DPP8

DPP8
Identifiers
Aliases	DPP8 , DP8, DPRP1, MSTP141, MST097, MSTP097, MSTP135, DPRP-1, dipeptidyl peptidase 8
External IDs	OMIM: 606819; MGI: 1921638; HomoloGene: 57098; GeneCards: DPP8; OMA:DPP8 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q22.31 Start 65,442,463 bp [1] End 65,517,704 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 C Start 64,939,696 bp [2] End 64,989,933 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell secondary oocyte nipple middle temporal gyrus pons postcentral gyrus Skeletal muscle tissue of rectus abdominis lateral nuclear group of thalamus Brodmann area 23 biceps brachii Top expressed in spermatocyte muscle of thigh superior frontal gyrus aortic valve cerebellar cortex dentate gyrus of hippocampal formation granule cell ascending aorta temporal muscle inferior colliculi perirhinal cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity serine-type peptidase activity aminopeptidase activity dipeptidyl-peptidase activity hydrolase activity Cellular component cytoplasm cytosol Biological process immune response proteolysis apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54878 74388 Ensembl ENSG00000074603 ENSMUSG00000032393 UniProt Q6V1X1 Q80YA7 RefSeq (mRNA) NM_017743 NM_130434 NM_197960 NM_197961 NM_001320875 NM_001320876 NM_028906 NM_001401136 RefSeq (protein) NP_001307804 NP_001307805 NP_060213 NP_569118 NP_932064 NP_932065 NP_932064.1 NP_001307804.1 NP_083182 NP_001388065 Location (UCSC) Chr 15: 65.44 – 65.52 Mb Chr 9: 64.94 – 64.99 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8 gene. ^{[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] A relatively specific inhibitor of DPP8 and DPP9, Val-boroPro ^[7] -, ^[8] leads to increased activation of the inflammasome though both NLRBP1 and CARD8 and can trigger pyroptosis. ^[9]

References

Notes

1. GRCh38: Ensembl release 89: ENSG00000074603 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032393 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Abbott CA, Yu DM, Woollatt E, Sutherland GR, McCaughan GW, Gorrell MD (Nov 2000). "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8". Eur J Biochem. 267 (20): 6140–50. doi: 10.1046/j.1432-1327.2000.01617.x . PMID   11012666.
6. "Entrez Gene: DPP8 dipeptidyl-peptidase 8".
7. "PubChem:Val-boroPro".
8. Okondo MC, Rao SD, Taabazuing CY, Chui AJ, Poplawski SE, Johnson DC, Bachovchin DA (March 2018). "Inhibition of Dpp8/9 Activates the Nlrp1b Inflammasome". Cell Chemical Biology. 25 (3): 262–267.e5. doi:10.1016/j.chembiol.2017.12.013. PMC   5856610 . PMID   29396289.
9. Johnson DC, Taabazuing CY, Okondo MC, Chui AJ, Rao SD, Brown FC, Reed C, Peguero E, de Stanchina E, Kentsis A, Bachovchin DA (August 2018). "DPP8/DPP9 inhibitor-induced pyroptosis for treatment of acute myeloid leukemia". Nature Medicine. 24 (8): 1151–1156. doi:10.1038/s41591-018-0082-y. PMC   6082709 . PMID   29967349.

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Ajami K, Abbott CA, Obradovic M, et al. (2003). "Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family". Biochemistry. 42 (3): 694–701. doi:10.1021/bi026846s. PMID   12534281.
• Qi SY, Riviere PJ, Trojnar J, et al. (2003). "Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases". Biochem. J. 373 (Pt 1): 179–89. doi:10.1042/BJ20021914. PMC   1223468 . PMID   12662155.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Shu H, Chen S, Bi Q, et al. (2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Mol. Cell. Proteomics. 3 (3): 279–86. doi: 10.1074/mcp.D300003-MCP200 . PMID   14729942.
• Chen YS, Chien CH, Goparaju CM, et al. (2004). "Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells". Protein Expr. Purif. 35 (1): 142–6. doi:10.1016/j.pep.2003.12.019. PMID   15039077.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• 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. PMID   15664838.
• 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. PMID   15866709.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• Yu DM, Wang XM, Ajami K, et al. (2006). "DP8 and DP9 have Extra-Enzymatic Roles in Cell Adhesion, Migration and Apoptosis". Dipeptidyl Aminopeptidases. Advances in Experimental Medicine and Biology. Vol. 575. pp. 63–72. doi:10.1007/0-387-32824-6_7. ISBN   978-0-387-29058-4. PMID   16700509.
• 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 . PMID   16704418.
• Lee HJ, Chen YS, Chou CY, et al. (2007). "Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8". J. Biol. Chem. 281 (50): 38653–62. doi: 10.1074/jbc.M603895200 . PMID   17040910.