Establishment of a dipeptidyl peptidases (DPP) 8/9 expressing cell model for evaluating the selectivity of DPP4 inhibitors

J Pharmacol Toxicol Methods. 2015 Jan-Feb:71:8-12. doi: 10.1016/j.vascn.2014.11.002. Epub 2014 Nov 15.

Abstract

Introduction: Dipeptidyl peptidases (DPPs) 8 and 9 are homologous, cytoplasmic postproline-cutting enzymes, which have similar enzymatic activity and preferred substrates as DPP4. DPP4 is a well-known target for treating diabetes mellitus. 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.

Method: Here we reported a newly established cell model system by cloning and transfecting human DPP8/9 genes into HEK 293 cells. We then used this model to evaluate the clinically applied DPP4 inhibitors' effect on DPP8/9, by direct enzymatic activity assay. Given the difference of cellular locations between DPP4 and DPP8/9, we also evaluated the influence of these drugs on intracellular DPP8/9 activity and cell viability by extracellular treatment with different inhibitors.

Results: Direct enzymatic activity assay revealed significant and concentration-dependent inhibition effect of vildagliptin, saxagliptin on DPP8/9. Extracellular incubation of DPP8/9 over expressed cells with sitagliptin, vildagliptin, saxagliptin, alogliptin and linagliptin, showed only mild inhibition on DPP8/9. Moreover, all of these drugs showed no significant influence on cell viability.

Discussion: Our results demonstrated that the DPP8/9 over-expressing cell model system is a very useful and promising system for investigating the selectivity and associated toxicity of DPP4 inhibitors on DPP8/9.

Keywords: cell model; dipeptidyl peptidases; inhibitors; selectivity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adamantane / analogs & derivatives*
  • Adamantane / chemistry
  • Adamantane / pharmacology
  • Cell Survival / drug effects
  • Dipeptidases / genetics*
  • Dipeptidases / metabolism
  • Dipeptides / chemistry
  • Dipeptides / pharmacology*
  • Dipeptidyl Peptidase 4 / metabolism
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / genetics*
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism
  • Dose-Response Relationship, Drug
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • HEK293 Cells
  • Humans
  • Models, Biological*
  • Nitriles / chemistry
  • Nitriles / pharmacology*
  • Pyrrolidines / chemistry
  • Pyrrolidines / pharmacology*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship
  • Vildagliptin

Substances

  • Dipeptides
  • Enzyme Inhibitors
  • Nitriles
  • Pyrrolidines
  • Recombinant Proteins
  • saxagliptin
  • Dipeptidases
  • DPP9 protein, human
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • DPP4 protein, human
  • DPP8 protein, human
  • Dipeptidyl Peptidase 4
  • Vildagliptin
  • Adamantane