DPP8
DPP8 (dipeptidyl peptidase 8, also known as DP8, DPRP1 or MSTP141) is a cytoplasmic dipeptidyl peptidase of the peptidase S9B family. It removes N-terminal dipeptides from proteins with Pro or Ala at position 2 and restrains inflammasome activation in resting cells. Browse Assay Genie's current range of DPP8 research reagents below, or read on for the biology behind the target.
DPP8 is a dipeptidyl peptidase that cleaves N-terminal dipeptides from proteins carrying a Pro or Ala residue at position 2. It is also described as hydrolysing peptide substrates at a prolyl bond. Beyond this catalytic role, DPP8 acts as a key inhibitor of caspase-1-dependent pyroptosis in resting monocytes and macrophages. It does so by preventing activation of NLRP1 and CARD8.
Mechanistically, DPP8 sequesters the cleaved C-terminal fragments of NLRP1 and CARD8, which form the active part of the respective inflammasomes, in a ternary complex. This blocks their oligomerisation and activation. The dipeptidyl peptidase activity is required for this suppression, yet neither NLRP1 nor CARD8 is a bona fide DPP8 substrate. This suggests that one or more as yet unidentified substrates are needed for inflammasome inhibition.
The DPP8 gene encodes a member of the peptidase S9B family, DPPIV subfamily, and belongs to the DASH family in HGNC nomenclature. According to the RefSeq summary, the protein is ubiquitously expressed and hydrolyses the same substrates as dipeptidyl peptidase IV (DPP4), which suggests a possible role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described. Previous names include dipeptidylpeptidase 8, and the mouse ortholog is Dpp8.
DPP8 prevents NLRP1 and CARD8 activation in resting monocytes and macrophages, making it central to studies of caspase-1-dependent pyroptosis.
By holding the active fragments of NLRP1 and CARD8 in a ternary complex, DPP8 helps define how inflammasome signalling is kept in check.
DPP8 is ubiquitously expressed and shares substrates with DPP4, so it is studied for a possible role in T-cell activation.
DPP8 cleaves N-terminal dipeptides after Pro or Ala at position 2, and its relevant substrates for inflammasome control remain to be identified.
DPP8 is a cytoplasmic dipeptidyl peptidase that removes N-terminal dipeptides from proteins with Pro or Ala at position 2. In resting monocytes and macrophages it inhibits caspase-1-dependent pyroptosis by preventing activation of the NLRP1 and CARD8 inflammasomes.
DPP8 is also known as DP8, DPRP1, MSTP141, FLJ14920, FLJ20283 and MGC26191. Earlier names include dipeptidylpeptidase 8 and dipeptidyl-peptidase 8. The RefSeq entry notes that alternatively spliced transcript variants encode different isoforms.
DPP8 belongs to the peptidase S9B family, DPPIV subfamily. Like DPP4 it is ubiquitously expressed and hydrolyses the same substrates, hinting at a role in immune function. The mouse ortholog is Dpp8; check the datasheet of any product for its validated reactivity.
Other dipeptidyl peptidases, including the closely related DPP4 and DPP9, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q6V1X1; product specifications from Assay Genie datasheets.