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Published online before print November 21, 2003
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* Graduate School of Biostudies and Institute for Virus Research and
Department of Cardiovascular Medicine, Graduate School of Medicine, Kyoto University, Sakyo-ku, Japan;
Department of Microbiology, Kinki University School of Medicine, Osaka-Sayama, Japan; and
Biomedical Research Laboratories and
¶ Molecular Biology Research Laboratories, Sankyo Co. Ltd., Shinagawa-ku, Tokyo, Japan
1 Correspondence: Graduate School of Biostudies and Institute for Virus Research, Kyoto University, Shogoin Kawahara-cho 53, Sakyo-ku, Kyoto 606-8507, Japan. E-mail: syonehar{at}virus.kyoto-u.ac.jp
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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i protein blocker, which inhibited chemotaxis of CXCR6-expressing cells induced by SR-PSOX/CXCL16. Furthermore, the adhesion activity was up-regulated by treatment of SR-PSOX/CXCL16-expressing cells with a metalloprotease inhibitor, which increased surface expression levels of SR-PSOX/CXCL16. Thus, SR-PSOX/CXCL16 is a unique molecule that not only attracts T cells and NKT cells toward DCs but also supports their firm adhesion to DCs.
Key Words: scavenger receptor • metalloprotease • T cells
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Recently, we have identified and characterized SR-PSOX, a novel scavenger receptor for phosphatidylserine and oxidized low-density lipoprotein and bacteria [10 , 11 ]. Separately, other groups have identified chemokine ligand 16 (CXCL16) [12 , 13 ], the chemokine ligand for a G protein-coupled receptor CXC chemokine receptor 6 (CXCR6) [14 , 15 ], and then SR-PSOX and CXCL16 turned out to be identical. Thus, SR-PSOX/CXCL16 is the second transmembrane-type chemokine with a chemokine domain fused to a mucin-like stalk, a structure very similar to that of FNK [6 , 7 ]. SR-PSOX/CXCL16 is selectively expressed on antigen-presenting cells (APCs) such as dendritic cells (DCs) and macrophages, and its receptor CXCR6 is expressed on naive CD8+ T cells, natural killer T (NKT) cells, and type 1-polarized, activated CD4+ and CD8+ T cells [12 13 14 15 16 ]. It has been proposed that CXCL16 promotes the movement of T cells toward DCs in the splenic red pulp [12 ]. Furthermore, CXCR6-expressing effector T cells were found to be abundant in type 1 inflammatory lesions such as rheumatoid joints and inflamed livers [16 ].
DCs, which capture and process antigens to form major histocompatibility complex peptide complexes, function as professional APCs to T cells. After up-taking antigen and migrating from the periphery to the T cell areas of secondary lymphoid organs, DC contact can initiate primary immune responses via activation of resting T cells. In addition, contacts between DCs and T cells are essential to maintain and restart immune responses of previously activated T cells [17
, 18
]. Adhesion molecules such as lymphocyte function-associated antigen-3 (LFA-3)/CD2, LFA-1/intercellular adhesion molecule-1 (ICAM-1) and DC-specific ICAM-3-grabbing nonintegrin/ICAM-3 are reported to mediate interactions between DCs and T cells and to provide activation signals via DC–T cell adhesion [19
, 20
]. Notably, the membrane-anchored chemokine, FNK, whose molecular structure is similar to that of SR-PSOX/CXCL16, can directly function as an adhesion molecule for cells expressing its receptor CX3CR1 [8
, 9
]. Here, we demonstrate that in a manner very similar to that of FNK, SR-PSOX also functions as a direct adhesion cell molecule for cells expressing its receptor CXCR6. The chemokine domain of SR-PSOX primarily mediates the adhesion of CXCR6-expressing cells. The adhesion is not inhibited by pertussis toxin (PTX), the GI protein inhibitor, although it effectively suppresses chemotaxis of CXCR6-expressing cells induced by SR-PSOX/CXCL16. Furthermore, the adhesion of CXCR6-expressing cells can be enhanced by treatment of SR-PSOX/CXCL16-expressing cells with a metalloprotease inhibitor, which increases the surface expression of SR-PSOX/CXCL16. Thus, SR-PSOX/CXCL16 may play an important role in interactions between DCs and T cells or NKT cells as a chemoattractant as well as a cell adhesion molecule.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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Monoclonal anti-human (h)- and mouse (m)SR-PSOX antibodies
Female Lewis rats were immunized with mSR-PSOX-Fc fusion protein, produced by COS-7 cells, transfected with a fusion construct consisting of the extracellular domain of mSR-PSOX (amino acids 1–198) fused at its C terminus with an Fc fragment of human immunoglobulin G (IgG)1. Three days after the last immunization, spleen cells were fused with NS-1 mouse myeloma cells as described previously [21
]. Finally, we generated an anti-mSR-PSOX monoclonal antibody (mAb) 12-81. Anti-hSR-PSOX mAb 22-19-12, 49-36, and 28-12 were generated as described previously [11
].
Preparation of polyclonal anti-hSR-PSOX antibody
Synthetic peptides corresponding to amino acid residues 42–61 of hSR-PSOX were conjugated to Imject Maleimide-Activated mcKLH (Pierce, Rockford, IL). After the immunization of a rabbit with the conjugates, polyclonal antiserum was collected and purified using a column packed with peptide corresponding to amino acid residues 42–61 of hSR-PSOX.
SR-PSOX-FNK hybrid protein
Plasmids encoding SR-PSOX-FNK hybrid molecules were generated by polymerase chain reaction (PCR) and subsequent ligation of DNA fragments into pME18S [22
] as described previously [21
]. In brief, the following fragments were amplified by PCR using primers as indicated: DNA encoding the chemokine domain of hSR-PSOX (amino acids 1–118) using primers 5'-TCACTCGAGATGGGACGGGACTTGCGGCC-3' and 5'-TCAGAATTCAGGAAGTAAATGCTTCTGGTGGC-3'; DNA encoding the chemokine domain of hFNK (amino acids 1–206) using 5'-TCACTCGAGAGCTCTGCCGCCTGGCTCTA-3' and 5'-TCAGAATTCTAGGGCAGCAAGCCTGGCGGT-3'; DNA encoding the region containing the mucin, transmembrane, and cytoplasmic domains of hSR-PSOX (amino acids 120–254) using 5'-TCAGAATTCACCAGCCCCCCAATTTCTCA-3' and 5'-TCACTGCAGTCAGGTATTAGAGTCAGGTG-3'; and DNA encoding the region containing the mucin, transmembrane, and cytoplasmic domains of hFNK (amino acids 97–397) using 5'-TCAGAATTCACTCGAAATGGCGGCACCTT-3' and 5'-TCACTGCAGACTAGACACAGGCCAGAGGA-3'. PCR fragments of the chemokine domain were digested with XhoI and EcoRI, and PCR fragments of the other domains were digested with EcoRI and PstI. These digested fragments were ligated together into pME18S digested with XhoI and PstI, and expression vectors for four kinds of SR-PSOX-FNK hybrids (S-S, S-F, F-S, and F-F, see Fig. 4A ) were prepared. DNA encoding hSR-PSOX without the mucin domain (amino acids 119–205; 
mucin) was generated by ligating DNA fragments encoding the chemokine domain of hSR-PSOX and the transmembrane and cytoplasmic domains of hSR-PSOX, which were prepared at once by PCR using 5'-GCACAGGACCGGCACAGGAAGTAAATGCTT-3', 5'-TCACTCGAGATGGGACGGGACTTGCGGCC-3', and 5'-GCAGTGGCTGGTTAGTCCTA-3' as primers. These PCR fragments digested with XhoI and HindIII and with adaptor fragments generated by digestion of pME18S with XhoI and HindIII were ligated together into HindIII-digested pME18S-SR-PSOX.
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Cell adhesion assays
Cell adhesion to immobilized SR-PSOX or FNK was measured essentially as described previously [8
]. In adhesion assays with immobilized chemokines, enzyme-linked immunosorbent assay (ELISA) plates (Corning Costar) were precoated with 10 nM chemokines fused with a secreted form of placental alkaline phosphatase (SEAP). L-CXCR6 cells or mouse-activated T cells were transferred to each well (5x104 cells/well) and incubated for 30 min at room temperature (RT). After being washed, adherent cells were quantified using Picogreen double-strand DNA quantitation reagent (Molecular Probes, Eugene, OR). In adhesion assays with chemokine-expressing cells, L-CXCR6 or mouse-activated T cells labeled with calcein acetoxymethyl ester (calcein-AM; Molecular Probes) were transferred to 12-well plates (5x105 cells/well), where COS-7 cells expressing SR-PSOX (COS-SR-PSOX cells) were preseeded. After incubation for 60 min at 37°C, nonadherent cells were removed by washing, and fluorescence intensity was measured using Wallac 1420 ARVO fluoroscan (Wallac, Turku, Finland). To analyze effects of various inhibitors, COS-SR-PSOX cells and L-CXCR6 cells were preincubated with PTX (500 ng/ml), wortmannin (100 nM), PD098059 (50 µM), or soluble (s)SR-PSOX-SEAP (20 nM) for 30 min at 37°C.
Expression analysis of SR-PSOX and CXCR6
For flow cytometric analysis of cell surface-expressed hSR-PSOX, cells were detached from dishes with 5 mM EDTA and incubated for 1 h on ice with 20 µg/ml anti-hSR-PSOX mAb, clone 22-19-12, 49-36, or 28-12 or control mouse IgG. After being washed, cells were incubated with 20 µg/ml fluorescein isothiocyanate (FITC)-conjugated anti-mouse IgG antibody (Cappel, Aurora, OH) on ice for 1 h. After two-times washes, cells were analyzed on an EPICS Elite (Coulter, Hialeah, FL). Flow cytometric analysis of cell surface-expressed mSR-PSOX was similarly performed using the anti-mSR-PSOX mAb 12-81. For flow cytometric analysis of cell surface-expressed hCXCR6, Fc receptors on cells were blocked by treatment with human IgG, and then cells were stained with phycoerythrin (PE)-labeled anti-hCXCR6 mAb (clone 56811). For flow cytometric analysis of mCXCR6, Fc receptors were blocked by FITC-labeled anti-CD16/CD32 (PharMingen), and then cells were stained with SR-PSOX-Fc and PE-labeled goat anti-human Fc
as described previously [12
].
Quantification of SR-PSOX by ELISA
ELISA plates were coated with the monoclonal anti-SR-PSOX antibody 28-12 (10 µg/ml, 50 µl/well) by incubating for 2 h at 37°C. After three-times washes with phosphate-buffered saline (PBS) containing 0.1% Tween 20, the plates were blocked with fourfold-diluted BlockAce (Dainippon Seiyaku, Osaka, Japan) for 1 h at RT. After three more washes, appropriately diluted samples or standards (50 µl/well) were loaded and incubated for 2 h at RT. After another three-times washes, rabbit polyclonal anti-SR-PSOX antibody (50 µl/well) against synthetic peptides corresponding to amino acid residues 42–61 of hSR-PSOX (10 µg/ml) was transferred to the plate and incubated for 1 h at RT. After three-times washes with PBS containing 0.1% Tween 20, anti-rabbit IgG–horseradish peroxidase (50 µl/well), which does not cross-react with mouse IgG (Amersham Biosciences, Little Chalfont, UK), was transferred and incubated for 30 min at RT. After another three washes with PBS containing 0.1% Tween 20, tetramethylbenzidine substrate buffer (100 µl/well; Dako, Carpinteria, CA) was transferred to each well. After incubation for 5–30 min at RT, stop solution (100 µl/well) was transferred to each well, and the optical density (O.D.) at 450 nm was determined using Wallac 1420 ARVO fluoroscan (Wallac).
Preparation of SR-PSOX-containing samples for ELISA
COS-SR-PSOX cells in 24-well tissue-culture plates were cultured for 24 h with serum-free medium in the presence or absence of the metalloproteinase inhibitor GM6001 (10 µM). Then, culture supernatants were collected for quantification of sSR-PSOX. After being washed with PBS, cells were lysed for 30 min with lysis buffer (PBS containing 1% Nonidet P-40, 0.5% sodium deoxycholate, 0.1% sodium dodecyl sulfate, 0.1 mM phenylmethylsulfonyl fluoride, and 1% protease inhibitor mixture). After clarification of the culture supernatants and cell lysates by centrifugation, ELISA quantified the SR-PSOX. The data shown represent the mean ± SD from at least three independent experiments.
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RESULTS |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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i class of G proteins, effectively suppressed responses of L-hCXCR6 cells to hSR-PSOX-SEAP in chemotaxis and calcium-mobilization assays as described previously [12
]. Chemotaxis but not calcium mobilization was also slightly inhibited by the phosphatidylinositol-3 kinase (PI-3K) inhibitor wortmannin, and the mitogen-activated protein kinase kinase inhibitor PD098059 did not show any significant inhibition of chemotaxis or calcium mobilization. The effects of wortmannin on chemotaxis and calcium mobilization are very similar to those shown in T lymphoblasts stimulated with another chemokine, stromal cell-derived factor 1/CXCL12 [23
]. Conversely, the adhesion of L-hCXCR6 cells to immobilized hSR-PSOX-SEAP or COS-hSR-PSOX cells was not inhibited by PTX, wortmannin, or PD098059 (Fig. 3C
and 3D)
. We also confirmed that EGTA did not suppress the adhesion of L-hCXCR6 cells to hSR-PSOX-SEAP-coated plates (Fig. 3C)
. Therefore, the adhesion of CXCR6-expressing cells to SR-PSOX/CXCL16 did not require signaling via PTX-sensitive G proteins or PI-3K downstream of chemokine receptors or calcium-dependent activation of integrins. These data were very similar to those reported for adhesion of CX3CR1-expressing cells mediated by membrane-anchored FNK [8
]. In addition, L-hCXCR6 cells were shown to bind not only to the immobilized extracellular domain of SR-PSOX on plastic culture dishes (Fig. 1)
but also to the cytoplasmic domain-truncated SR-PSOX expressed on COS-7 cells (data not shown). These results indicate that the cytoplasmic domain of SR-PSOX is not required for adhesion between cells expressing SR-PSOX and those expressing CXCR6, although SR-PSOX has a predictable phosphorylation site in the cytoplasmic domain [12
].
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Enhancing effect of metalloproteinase inhibitor on cell adhesion mediated by SR-PSOX/CXCL16
FNK was reported to be prototypically released from the cell surface by the function of metalloproteinase, and the soluble form thus generated functions as a chemoattractant similar to other members of the chemokine family [26
, 27
]. Given the possibility of a similar processing of the membrane-anchored SR-PSOX/CXCL16, we examined the effect of metalloproteinase inhibitor on the ratio of soluble-to-membrane-bound forms of SR-PSOX/CXCL16. The release of sSR-PSOX from COS-hSR-PSOX cells was clearly inhibited by a metalloproteinase inhibitor GM6001, and cell-surface and cell-associated hSR-PSOX expression was increased by the treatment (Fig. 5A
5B
5C
5D
). This prompted us to examine the effect of the metalloproteinase inhibitor on SR-PSOX/CXCL16-mediated adhesion activity. As expected from the increased cell-surface expression of SR-PSOX, more L-hCXCR6 cells were found to bind to GM6001-treated COS-hSR-PSOX cells than untreated COS-hSR-PSOX cells (Fig. 5E)
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONMATERIALS AND METHODSRESULTSDISCUSSIONREFERENCES |
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SR-PSOX and CXCR6 regulate the processes of chemotaxis as well as direct adhesion. The Gi protein blocker, PTX, can inhibit CXCR6-mediated migratory activity, however, by indicating that activation of Gi protein is necessary for the induction of the chemotactic response. In contrast, adhesion occurs even in the presence of PTX (Fig. 3)
. These findings are similar to those reported for FNK [8
]. Indeed, the adhesion between cells expressing SR-PSOX and those expressing CXCR6 can be induced, independent of the activation of G protein or the activation of integrins.
COS-7 cells expressing SR-PSOX without its mucin domain were shown to have impaired adhesion activity, although COS-7 cells expressing a hybrid with the chemokine domain of hSR-PSOX and the mucin domain of FNK efficiently bind L-hCXCR6 cells (Fig. 4) . These results indicate that the chemokine domain of SR-PSOX/CXCL16 only determines specificity for CXCR6, and the mucin domain of SR-PSOX/CXCL16 is necessary for the efficient adhesion. The mucin domain of FNK was also shown to contribute to the efficient adhesion activity of CX3CR1-expressing cells (Fig. 4B) . However, the mucin domain is unlikely to determine the specificity of the cell adhesion directly, as the mucin domain of FNK when substituted for that of SR-PSOX is functional in terms of adhesion activity for CXCR6-expressing cells. Cell adhesion is mediated by direct protein–protein interactions, which may require some distance from the cell surface as discussed previously [8 , 24 , 25 ]. Thus, the mucin domain of SR-PSOX/CXCL16 may function as a necessary presenting structure of the chemokine domain, which provides some distance from the cell surface for the chemokine domain to interact with CXCR6 on the surface of target cells.
We have shown the multiple functions of SR-PSOX/CXCL16, which include the scavenger receptor activity, the chemotaxis-inducing activity, and the direct cell-adhesion activity. We therefore suggest that SR-PSOX/CXCL16 plays multifunctional roles in DCs. The soluble form of SR-PSOX/CXCL16 generated by metalloproteinase cleavage recruits CXCR6-expressing, activated T cells and NKT cells via its chemotactic activity in cooperation with other chemokines. Then, the membrane-anchored form of SR-PSOX/CXCL16 on DCs can function as a cell-surface adhesion molecule for CXCR6-expressing T and NKT cells in cooperation with other adhesion molecules. Such adhesion may lead to bidirectional stimulatory signals and may contribute to the formation of docking sites for the activation of antigen-specific, primary and secondary T cell responses. Thus, SR-PSOX/CXCL16 may play a role in DC functions for primary and secondary immune responses. These possibilities are currently under investigation.
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ACKNOWLEDGEMENTS |
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Received October 9, 2003; accepted October 14, 2003.
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