GRP78 inhibits macrophage adhesion via SR-A

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 stu...

Descripción completa

Detalles Bibliográficos
Autores principales: Bai, Hui, Li, Nan, Zhou, Xiaodan, Wang, Chenchen, Zhang, Yan, Zhu, Xudong, Huang, Min, Chen, Yaoyu, Li, Xiaoyu, Yang, Qing, Li, Chaojun, Ben, Jingjing, Chen, Qi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Editorial Department of Journal of Biomedical Research 2014
Materias:
Research-Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4102840/
https://www.ncbi.nlm.nih.gov/pubmed/25050110
http://dx.doi.org/10.7555/JBR.28.20130054
Descripción
Sumario: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.

Ejemplares similares