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The Journal of Immunology, 2007, 179, 6052 -6063
Copyright © 2007 by The American Association of Immunologists, Inc.
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The Novel Endocytic and Phagocytic C-Type Lectin Receptor DCL-1/CD302 on Macrophages Is Colocalized with F-Actin, Suggesting a Role in Cell Adhesion and Migration1

Masato Kato2,*, Seema Khan*, Elisabetta d’Aniello*, Kylie J. McDonald* and Derek N. J. Hart*,{dagger}

* Dendritic Cell Program, Mater Medical Research Institute, South Brisbane, Queensland, Australia; and {dagger} School of Medicine, University of Queensland, Herston, Queensland, Australia

C-type lectin receptors play important roles in mononuclear phagocytes, which link innate and adaptive immunity. In this study we describe characterization of the novel type I transmembrane C-type lectin DCL-1/CD302 at the molecular and cellular levels. DCL-1 protein was highly conserved among the human, mouse, and rat orthologs. The human DCL-1 (hDCl-1) gene, composed of six exons, was located in a cluster of type I transmembrane C-type lectin genes on chromosomal band 2q24. Multiple tissue expression array, RT-PCR, and FACS analysis using new anti-hDCL-1 mAbs established that DCL-1 expression in leukocytes was restricted to monocytes, macrophages, granulocytes, and dendritic cells, although DCL-1 mRNA was present in many tissues. Stable hDCL-1 Chinese hamster ovary cell transfectants endocytosed FITC-conjugated anti-hDCL-1 mAb rapidly (t1/2 = 20 min) and phagocytosed anti-hDCL-1 mAb-coated microbeads, indicating that DCL-1 may act as an Ag uptake receptor. However, anti-DCL-1 mAb-coated microbead binding and subsequent phagocytic uptake by macrophages was ~8-fold less efficient than that of anti-macrophage mannose receptor (MMR/CD206) or anti-DEC-205/CD205 mAb-coated microbeads. Confocal studies showed that DCL-1 colocalized with F-actin in filopodia, lamellipodia, and podosomes in macrophages and that this was unaffected by cytochalasin D, whereas the MMR/CD206 and DEC-205/CD205 did not colocalize with F-actin. Furthermore, when transiently expressed in COS-1 cells, DCL-1-EGFP colocalized with F-actin at the cellular cortex and microvilli. These data suggest that hDCL-1 is an unconventional lectin receptor that plays roles not only in endocytosis/phagocytosis but also in cell adhesion and migration and thus may become a target for therapeutic manipulation.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 This work was supported by grants from National Health and Medical Research Council of Australia, and Mater Medical Research Institute.

2 Address correspondence and reprint request to Dr. Masato Kato, Mater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland, 4101 Australia. E-mail address: mkato{at}mmri.mater.org.au

3 Abbreviations used in this paper: Mo, monocyte; BDC, blood dendritic cell; BDCA, BDC Ag; BLAST, basic local alignment search tool; CHO, Chinese hamster ovary; CP, cytoplasmic domain; CTLD, C-type lectin-like domain; DAPI, 4',6-diamidino-2-phenylindole; DC, dendritic cell; DCL-1, DEC-205-associated C-type lectin 1; DC-SIGN, DC-specific ICAM-3 grabbing nonintegrin; EGFP, enhanced GFP; GAM, goat anti-mouse; IgG, F(ab')2; hDCL-1, human DCL-1; hDEC-205, human DEC-205; IP, immunoprecipitation; Lin, lineage; LSM, laser scanning microscope/microscopy; MGL, macrophage C-type galactose/N-acetyl galactosamine-specific lectin; MMR, macrophage mannose receptor; MoDC, monocyte-derived dendritic cell; Mph, macrophage; PFA, paraformaldehyde; pI, isoelectric point; PLA2R, phospholipase A2 receptor; SP, signal peptide; WB, Western blot.




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