The thymus specific serine protease or TSSP was identified in the late 90’s by two different laboratories1,2. It is the third member of the S28 group of serine proteases, the first member being Prolyl Carboxypeptidase (PRCP) and the second the dipeptidyl peptidase II (DPPII). It is named a serine protease with respect to its suspected enzymatic activity due to the presence of three amino acids (Serine, Aspartate and Histidine) in regions highly similar to the ones forming the catalytic site of PRCP.3,4

PRSS16, the gene encoding TSSP is predominantly expressed in the cortical thymic epithelial cells (cTEC) and to a lesser extend in different immunologically relevant tissues.1,2,4,5 In cTEC TSSP localizes in endosomes, where it possibly plays a role as a protease in the class II presentation pathway that shapes, by yet unknown mechanisms, the peptide repertoire presented by TEC and DC in the thymus.6

TSSP has been associated with different auto-immune diseases like diabetes mellitus type I, where mouse experiments showed a protective effect of TSSP absence. This protective effect is probably due to the impaired thymic selection of CD4+ T cells specific for islet antigens.5

We are currently trying to express the recombinant human TSSP protein, this can help us elucidate the enzymatic activity and other characteristics of this protein.

Literature