
pmid: 16920484
A soluble form of CD83 ("sCD83") has been shown to block DC-mediated T cell stimulation in vitro and an immunosuppressive role has also been shown in vivo using an experimental-autoimmune-encephalomyelits (EAE) model. Using recombinant mutational analyses, recently, we could show that sCD83 forms a homo-dimer, whereby four cysteines are involved in the intra-molecular disulfide bonds and the fifth cysteine is responsible for the inter-molecular bridging of the two molecules. Further studies revealed that the two CD83-isoforms, i.e. the dimer and the monomer, have a similar inhibitory capacity when tested in vitro. Here we show that the biological (in vivo) half-life of the two sCD83 isoforms is comparable and was between 2 and 3h. In addition, using the EAE-model, we were able to show that a monomeric-mutant isoform of soluble CD83 has a similar inhibitory activity in vivo when compared with a dimeric-wildtype isoform.
Membrane Glycoproteins, Immunoglobulins, Mice, Inbred C57BL, Mice, Antigens, CD, CD83 Antigen, Mutation, Animals, Humans, Protein Isoforms, Female, Dimerization
Membrane Glycoproteins, Immunoglobulins, Mice, Inbred C57BL, Mice, Antigens, CD, CD83 Antigen, Mutation, Animals, Humans, Protein Isoforms, Female, Dimerization
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