Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8gene.[5][6]
This gene encodes a member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. The encoded protein shares similarity with Dipeptidyl peptidase-4 in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.[6]
Jiaang WT; Chen YS; Hsu T; et al. (2005). "Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8". Bioorg. Med. Chem. Lett. 15 (3): 687–91. doi:10.1016/j.bmcl.2004.11.023. PMID15664838. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Ogasawara W; Tanaka C; Suzuki M; et al. (2005). "Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role of the signal sequence and overexpression in Escherichia coli". Protein Expr. Purif. 41 (2): 241–51. doi:10.1016/j.pep.2004.10.027. PMID15866709. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Yu DM; Wang XM; Ajami K; et al. (2006). DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis. Advances in Experimental Medicine and Biology. Vol. 575. pp. 63–72. doi:10.1007/0-387-32824-6_7. ISBN978-0-387-29058-4. PMID16700509. {{cite book}}: |journal= ignored (help); Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Yu DM, Wang XM, McCaughan GW, Gorrell MD (2006). "Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis". FEBS J. 273 (11): 2447–60. doi:10.1111/j.1742-4658.2006.05253.x. PMID16704418.