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
Gene location (Human)
Chr.	Chromosome 15 (human)
End	65,517,704 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	64,989,933 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; nipple; ; middle temporal gyrus; ; pons; ; postcentral gyrus; ; Brodmann area 23; ; biceps brachii; ; superior vestibular nucleus; ; palpebral conjunctiva; ; jejunum;
	Top expressed in
	spermatocyte; ; superior frontal gyrus; ; aortic valve; ; cerebellar cortex; ; ascending aorta; ; temporal muscle; ; inferior colliculus; ; entorhinal cortex; ; spermatid; ; primary motor cortex;
	More reference expression data
	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
	54878
	74388
	ENSG00000074603
	ENSMUSG00000032393
	Q6V1X1
	Q80YA7
NM_017743 ; NM_130434 ; NM_197960 ; NM_197961 ; NM_001320875 ;
	NM_001320876
	NM_028906 ; NM_001401136
NP_001307804 ; NP_001307805 ; NP_060213 ; NP_569118 ; NP_932064 ;
	NP_932065 ; NP_932064.1 ; NP_001307804.1
	NP_083182 ; NP_001388065
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 09, 2024

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]

Related Research Articles

Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. In humans, it is encoded by the CTSC gene.

<span class="mw-page-title-main">Dipeptidyl peptidase-4</span> Mammalian protein found in humans

Dipeptidyl peptidase-4, also known as adenosine deaminase complexing protein 2 or CD26 is a protein that, in humans, is encoded by the DPP4 gene. DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].

Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human placental leucine aminopeptidase (PLAP), oxytocinase, and vasopressinase, is an enzyme of the aminopeptidase group that in humans is encoded by the LNPEP gene.

Tyrosine-protein kinase ITK/TSK also known as interleukin-2-inducible T-cell kinase or simply ITK, is a protein that in humans is encoded by the ITK gene. ITK is a member of the TEC family of kinases and is highly expressed in T cells.

Cartilage associated protein is a protein that in humans is encoded by the CRTAP gene.

Gamma-interferon-inducible protein Ifi-16 (Ifi-16) also known as interferon-inducible myeloid differentiation transcriptional activator is a protein that in humans is encoded by the IFI16 gene.

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene. ELGN2 is an alpha-ketoglutarate-dependent hydroxylase, a superfamily of non-haem iron-containing proteins.

Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that in humans is encoded by the FAP gene.

Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.

Dipeptidyl aminopeptidase-like protein 6 is a protein that in humans is encoded by the DPP6 gene.

40S ribosomal protein S10 is a protein that in humans is encoded by the RPS10 gene.

Attractin is a protein that in humans is encoded by the ATRN gene.

Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.

Inactive dipeptidyl peptidase 10 is a protein that in humans is encoded by the DPP10 gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Xaa-Pro aminopeptidase 1 is an enzyme that in humans is encoded by the XPNPEP1 gene.

Dipeptidyl peptidase 9 is an enzyme that in humans is encoded by the DPP9 gene.

Aminopeptidase B is an enzyme that in humans is encoded by the RNPEP gene.

Prolyl endopeptidase-like is an enzyme that in humans is encoded by the PREPL gene.

The PGPEP1 gene in humans encodes the enzyme Pyroglutamyl-peptidase I.

William W. Bachovchin is an American chemist/chemical biologist, academic and researcher. He is a professor of Molecular and Chemical Biology at Tufts University School of Medicine, and the founder of three biopharmaceutical companies: Point Therapeutics, Arisaph Pharmaceuticals, and Bach BioSciences.

References

Notes

1 2 3 GRCh38: Ensembl release 89: ENSG00000074603 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032393 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: DPP8 dipeptidyl-peptidase 8".
↑ "PubChem:Val-boroPro".
↑ 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.
↑ 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000074603 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid11012666-5] 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.

[entrez-6] 1 2 "Entrez Gene: DPP8 dipeptidyl-peptidase 8".

[7] "PubChem:Val-boroPro".

[pmid29396289-8] 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.

[pmid29967349-9] 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.

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