GRP78 inhibits macrophage adhesion via SR-A

J Biomed Res. 2014 Jul;28(4):269-74. doi: 10.7555/JBR.28.20130054. Epub 2014 Mar 20.

Abstract

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.

Keywords: 6-aminonicotinamide; class A scavenger receptor; fluorescence resonance energy transfer; glucose-regulated protein 78 (GRP78); macrophage adhesion.