Yaoyu Chen,
Xiaoyü Li,
Qing Yang,
ChaoJun Li,
Jingjing Ben,
Qi Chen
Publication year - 2014
Publication title -
journal of biomedical research/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.