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The zymogen granule protein 2 (GP2) binds to scavenger receptor expressed on endothelial cells I (SREC-I).

Hölzl MA, Hofer J, Kovarik JJ, Roggenbuck D, Reinhold D, Goihl A, Gärtner M, Steinberger P, Zlabinger GJ - Cell. Immunol. (2010)

Bottom Line: Inhibition of SREC-I on moDCs with anti-SREC-I antibodies does not result in a decreased GP2 binding.Interaction 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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Immunology, Center of Pathophysiology, Infectiology and Immunology, Medical University of Vienna, A-1090 Vienna, Austria.

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SR expression and binding to acLDL-488 and GP2-bio by transduced Bw cells. SR expressing Bw cells were stained with PE-labeled antibodies (Bw-SR-AI), biotinylated antibodies (Bw-SREC-I) or unlabeled antibodies (Bw-SR-BI). Binding of primary antibodies was detected with appropriate PE-labeled secondary reagents (left panel, bold line). acLDL-488 was tested for its binding to SR expressing clones (middle panel, bold line). GP2-bio was incubated with SR expressing Bw clones and stained with SA-PE (right panel, bold line). Mock transfected Bw cells were used as control in all binding experiments (thin lines). The depicted results are representative for three independent experiments. MFI = mean fluorescence intensity.
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f0005: SR expression and binding to acLDL-488 and GP2-bio by transduced Bw cells. SR expressing Bw cells were stained with PE-labeled antibodies (Bw-SR-AI), biotinylated antibodies (Bw-SREC-I) or unlabeled antibodies (Bw-SR-BI). Binding of primary antibodies was detected with appropriate PE-labeled secondary reagents (left panel, bold line). acLDL-488 was tested for its binding to SR expressing clones (middle panel, bold line). GP2-bio was incubated with SR expressing Bw clones and stained with SA-PE (right panel, bold line). Mock transfected Bw cells were used as control in all binding experiments (thin lines). The depicted results are representative for three independent experiments. MFI = mean fluorescence intensity.

Mentions: Retrovirally transduced Bw cells were evaluated for the expression of SRs by flow cytometry using SR specific antibodies. SR-AI, SR-BI and SREC-I were expressed on the surface of the respective Bw-clones at high levels (Fig. 1). To address whether SRs can bind their genuine ligand, SR expressing Bw clones were incubated with acLDL-488. All SR expressing clones but not mock transfected Bw cells strongly bound acLDL-488 (Fig. 1) and were therefore considered to be functional. Subsequently, SR expressing Bw clones were incubated with GP2-bio, which strongly bound to clones expressing SREC-I. No binding was observed with SR-AI or SR-BI or mock transfected Bw cells (Fig. 1). These results clearly identify SREC-I as a cellular receptor for GP2.


The zymogen granule protein 2 (GP2) binds to scavenger receptor expressed on endothelial cells I (SREC-I).

Hölzl MA, Hofer J, Kovarik JJ, Roggenbuck D, Reinhold D, Goihl A, Gärtner M, Steinberger P, Zlabinger GJ - Cell. Immunol. (2010)

SR expression and binding to acLDL-488 and GP2-bio by transduced Bw cells. SR expressing Bw cells were stained with PE-labeled antibodies (Bw-SR-AI), biotinylated antibodies (Bw-SREC-I) or unlabeled antibodies (Bw-SR-BI). Binding of primary antibodies was detected with appropriate PE-labeled secondary reagents (left panel, bold line). acLDL-488 was tested for its binding to SR expressing clones (middle panel, bold line). GP2-bio was incubated with SR expressing Bw clones and stained with SA-PE (right panel, bold line). Mock transfected Bw cells were used as control in all binding experiments (thin lines). The depicted results are representative for three independent experiments. MFI = mean fluorescence intensity.
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Related In: Results  -  Collection

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f0005: SR expression and binding to acLDL-488 and GP2-bio by transduced Bw cells. SR expressing Bw cells were stained with PE-labeled antibodies (Bw-SR-AI), biotinylated antibodies (Bw-SREC-I) or unlabeled antibodies (Bw-SR-BI). Binding of primary antibodies was detected with appropriate PE-labeled secondary reagents (left panel, bold line). acLDL-488 was tested for its binding to SR expressing clones (middle panel, bold line). GP2-bio was incubated with SR expressing Bw clones and stained with SA-PE (right panel, bold line). Mock transfected Bw cells were used as control in all binding experiments (thin lines). The depicted results are representative for three independent experiments. MFI = mean fluorescence intensity.
Mentions: Retrovirally transduced Bw cells were evaluated for the expression of SRs by flow cytometry using SR specific antibodies. SR-AI, SR-BI and SREC-I were expressed on the surface of the respective Bw-clones at high levels (Fig. 1). To address whether SRs can bind their genuine ligand, SR expressing Bw clones were incubated with acLDL-488. All SR expressing clones but not mock transfected Bw cells strongly bound acLDL-488 (Fig. 1) and were therefore considered to be functional. Subsequently, SR expressing Bw clones were incubated with GP2-bio, which strongly bound to clones expressing SREC-I. No binding was observed with SR-AI or SR-BI or mock transfected Bw cells (Fig. 1). These results clearly identify SREC-I as a cellular receptor for GP2.

Bottom Line: Inhibition of SREC-I on moDCs with anti-SREC-I antibodies does not result in a decreased GP2 binding.Interaction 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.

View Article: PubMed Central - PubMed

Affiliation: Institute of Immunology, Center of Pathophysiology, Infectiology and Immunology, Medical University of Vienna, A-1090 Vienna, Austria.

Show MeSH
Related in: MedlinePlus