Granzyme B (GrB) is single chain and single domain serine protease. GrB is member of the chymotrypsin superfamily. GrB is synthesised as an inactive preproenzyme and transported into the endoplasmatic reticulum (ER) as proGrB. ProGrB, covalently modified with a mannose-6-phosphate (M6P) group, is transported in ER-derived vesicles to the Golgi apparatus (GA). Within the secretory granules, granzymes are stored in association with the chondroitin sulphate containing proteoglycan serglycin (SG). The GrB molecule alone has a high positive surface charge, but when GrB binds to SG its charge may be substantially neutralized. The newly synthesised GrB is heterogeneously glycosylated. The mature enzyme has two potential glycosylation sites. The process of GrB glycosylation results in generation of both the 32 and 35 kDa glycosylated forms of GrB. The 32 kDa GrB forms contain high mannose oligosaccharide moieties and accumulate in cytotoxic T lymphocytes (CTLs) after T cell receptor (TCR) stimulation. In contrast, the 35 kDa GrB forms, which possess only the complex oligosaccharide groups, are not stored in CTLs and instead they are secreted through the constitutive calcium-independent secretory pathway after TCR activation. GrB is the most abundant serene protease stored in secretory granules of CTLs and NK cells. GrB can be produced by plasmacytoid dendritic cells (pecs). GrB-induced cell death is a primary mechanism in cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells to eliminate harmful target cells including allogeneic, virally infected and tumor cells. This mechanism implies activation of several pro-apoptotic pathways by direct proteolysis. The mannose 6-phosphate receptor has been identified as the plasma membrane receptor for GrB.
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