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Dpp4  -  dipeptidylpeptidase 4

Mus musculus

Synonyms: Cd26, DPP IV, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, Dpp-4, ...
 
 
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Disease relevance of Dpp4

 

High impact information on Dpp4

 

Chemical compound and disease context of Dpp4

 

Biological context of Dpp4

  • These data indicate that the human Dpp4 locus is located within this synteny region (i.e., 2q14-q37) [9].
  • In conclusion, PACAP is inactivated by DPP IV and despite insulin-releasing effects, its actions on glucagon secretion and glucose homeostasis do not make it a good therapeutic tool for the treatment of type 2 diabetes [10].
  • Whilst DPP-IV is the most exhaustively studied peptidase in this class, relatively less is known about the inhibitor/substrate specificity of its close homolog seprase [11].
  • In this study, analysis of the similarity of secondary structures and amino acid sequences between these enzymes led us to identify several conserved residues likely to be involved in the catalytic site of these DPP IV-related enzymes [12].
  • In contrast, mutagenesis of two other aspartic residues (Asp599 and Asp657), also conserved between these DPP IV-related enzymes, did not affect the enzymatic properties of the mouse enzyme [12].
 

Anatomical context of Dpp4

  • Thymocyte-activating molecule (THAM) was initially characterized as a developmentally regulated, dimeric cell-surface molecule capable of activating mouse thymocytes and T lymphocytes upon monoclonal antibody (mAb)-mediated cross-linking [13].
  • We previously described a developmentally regulated, Mr 115,000 (reduced) and 110,000/128,000 (nonreduced) mouse T cell-activating molecule (THAM) also expressed on a variety of epithelial cell surfaces, and associated with neutral exoaminopeptidase activity [2].
  • WP inhibited dipeptidyl peptidase IV activity in the proximal small intestine by 50% (P < 0.05), suggesting that luminal degradation of WP generates small fragments, which are substrates for dipeptidyl peptidase IV and act as competitive inhibitors [14].
  • The effects of daily administration of a novel dipeptidyl peptidase IV-resistant glucagon-like peptide-1 (GLP-1) analog, (Val8)GLP-1, on glucose tolerance and pancreatic beta-cell function were examined in obese-diabetic (ob/ob) mice [15].
  • RESULTS: No statistical difference in the number of CFU-GM, BFU-E, or CFU-GEMM in the peripheral blood, bone marrow, or spleen of untreated WT vs untreated CD26(-/-) mice was observed [16].
 

Associations of Dpp4 with chemical compounds

  • AIMS/HYPOTHESIS: The rapid degradation and clearance of glucagon-like peptide-1 (GLP-1) by the enzymes dipeptidyl peptidase-IV and neutral endopeptidase 24.11 are the main impediments to the development of GLP-1 as a potential glucose-lowering agent [17].
  • Dipeptidyl peptidase IV (DPP-IV) and seprase belong to a small group of membrane-bound, proline-specific serine proteases, the serine integral membrane proteases (SIMPs) [11].
  • Against this background, we now wish to report on the design, synthesis, and kinetic testing of a series of dipeptide proline diphenyl phosphonates, against DPP-IV and seprase [11].
  • Dipeptidyl-peptidase IV (DPP IV, CD26, EC 3.4.14.5), a multifunctional ectoenzyme, is involved not only in the proteolytic cleavage of X-Pro from the NH2 terminus of a variety of biologically active peptides, but also in activation signal transduction and cell matrix adherence processes [12].
  • Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases [12].
 

Physical interactions of Dpp4

  • RESULTS: The results reveal that glycation of the N-terminus of GLP-1 or GIP stabilized both peptides against DPP-IV degradation [18].
 

Regulatory relationships of Dpp4

 

Other interactions of Dpp4

  • Glucose-dependent insulinotrophic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) are important enteroendocrine hormones that are rapidly degraded by an ubiquitous enzyme dipeptidyl peptidase IV to yield truncated metabolites GIP(3-42) and GLP-1(9-36)amide [20].
  • Jejunal ApN and DPPIV activities were lower for obese mice before resection; ileal ApN activity was unaltered after resection for both strains [21].
  • Pituitary adenylate cyclase-activating peptide (PACAP): assessment of dipeptidyl peptidase IV degradation, insulin-releasing activity and antidiabetic potential [10].
  • Our observations provide evidence for a relationship between DPP IV and leptin [22].
  • CONCLUSIONS: CD26 plays a critical role in G-CSF-induced mobilization of HPC [16].
 

Analytical, diagnostic and therapeutic context of Dpp4

References

  1. Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance. Conarello, S.L., Li, Z., Ronan, J., Roy, R.S., Zhu, L., Jiang, G., Liu, F., Woods, J., Zycband, E., Moller, D.E., Thornberry, N.A., Zhang, B.B. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV). Vivier, I., Marguet, D., Naquet, P., Bonicel, J., Black, D., Li, C.X., Bernard, A.M., Gorvel, J.P., Pierres, M. J. Immunol. (1991) [Pubmed]
  3. The binding site of human adenosine deaminase for CD26/Dipeptidyl peptidase IV: the Arg142Gln mutation impairs binding to cd26 but does not cause immune deficiency. Richard, E., Arredondo-Vega, F.X., Santisteban, I., Kelly, S.J., Patel, D.D., Hershfield, M.S. J. Exp. Med. (2000) [Pubmed]
  4. Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Marguet, D., Baggio, L., Kobayashi, T., Bernard, A.M., Pierres, M., Nielsen, P.F., Ribel, U., Watanabe, T., Drucker, D.J., Wagtmann, N. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Purification and characterization of mouse fetal liver epithelial cells with high in vivo repopulation capacity. Nierhoff, D., Ogawa, A., Oertel, M., Chen, Y.Q., Shafritz, D.A. Hepatology (2005) [Pubmed]
  6. Targeting dipeptidyl peptidase IV (CD26) suppresses autoimmune encephalomyelitis and up-regulates TGF-beta 1 secretion in vivo. Steinbrecher, A., Reinhold, D., Quigley, L., Gado, A., Tresser, N., Izikson, L., Born, I., Faust, J., Neubert, K., Martin, R., Ansorge, S., Brocke, S. J. Immunol. (2001) [Pubmed]
  7. Redistribution of glomerular dipeptidyl peptidase type IV in experimental lupus nephritis. Demonstration of decreased enzyme activity at the ultrastructural level. van Leer, E.H., Bruijn, J.A., Prins, F.A., Hoedemaeker, P.J., de Heer, E. Lab. Invest. (1993) [Pubmed]
  8. Effects of the Combination of a Dipeptidyl Peptidase IV Inhibitor and an Insulin Secretagogue on Glucose and Insulin Levels in Mice and Rats. Yamazaki, K., Yasuda, N., Inoue, T., Yamamoto, E., Sugaya, Y., Nagakura, T., Shinoda, M., Clark, R., Saeki, T., Tanaka, I. J. Pharmacol. Exp. Ther. (2007) [Pubmed]
  9. Structure of the mouse dipeptidyl peptidase IV (CD26) gene. Bernard, A.M., Mattei, M.G., Pierres, M., Marguet, D. Biochemistry (1994) [Pubmed]
  10. Pituitary adenylate cyclase-activating peptide (PACAP): assessment of dipeptidyl peptidase IV degradation, insulin-releasing activity and antidiabetic potential. Green, B.D., Irwin, N., Flatt, P.R. Peptides (2006) [Pubmed]
  11. Dipeptide proline diphenyl phosphonates are potent, irreversible inhibitors of seprase (FAPalpha). Gilmore, B.F., Lynas, J.F., Scott, C.J., McGoohan, C., Martin, L., Walker, B. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  12. Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases. David, F., Bernard, A.M., Pierres, M., Marguet, D. J. Biol. Chem. (1993) [Pubmed]
  13. cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases. Marguet, D., Bernard, A.M., Vivier, I., Darmoul, D., Naquet, P., Pierres, M. J. Biol. Chem. (1992) [Pubmed]
  14. Glucose-induced incretin hormone release and inactivation are differently modulated by oral fat and protein in mice. Gunnarsson, P.T., Winzell, M.S., Deacon, C.F., Larsen, M.O., Jelic, K., Carr, R.D., Ahrén, B. Endocrinology (2006) [Pubmed]
  15. Novel glucagon-like peptide-1 (GLP-1) analog (Val8)GLP-1 results in significant improvements of glucose tolerance and pancreatic beta-cell function after 3-week daily administration in obese diabetic (ob/ob) mice. Green, B.D., Lavery, K.S., Irwin, N., O'harte, F.P., Harriott, P., Greer, B., Bailey, C.J., Flatt, P.R. J. Pharmacol. Exp. Ther. (2006) [Pubmed]
  16. CD26 is essential for normal G-CSF-induced progenitor cell mobilization as determined by CD26-/- mice. Christopherson, K.W., Cooper, S., Hangoc, G., Broxmeyer, H.E. Exp. Hematol. (2003) [Pubmed]
  17. PEGylated glucagon-like peptide-1 displays preserved effects on insulin release in isolated pancreatic islets and improved biological activity in db/db mice. Lee, S., Youn, Y.S., Lee, S.H., Byun, Y., Lee, K.C. Diabetologia (2006) [Pubmed]
  18. A comparison of the cellular and biological properties of DPP-IV-resistant N-glucitol analogues of glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide. Green, B.D., Gault, V.A., O'Harte, F.P., Flatt, P.R. Diabetes, obesity & metabolism. (2005) [Pubmed]
  19. Inhibition of dipeptidyl peptidase IV (DP IV, CD26) activity abrogates stress-induced, cytokine-mediated murine abortions. Hildebrandt, M., Arck, P.C., Kruber, S., Demuth, H.U., Reutter, W., Klapp, B.F. Scand. J. Immunol. (2001) [Pubmed]
  20. Effects of sub-chronic exposure to naturally occurring N-terminally truncated metabolites of glucose-dependent insulinotrophic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1), GIP(3-42) and GLP-1(9-36)amide, on insulin secretion and glucose homeostasis in ob/ob mice. Parker, J.C., Lavery, K.S., Irwin, N., Green, B.D., Greer, B., Harriott, P., O'harte, F.P., Gault, V.A., Flatt, P.R. J. Endocrinol. (2006) [Pubmed]
  21. Altered small intestinal absorptive enzyme activities in leptin-deficient obese mice: influence of bowel resection. Kiely, J.M., Noh, J.H., Svatek, C.L., Pitt, H.A., Swartz-Basile, D.A. J. Pediatr. Surg. (2006) [Pubmed]
  22. Evidence for an interaction between leptin, T cell costimulatory antigens CD28, CTLA-4 and CD26 (dipeptidyl peptidase IV) in BCG-induced immune responses of leptin- and leptin receptor-deficient mice. Rüter, J., Hoffmann, T., Demuth, H.U., Moschansky, P., Klapp, B.F., Hildebrandt, M. Biol. Chem. (2004) [Pubmed]
  23. The expression of T-cell surface antigens CTLA-4, CD26, and CD28 is modulated by inhibition of dipeptidylpeptidase IV (DPP IV, CD26) activity in murine stress-induced abortions. Rüter, J., Hoffmann, T., Heiser, U., Demuth, H.U., Arck, P.C., Klapp, B.F., Hildebrandt, M. Cell. Immunol. (2002) [Pubmed]
  24. Quantitative gene expression analysis reveals transition of fetal liver progenitor cells to mature hepatocytes after transplantation in uPA/RAG-2 mice. Cantz, T., Zuckerman, D.M., Burda, M.R., Dandri, M., Göricke, B., Thalhammer, S., Heckl, W.M., Manns, M.P., Petersen, J., Ott, M. Am. J. Pathol. (2003) [Pubmed]
 
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