Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells.
Extracellular HSP70 has been found to participate in both innate and adaptive immune responses. However, little is known about the molecular mechanisms that mediate this process. Previous reports suggest that HSP70 interacts with antigen presenting cells (APC) through a plethora of surface receptors. In this study, we have examined the relative binding of potential HSP70 receptors and found high affinity binding to LOX-1 but not other structures with a role in HSP70-APC interactions such as LRP/CD91, CD40, TLR2, TLR4 or another c-type lectin family member (DC-SIGN) closely related to LOX-1. In addition to APC, HSP70 can avidly bind to non-APC cell lines, especially those from epithelial or endothelial background.
Thériault
Jimmy R
JR
Department of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 21-27 Burlington Avenue, Boston, MA 02215, USA.
Mambula
Salamatu S
SS
Sawamura
Tatsuya
T
Stevenson
Mary Ann
MA
Calderwood
Stuart K
SK
D000818:Animals; D000938:Antigen-Presenting Cells / Q000378:metabolism*; D002478:Cells, Cultured; D042783:Endothelial Cells / Q000378:metabolism; D004847:Epithelial Cells / Q000378:metabolism; D005434:Flow Cytometry; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D051379:Mice; D010455:Peptides / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins; D010455:Peptides; D011956:Receptors, Cell Surface