Biology:DPP8
From HandWiki
 Generic protein structure example |
Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8 gene.[1][2]
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.[2] A relatively specific inhibitor of DPP8 and DPP9, Val-boroPro [3]-,[4] leads to increased activation of the inflammasome though both NLRBP1 and CARD8 and can trigger pyroptosis.[5]
References
- Notes
- ↑ "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8". Eur J Biochem 267 (20): 6140–50. Nov 2000. doi:10.1046/j.1432-1327.2000.01617.x. PMID 11012666.
- ↑ 2.0 2.1 "Entrez Gene: DPP8 dipeptidyl-peptidase 8". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54878.
- ↑ "PubChem:Val-boroPro". https://pubchem.ncbi.nlm.nih.gov/#query=Val-boroPro.
- ↑ "Inhibition of Dpp8/9 Activates the Nlrp1b Inflammasome". Cell Chemical Biology 25 (3): 262–267.e5. March 2018. doi:10.1016/j.chembiol.2017.12.013. PMID 29396289.
- ↑ "DPP8/DPP9 inhibitor-induced pyroptosis for treatment of acute myeloid leukemia". Nature Medicine 24 (8): 1151–1156. August 2018. doi:10.1038/s41591-018-0082-y. 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. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- 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. 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. 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. PMID 16344560.
- 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. 575. 63–72. doi:10.1007/0-387-32824-6_7. ISBN 978-0-387-29058-4.
- "Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis". FEBS J. 273 (11): 2447–60. 2006. 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.
 |
