Cloning, recombinant expression and biochemical characterization of the murine CD83 molecule which is specifically upregulated during dendritic cell maturation

Human CD83 (hCD83) is a glycoprotein expressed predominantly on the surface of dendritic cells (DC) and represents the best marker for mature DC. Here , we report the cloning of the cDNA encoding mouse CD83 (mCD83) from a muri ne bone marrow-derived DC (BM-DC) cDNA library, DNA sequence analysis revea led a 196 amino acid protein including a signal peptide of 21 amino acids w hich shares 63% amino acid identity with hCD83, Using Northern blot analyse s, mCD83 mRNA was found to be strongly expressed in mouse BM-DC and its exp ression was upregulated following stimulation with LPS or TNF-alpha. Transf ection experiments using COS-7 cells revealed that mCD83 is glycosylated. F urthermore, the extracellular CD83 domain was recombinantly expressed in Es cherichia coli and one-dimensional NMR data strongly support that the prote in is structurally folded. (C) 1999 Federation of European Biochemical Soci eties.