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Dipeptidyl-peptidase 8

DPP8, DP8, dipeptidyl peptidase 8
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 IV 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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DPP9, DSP, CD26, Glucagon, ACID
Papers on DPP8
Unravelling the immunological roles of dipeptidyl peptidase 4 (DPP4) activity and/or structure homolog (DASH) proteins.
von Hörsten et al., Stuttgart, Germany. In Clin Exp Immunol, Jan 2016
Apart from DPP4, DASH proteins include fibroblast activation protein alpha (FAP), dipeptidyl peptidase 8 (DPP8), dipeptidyl peptidase 9 (DPP9), dipeptidyl peptidase 4-like protein 1 (DPL1, DPP6, DPPX L, DPPX S), dipeptidyl peptidase 4-like protein 2 (DPL2, DPP10) from the DPP4-gene family S9b and structurally unrelated enzyme dipeptiyl peptidase 2 (DPP2), displaying DPP4-like activity.
Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions.
Rajarathnam et al., Galveston, United States. In Biochem J, Dec 2015
To resolve these issues, we characterized the binding of a series of heparin-derived oligosaccharides [heparin disaccharide (dp2), heparin tetrasaccharide (dp4), heparin octasaccharide (dp8) and heparin 14-mer (dp14)] to the wild-type (WT) dimer and a designed monomer using solution NMR spectroscopy.
The Dipeptidyl Peptidases 4, 8, and 9 in Mouse Monocytes and Macrophages: DPP8/9 Inhibition Attenuates M1 Macrophage Activation in Mice.
De Meester et al., Antwerp, Belgium. In Inflammation, Nov 2015
Family members DPP8 and 9 are abundantly present in macrophage-rich regions of atherosclerotic plaques, and DPP9 inhibition attenuates activation of human M1 macrophages in vitro.
Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.
Stephens et al., Sydney, Australia. In Febs J, Oct 2015
Moreover, we also identified the dipeptide Val-Ala as a consensus site for DPP9 cleavage that was not recognized by DPP8, suggesting different in vivo roles for these closely related enzymes.
Design, Synthesis and Biological Evaluation of Imidazo[1,2-a]pyridine Derivatives as Novel DPP-4 Inhibitors.
Zhang et al., Nanjing, China. In Chem Biol Drug Des, Oct 2015
Based on docking binding model, structural modifications of 2-benzene ring and pyridine moieties of compound 5a led to the identification of compound 5d with 2, 4-dichlorophenyl group at the 2-position as a potent (IC50  = 0.13 μm), selective (DPP-8/DPP-4 = 215 and DPP-9/DPP-4 = 192) and in vivo efficacious DPP-4 inhibitor.
High structural resolution hydroxyl radical protein footprinting reveals an extended Robo1-heparin binding interface.
Sharp et al., Athens, United States. In J Biol Chem, May 2015
For the first time, we utilized electron transfer dissociation-based high spatial resolution hydroxyl radical protein footprinting to identify two separate binding sites for heparin interaction with Robo1: one binding site at the previously identified site for heparin dp8 and a second binding site at the N terminus of Robo1 that is disordered in the x-ray crystal structure.
Dipeptidyl peptidase 9 subcellular localization and a role in cell adhesion involving focal adhesion kinase and paxillin.
Gorrell et al., Sydney, Australia. In Biochim Biophys Acta, Feb 2015
DPP9 gene silencing and treatment with a DPP8/DPP9 specific inhibitor both reduced cell adhesion and migration.
The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis.
De Meester et al., Antwerp, Belgium. In Front Immunol, 2014
In this review, we provide a comprehensive discussion on the role of prolyl-specific peptidases DPPIV, FAP, DPP8, DPP9, dipeptidyl peptidase II, prolyl carboxypeptidase, and prolyl oligopeptidase in the immune system and its diseases.
Inhibition of dipeptidyl peptidase 8/9 impairs preadipocyte differentiation.
Osborn et al., Minneapolis, United States. In Sci Rep, 2014
The dipeptidyl peptidase (DPP) 4 family includes four enzymes, DPP4, DPP8, DPP9 and fibroblast activation protein (FAP).
An essential signal peptide peptidase identified in an RNAi screen of serine peptidases of Trypanosoma brucei.
Mottram et al., Glasgow, United Kingdom. In Plos One, 2014
We also found no effect on parasite survival in an animal host when the S9 peptidases oligopeptidase B, prolyl oligopeptidase or dipeptidyl peptidase 8 were targeted.
Composition, sequencing and ion mobility mass spectrometry of heparan sulfate-like octasaccharide isomers differing in glucuronic and iduronic acid content.
Turnbull et al., United States. In Eur J Mass Spectrom (chichester, Eng), 2014
Here we report ion mobility mass spectrometry (IMMS) separation and tandem mass spectrometry (MS(2)) sequencing methods used to analyze and differentiate six synthetically produced heparin/heparan sulfate (HS)-like octasaccharide (dp8) isomeric structures.
The pharmacokinetic considerations and adverse effects of DPP-4 inhibitors [corrected].
Elisaf et al., Thessaloníki, Greece. In Expert Opin Drug Metab Toxicol, 2014
DPP-4 inhibitors have certain differences in their structure, metabolism, route of elimination and selectivity for DPP-4 over structurally related enzymes, such as DPP-8/DPP-9.
Dipeptidyl peptidase IV inhibitors: a new paradigm in type 2 diabetes treatment.
Sastry et al., Hyderābād, India. In Curr Drug Targets, 2014
Though several clinical trial compounds were discontinued because of severe adverse toxic effects that are associated with other prolyldipeptidases include DPP8 and DPP9.
Establishment of a selective evaluation method for DPP4 inhibitors based on recombinant human DPP8 and DPP9 proteins.
Shen et al., Beijing, China. In Acta Pharm Sin B, 2014
As members of the same gene family, dipeptidyl peptidase 8 (DPP8) and dipeptidyl peptidase 9 (DPP9) share high sequence and structural homology as well as functional activity with DPP4.
Advances in understanding the expression and function of dipeptidyl peptidase 8 and 9.
Gorrell et al., Australia. In Mol Cancer Res, 2013
DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the rare ability to cleave a post-proline bond two residues from the N-terminus of a substrate.
Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
Van der Veken et al., Antwerp, Belgium. In J Med Chem, 2011
Data identify modification points in the topology of a representative DPP8/9-inhibitor, capable of rendering selectivity for DPP8 over DPP9.
Expression and prognostic assessment of dipeptidyl peptidase IV and related enzymes in B-cell chronic lymphocytic leukemia.
Kuss et al., Adelaide, Australia. In Cancer Biol Ther, 2010
This is the first study to demonstrate the presence of DP8 in chronic lymphocytic leukemia (CLL) and the upregulation of DP8 mRNA in CLL.
Expression of dipeptidyl peptidase-IV activity and/or structure homologs in human meningiomas.
Sedo et al., Praha, Czech Republic. In Int J Oncol, 2010
DPP8 and DPP9 prevail over canonical DPP-IV/CD26 and FAPalpha in all examined meningioma patients
The in vivo expression of dipeptidyl peptidases 8 and 9.
Gorrell et al., Sydney, Australia. In J Histochem Cytochem, 2009
DP8 and DP9 tissue and cellular expression
Enzyme activity and immunohistochemical localization of dipeptidyl peptidase 8 and 9 in male reproductive tissues.
De Meester et al., Antwerp, Belgium. In J Histochem Cytochem, 2009
We showed the expression of DPP8 and DPP9 in the testis, epididymis, and sperm. [DPP9]
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