Author/Authors :
Hِlzl، نويسنده , , Markus A. and Hofer، نويسنده , , Johannes and Kovarik، نويسنده , , Johannes J. and Roggenbuck، نويسنده , , Dirk and Reinhold، نويسنده , , Dirk and Goihl، نويسنده , , Alexander and Gنrtner، نويسنده , , Miriam and Steinberger، نويسنده , , Peter and Zlabinger، نويسنده , , Gerhard J.، نويسنده ,
Abstract :
The pancreatic zymogen granule membrane protein (GP2) is expressed by pancreatic acinar cells and M cells of the ileum. GP2 is the closest related homologue of the urine resident Tamm–Horsfall protein (THP). Recently, it was shown that THP is a ligand of various scavenger receptors (SRs). Therefore, we were interested, if GP2 has similar properties.
f different SRs was stably transfected into a murine thymoma cell line. GP2 was recombinantly expressed, purified and biotinylated. Binding or uptake of GP2 by transfected cells or monocyte-derived dendritic cells (moDCs) was analyzed by flow-cytometry.
a binding partner of the scavenger receptor expressed on endothelial cells I (SREC-I) but not of SR-AI and SR-BI. The dissociation constant (Kd) of GP2 binding to SREC-I is 41.3 nM. SREC transfected cells are able to internalize GP2. moDCs express SREC-I and also bind and internalize GP2. Inhibition of SREC-I on moDCs with anti-SREC-I antibodies does not result in a decreased GP2 binding.
ction of GP2 with SREC-I and uptake might have profound effects in antigen clearance and mediation of the immune response. In addition to SREC-I other presently unknown receptors for GP2 on DCs might be involved in this process.
Keywords :
GP2 , SREC-I , dendritic cell , THP , Internalization , acLDL