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Gene Review

DPP4  -  dipeptidyl-peptidase 4

Sus scrofa

Synonyms: ADABP, CD26, DPPIV
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Disease relevance of DPPIV


High impact information on DPPIV

  • Dipeptidyl peptidase IV (DP-IV; dipeptidyl-peptide hydrolase, EC is a serine protease with a specificity for cleaving Xaa-Pro dipeptides from polypeptides and proteins [5].
  • In the crystal structure of porcine DPPIV, the observed tetramer formation was suggested to mediate epithelial and lymphocyte cell-cell adhesion [6].
  • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig [7].
  • Glucagon-like peptide 1 (GLP-1) has been proposed as a new therapeutic agent in the management of diabetes because of its glucose-dependent stimulation of insulin secretion, but this is limited by its rapid degradation in vivo by dipeptidyl peptidase IV (DPP IV) [7].
  • Employing identical methods used previously in MDCK cells, it was found that both direct and transcytotic pathways are involved in the apical surface localization of DPPIV in this epithelial cell type [1].

Chemical compound and disease context of DPPIV


Biological context of DPPIV

  • When candoxatril was co-administered with valine pyrrolidide (a DPP-IV inhibitor), changes in C-terminal GLP-1 pharmacokinetics mirrored those seen when candoxatril alone was administered (t(1/2) 2.7+/-0.3 and 7.7+/-0.8 min; MCR 17.3+/-2.6 and 6.5+/-0.8 for valine pyrrolidide without and with candoxatril, respectively) [8].
  • In transfected Madin-Darby canine kidney (MDCK) cells using domain-selective biotinylation and streptavidin absorption, it was, however, shown that DPPIV is directly sorted to the apical surface (Low, S. H., Wong, S. H., Tang, B. L. Subramaniam, V. N., and Hong, W. (1991) J. Biol. Chem, 266, 13391-13396) [1].
  • The porcine DPPIV promoter lacks a consensus TATA-box, but contains two TATA-like sequences [9].
  • Different deletion constructs of the DPPIV 5'-flanking region in front of the CAT gene were analyzed for transient CAT-expression after transfection of the intestinal Caco-2 cell line [9].
  • Docking experiments with the compact rigid 58 residue protein aprotinin, which had been shown to be processed by DPIV, indicate that the Arg1-Pro2 N terminus can access the DPIV active site only upon widening of its side openings, probably by separation of the first and the last propeller blades, and/or of the catalytic and the propeller domain [10].

Anatomical context of DPPIV


Associations of DPPIV with chemical compounds


Regulatory relationships of DPPIV


Other interactions of DPPIV


Analytical, diagnostic and therapeutic context of DPPIV

  • The effects of various inhibitors were studied on the biogenesis of endopeptidase-24.11 (EC and dipeptidyl peptidase IV (EC in slices of renal cortex, from piglets of the Yucatan strain, maintained in organ culture [14].
  • Radioautography established that aminopeptidases M and A, dipeptidyl peptidase IV and neutral endopeptidase were transmembrane proteins [20].
  • Both IgG preparations caused loss of DPP IV from the organs studied, as shown by reduction in enzyme activity in tissue homogenates and by immunofluorescence microscopy, which showed loss of DPP IV from cell surface [21].
  • The subcellular distribution of the plasma membrane ectoenzymes, aminopeptidase N (aminopeptidase M) and dipeptidyl peptidase IV, has been examined by fractionating homogenates of porcine striata by a discontinuous Percoll gradient centrifugation procedure which distinguishes fractions containing pre- and post-synaptic elements [22].
  • Plasma samples were analyzed by radioimmunoassays allowing determination of intact, biologically active GLP-2 and the DPP-IV metabolite GLP-2 (3-33) [23].


  1. Involvement of both vectorial and transcytotic pathways in the preferential apical cell surface localization of rat dipeptidyl peptidase IV in transfected LLC-PK1 cells. Low, S.H., Wong, S.H., Tang, B.L., Hong, W.J. J. Biol. Chem. (1991) [Pubmed]
  2. Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis. Jobin, M.C., Martinez, G., Motard, J., Gottschalk, M., Grenier, D. J. Bacteriol. (2005) [Pubmed]
  3. Chemical modification of dipeptidyl peptidase iv: involvement of an essential tryptophan residue at the substrate binding site. Harada, M., Hiraoka, B.Y., Fukasawa, K.M., Fukasawa, K. Arch. Biochem. Biophys. (1984) [Pubmed]
  4. Mechanism of proline-specific proteinases: (I) Substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum. Heins, J., Welker, P., Schönlein, C., Born, I., Hartrodt, B., Neubert, K., Tsuru, D., Barth, A. Biochim. Biophys. Acta (1988) [Pubmed]
  5. Inhibition of dipeptidyl aminopeptidase IV (DP-IV) by Xaa-boroPro dipeptides and use of these inhibitors to examine the role of DP-IV in T-cell function. Flentke, G.R., Munoz, E., Huber, B.T., Plaut, A.G., Kettner, C.A., Bachovchin, W.W. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  6. Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface. Weihofen, W.A., Liu, J., Reutter, W., Saenger, W., Fan, H. J. Biol. Chem. (2004) [Pubmed]
  7. Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Deacon, C.F., Hughes, T.E., Holst, J.J. Diabetes (1998) [Pubmed]
  8. Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig. Plamboeck, A., Holst, J.J., Carr, R.D., Deacon, C.F. Diabetologia (2005) [Pubmed]
  9. The TATA-less, GC-rich porcine dipeptidylpeptidase IV (DPPIV) promoter shows bidirectional activity. Qvist, H., Sjöström, H., Norén, O. Biol. Chem. (1998) [Pubmed]
  10. Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV. Engel, M., Hoffmann, T., Manhart, S., Heiser, U., Chambre, S., Huber, R., Demuth, H.U., Bode, W. J. Mol. Biol. (2006) [Pubmed]
  11. Loss of dipeptidylpeptidase IV activity in chronic rhinosinusitis contributes to the neurogenic inflammation induced by substance P in the nasal mucosa. Grouzmann, E., Monod, M., Landis, B., Wilk, S., Brakch, N., Nicoucar, K., Giger, R., Malis, D., Szalay-Quinodoz, I., Cavadas, C., Morel, D.R., Lacroix, J.S. FASEB J. (2002) [Pubmed]
  12. Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. Hansen, L., Deacon, C.F., Orskov, C., Holst, J.J. Endocrinology (1999) [Pubmed]
  13. Valine pyrrolidide preserves intact glucose-dependent insulinotropic peptide and improves abnormal glucose tolerance in minipigs with reduced beta-cell mass. Larsen, M.O., Rolin, B., Ribel, U., Wilken, M., Deacon, C.F., Svendsen, O., Gotfredsen, C.F., Carr, R.D. Exp. Diabesity Res. (2003) [Pubmed]
  14. Proteins of the kidney microvillar membrane. Effects of monensin, vinblastine, swainsonine and glucosamine on the processing and assembly of endopeptidase-24.11 and dipeptidyl peptidase IV in pig kidney slices. Stewart, J.R., Kenny, A.J. Biochem. J. (1984) [Pubmed]
  15. Is there a tripeptidyl peptidase in the renal brush-border membrane? Kenny, A.J., Ingram, J. Biochem. J. (1988) [Pubmed]
  16. Early weaning stimulates intestinal brush border enzyme activities in piglets, mainly at the posttranscriptional level. Marion, J., Petersen, Y.M., Romé, V., Thomas, F., Sangild, P.T., Le Dividich, J., Le Huërou-Luron, I. J. Pediatr. Gastroenterol. Nutr. (2005) [Pubmed]
  17. Biosynthesis of intestinal microvillar proteins. Pulse-chase labelling studies on maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV. Danielsen, E.M., Sjöström, H., Norén, O. Biochem. J. (1983) [Pubmed]
  18. Isolation and characterization of two distinct low-density, Triton-insoluble, complexes from porcine lung membranes. Parkin, E.T., Turner, A.J., Hooper, N.M. Biochem. J. (1996) [Pubmed]
  19. Membrane peptidases in the peripheral nervous system of the pig: their localization by immunohistochemistry at light and electron microscopic levels. Barnes, K., Bourne, A., Cook, P.A., Turner, A.J., Kenny, A.J. Neuroscience (1991) [Pubmed]
  20. Proteins of the kidney microvillar membrane. Asymmetric labelling of the membrane by lactoperoxidase-catalysed radioiodination and by photolysis of 3,5-di[125I]iodo-4-azidobenzenesulphonate. Booth, A.G., Kenny, A.J. Biochem. J. (1980) [Pubmed]
  21. In vivo modulation of CD26 (dipeptidyl peptidase IV) in the mouse: effects of polyreactive and monoreactive antibodies. Yamaguchi, N., Plant, C., Biancone, L., Bachovchin, W., McCluskey, R., Andres, G. Transplantation (1996) [Pubmed]
  22. Localization of aminopeptidase N and dipeptidyl peptidase IV in pig striatum and in neuronal and glial cell cultures. Barnes, K., Kenny, A.J., Turner, A.J. Eur. J. Neurosci. (1994) [Pubmed]
  23. Metabolism of glucagon-like peptide-2 in pigs: Role of dipeptidyl peptidase IV. Hansen, L., Hare, K.J., Hartmann, B., Deacon, C.F., Ugleholdt, R.K., Plamboeck, A., Holst, J.J. Regul. Pept. (2007) [Pubmed]
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