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DCAL-1 A novel dendritic cell-associated C-type lectin regulated by CD40

DCAL-1 A novel dendritic cell-associated C-type lectin regulated by CD40

FASEB Journal 16(5): A1056

Protein-carbohydrate interactions serve multiple functions in the immune system, mediating pathogen recognition and cell-cell interactions. We have identified a novel C-type lectin-like molecule, DCAL-1 (dendritic cell associated lectin-1), using subtractive hybridization with tester cDNA derived from follicular dendritic cells (DCs). The full-length sequence was confirmed by RACE PCR and searching EST databases. DCAL-1 has a truncated carbohydrate recognition domain (CRD), missing 3 cysteine residues required to complete the CRD. DCAL-1 may form homo- or hetero dimers analogous to CD94/NKG2a. DCAL-1 has two splice variants; both are expressed by B cells, but only the short form is expressed by DCs. The splicing site is in the neck region of the lectin. DCAL-1 mRNA is expressed in DCs and B cells, but not in T cells, and is up regulated in B cells by anti-CD40 stimulation. Also, DCAL-1 mRNA is increased upon the differentiation of monocytes to CD1a+ DCs. Using a DCAL-1 fusion protein we have identified T cells as expressing DCAL-1 ligand. DCAL-1 enhanced the expression of CD25 but not CD69 on T cells. DCAL-1 modulated the proliferation of T cells to anti-CD3 stimulation, but did not alter cytokine secretion. However, co-incubation of DC-SIGN fusion protein and CD28/CD3 enhances IL-4 and inhibited IFN-a secretion by CD4+ T cells. The role of DCAL-1 in antigen uptake and pathogen recognition will be the subject of future studies.

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Accession: 034679395

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