| DPP8/9 inhibition attenuates the TGF-beta1-induced excessive deposition of extracellular matrix (ECM) in human mesangial cells via Smad and Akt signaling pathways. | DPP8/9 inhibition attenuates the TGF-β1-induced excessive deposition of extracellular matrix (ECM) in human mesangial cells via Smad and Akt signaling pathways.
Li K, Zhang Y, Zhao W, Wang R, Li Y, Wei L, Wang L, Chen X, Chen Z, Liu P, Nie N, Tian X, Fu R. | 05/9/2024 |
| Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells. | Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the proximal renal tubule epithelial cells.
Zhang Y, Li K, Li Y, Zhao W, Wang L, Chen Z, Ma X, Yao T, Wang J, Dong W, Li X, Tian X, Fu R. | 02/12/2022 |
| Decrease of the pro-inflammatory M1-like response by inhibition of dipeptidyl peptidases 8/9 in THP-1 macrophages - quantitative proteomics of the proteome and secretome. | Decrease of the pro-inflammatory M1-like response by inhibition of dipeptidyl peptidases 8/9 in THP-1 macrophages - quantitative proteomics of the proteome and secretome.
Suski M, Wiśniewska A, Kuś K, Kiepura A, Stachowicz A, Stachyra K, Czepiel K, Madej J, Olszanecki R. | 12/5/2020 |
| Data show when cells were treated with siRNA-dipeptidyl peptidase 8 (DPP8), the expression of cyclin D1, matrix metalloproteinases, secreted MMP2 and MMP9 was downregulated. | Targeting dipeptidyl peptidase 8 genes inhibits proliferation, migration and invasion by inhibition of cyclin D1 and MMP2MMP9 signal pathway in cervical cancer.
Chen Y, Liu F, Wu K, Wu W, Wu H, Zhang W. | 09/21/2019 |
| The DPP8 expressing cell model system is a very useful and promising system for investigating the selectivity and associated toxicity of DPP4 inhibitors on DPP8. | Establishment of a dipeptidyl peptidases (DPP) 8/9 expressing cell model for evaluating the selectivity of DPP4 inhibitors.
Huan Y, Jiang Q, Liu JL, Shen ZF. | 04/23/2016 |
| The SUMO1-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9. | The SUMO1-E67 interacting loop peptide is an allosteric inhibitor of the dipeptidyl peptidases 8 and 9.
Pilla E, Kilisch M, Lenz C, Urlaub H, Geiss-Friedlander R., Free PMC Article | 01/25/2014 |
| Suggest roles for DPP8 and DPP9 in lymphocyte activation and apoptosis and in hepatocytes during liver disease pathogenesis. | Regulation of dipeptidyl peptidase 8 and 9 expression in activated lymphocytes and injured liver.
Chowdhury S, Chen Y, Yao TW, Ajami K, Wang XM, Popov Y, Schuppan D, Bertolino P, McCaughan GW, Yu DM, Gorrell MD., Free PMC Article | 01/4/2014 |
| DPP8 was found in macrophages of carotid atherosclerotic plaque and may play a role in disease progression. | Dipeptidyl peptidases in atherosclerosis: expression and role in macrophage differentiation, activation and apoptosis.
Matheeussen V, Waumans Y, Martinet W, Van Goethem S, Van der Veken P, Scharpé S, Augustyns K, De Meyer GR, De Meester I. | 08/31/2013 |
| analysis of dipeptidyl peptidases 8 and 9 reveals that they may have compensatory roles | Identifying natural substrates for dipeptidyl peptidases 8 and 9 using terminal amine isotopic labeling of substrates (TAILS) reveals in vivo roles in cellular homeostasis and energy metabolism.
Wilson CH, Indarto D, Doucet A, Pogson LD, Pitman MR, McNicholas K, Menz RI, Overall CM, Abbott CA., Free PMC Article | 08/10/2013 |
| this study demonstrates for the first time that DP8 and DP9 are expressed in breast and ovarian carcinoma cell lines | Expression profiling of dipeptidyl peptidase 8 and 9 in breast and ovarian carcinoma cell lines.
Wilson CH, Abbott CA. | 01/26/2013 |
| Data identify modification points in the topology of a representative DPP8/9-inhibitor, capable of rendering selectivity for DPP8 over DPP9. | Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?
Van Goethem S, Matheeussen V, Joossens J, Lambeir AM, Chen X, De Meester I, Haemers A, Augustyns K, Van der Veken P. | 12/10/2011 |
| 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 and prognostic assessment of dipeptidyl peptidase IV and related enzymes in B-cell chronic lymphocytic leukemia.
Sulda ML, Abbott CA, Macardle PJ, Hall RK, Kuss BJ. | 02/5/2011 |
| DPP8 and DPP9 prevail over canonical DPP-IV/CD26 and FAPalpha in all examined meningioma patients | Expression of dipeptidyl peptidase-IV activity and/or structure homologs in human meningiomas.
Stremenová J, Mares V, Lisá V, Hilser M, Krepela E, Vanicková Z, Syrucek M, Soula O, Sedo A. | 03/8/2010 |
| DP8 and DP9 tissue and cellular expression | The in vivo expression of dipeptidyl peptidases 8 and 9.
Yu DM, Ajami K, Gall MG, Park J, Lee CS, Evans KA, McLaughlin EA, Pitman MR, Abbott CA, McCaughan GW, Gorrell MD., Free PMC Article | 01/21/2010 |
| DP8 cleavage of the N-terminal two residues of IP10 (CXCL10), ITAC (CXCL11) and SDF-1 (CXCL12), is reported. | Stromal cell-derived factors 1alpha and 1beta, inflammatory protein-10 and interferon-inducible T cell chemo-attractant are novel substrates of dipeptidyl peptidase 8.
Ajami K, Pitman MR, Wilson CH, Park J, Menz RI, Starr AE, Cox JH, Abbott CA, Overall CM, Gorrell MD. | 01/21/2010 |
| cells overexpressing DP8 exhibit behavioral changesin the presence of ECM components; these effects were independent of enzyme activity | DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis.
Yu DM, Wang XM, Ajami K, McCaughan GW, Gorrell MD. | 01/21/2010 |
| study has identified the residues absolutely required for the optimal activity of DPP8 and its unique substrate specificity | Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8.
Lee HJ, Chen YS, Chou CY, Chien CH, Lin CH, Chang GG, Chen X. | 01/21/2010 |
| Dipeptidyl peptidase 8 and dipeptidyl peptidase 9 influence cell-extracellular matrix interactions, and thus may regulate tissue remodeling. | Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis.
Yu DM, Wang XM, McCaughan GW, Gorrell MD. | 01/21/2010 |