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Dipeptidyl-peptidase 9

DPP9, DP9, dipeptidyl peptidase 9
This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. The protein has been shown to have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Although the activity of this protein is similar to that of dipeptidyl peptidase 4 (DPP4), it does not appear to be membrane bound. In general, dipeptidyl peptidases appear to be involved in the regulation of the activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. Several transcript variants of this gene have been described but not fully characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DPP8, DSP, CD26, Glucagon, Insulin
Papers on DPP9
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.
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
Dipeptidyl peptidase 9 (DPP9) is a member of the S9B/DPPIV (DPP4) serine protease family, which cleaves N-terminal dipeptides at an Xaa-Pro consensus motif.
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.
Pharmacological characterization of ZYDPLA1, a novel long-acting dipeptidyl peptidase-4 inhibitor.
Desai et al., Ahmadābād, India. In J Diabetes, Sep 2015
ZYDPLA1 was more than 7000-fold selective for recombinant DPP-4 relative to DPP-8 and DPP-9, and more than 60 000-fold selective relative to fibroblast activation protein (FAP) in vitro.
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
Dipeptidyl peptidase 9 (DPP9) is a ubiquitously expressed member of the DPP4 gene and protease family.
Establishment of a dipeptidyl peptidases (DPP) 8/9 expressing cell model for evaluating the selectivity of DPP4 inhibitors.
Shen et al., Beijing, China. In J Pharmacol Toxicol Methods, 2015
With the increased concern of non-selectivity and toxicities caused by DPP4 inhibitors, it is essential to establish new ex vivo system to investigate DPP4 inhibitors' effect on DPP8 and DPP9.
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).
Genome-wide identification of housekeeping genes in maize.
Zhao et al., Nanjing, China. In Plant Mol Biol, 2014
Among them, nine genes (2OG-Fe, CDK, DPP9, DUF, NAC, RPN, SGT1, UPF1 and a hypothetical protein coding gene) were expressed in all 40 maize diverse genotypes tested covering 16 tissues at more than 20 developmental stages under normal and stress conditions, implying these as being the most reliable reference genes.
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.
Genome-wide association study identifies multiple susceptibility loci for pulmonary fibrosis.
Schwartz et al., Denver, United States. In Nat Genet, 2013
We confirmed association with TERT at 5p15, MUC5B at 11p15 and the 3q26 region near TERC, and we identified seven newly associated loci (Pmeta = 2.4 × 10(-8) to 1.1 × 10(-19)), including FAM13A (4q22), DSP (6p24), OBFC1 (10q24), ATP11A (13q34), DPP9 (19p13) and chromosomal regions 7q22 and 15q14-15.
Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9.
Chen et al., Taiwan. In Febs Lett, 2011
residues important for dimer formation and enzymatic activity
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.
A novel role of dipeptidyl peptidase 9 in epidermal growth factor signaling.
Gorrell et al., Sydney, Australia. In Mol Cancer Res, 2011
These findings suggest an important signaling role of DPP9 in the regulation of survival and proliferation pathways.
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 DP9 in chronic lymphocytic leukemia.
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
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