Dipeptidyl peptidase IV inhibitors as new therapeutic agents for the treatment of Type 2 diabetes

Bibliography

• BAILEY CJ: Potential new treatments for Type 2 diabetes. Trends In Pharmacol Sci. (2000) 21:259–265.
   PubMed Web of Science ®Google Scholar
• ZHANG BB, MOLLER DE: New approaches in the treatment of Type 2 diabetes. Curr. Opin. Chem. Biol. (2000) 4:461–467.
   PubMed Web of Science ®Google Scholar
• HOLST JJ, ORSKOV C: Incretin hormones- an update. Scand. I Gin. Lab. Invest. (2001) 61\(Supp1.234):75–86.
   Google Scholar
• •A review describing the effects and potential therapeutical applications of incretin hormones.
   Google Scholar
• CREUTZFELDT W: The entero-insular axis in Type 2 diabetes - incretins as therapeutic agents. Exp. Clin. Endocrinol Diabetes(2001) 109\(Supp1.2):S288–S303.
   Google Scholar
• ••An excellent review on the actions ofincretin hormones as well as on the historical research leading to their discovery.
   Google Scholar
• NAUCK MA, STOCKMANN F, EBERT R, CREUTZFELDT W: Reduced incretin effect in Type 2 (non-insulin-dependent) diabetes. Diabetologia (1986) 29:46–52.
   PubMed Web of Science ®Google Scholar
• NAUCK MA, HEIMESAAT MM, ORSKOV C, HOLST JJ, EBERT R, CREUTZFELDT W: Preserved incretin activity of GLP-1 [7-36 amide] but not of synthetic human GIP in patients with Type-2-diabetes mellitus.' Gin. Invest. (1993) 91:301–307.
   PubMed Web of Science ®Google Scholar
• RACHMAN J, BARROW BA, LEVY IC, TURNER RC: Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide 1 (GLP-1) in subjects with NIDDM. Diabetologia (1997) 40:205–211.
   PubMed Web of Science ®Google Scholar
• NAUCK MA, WOLLSCHLAGER D, WERNER J, HOLST JJ, ORSKOV C, CREUTZFELDT W: Effects of subcutaneous glucagon-like peptide 1 (GLP-1 [7-36 amide]) in patients with NIDDM. Diabetologia (1996) 39:1546–1553.
   PubMed Web of Science ®Google Scholar
• KNUDSEN LB, PRIDAL L: Glucagon-likepeptide 1 [9 36] amide is a major metabolite of glucagon-like peptide 1 [7-36] amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor. Eur. Pharmacol (1996) 318:429–435.
   PubMed Web of Science ®Google Scholar
• DE MEESTER I, KOROM S, VAN DAMME J, SCHARPE S: CD26, let it cut or cut it down. Immunol Today (1999) 20:367–375.
   PubMedGoogle Scholar
• DE MEESTER I, DURINX C, BAL G et al.: Natural substrates of dipeptidyl peptidase IV. Adv. Exp. Med. Biol. (2000) 477:67–87.
   PubMed Web of Science ®Google Scholar
• MENTLEIN R: Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul Pept. (1999) 85:9–24.
   PubMed Web of Science ®Google Scholar
• ••An excellent review describing theinvolvement of DPP IV in the metabolism of regulatory peptides in vitro and in vivo.
   Google Scholar
• AUGUSTYNS K, BAL G, THONUS G et al: The unique properties of dipeptidyl-peptidase IV (DPP IV/CD26) and the therapeutic potential of DPP IV inhibitors. Curr. Med. Chem. (1999) 6:311–327.
   PubMed Web of Science ®Google Scholar
• ••The reader is referred to this review givingan excellent overview of the design and development of DPP IV inhibitors from the beginning of DPP IV research until 1998.
   Google Scholar
• VILLHAUER EB, COPPOLA GM, HUGHES TE: Chapter 19. DPP-IV inhibition and therapeutic potential. Ann. Rep. Med. Chem. (2001) 36:191–200.
   Web of Science ®Google Scholar
• MENTLEIN R, GALLWITZ B, SCHMIDT E: Dipeptidyl-peptidase IV hydrolyses gastric inhihitory polypeptide, glucagon-like peptide-1 [7-36] amide, peptide histidine methionine and is responsible for their degradation in human serum. Ear: Biochem. (1993) 214:829–835.
   PubMedGoogle Scholar
• KIEFFER TJ, MCINTOSH CHS, PEDERSON RA: Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology (1998) 136:3585–3596.
   Google Scholar
• HANSEN L, DEACON CE ORSKOV C, HOLST JJ: 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 theL cells of the porcine intestine. Endocrinology(1999) 140:5356–5363.
   PubMed Web of Science ®Google Scholar
• DEACON CE NAUCK MA, TOFT-NIELSEN M, PRIDAL L, WILLMS B, HOLST JJ: Both subcutaneously and intravenously administered glucagon-like peptide I are rapidly degraded from the NH2-terminus in Type II diabetic patients and in healthy subjects. Diabetes (1995) 44:1126–1131.
   PubMed Web of Science ®Google Scholar
• HOLST JJ: Glucagon-like peptide-1, a gastrointestinal hormone with a pharmaceutical potential. Carr. Med. Chem. (1999) 6:1005–1017.
   PubMedGoogle Scholar
• DRUCKER DJ: Development of glucagon-likepeptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Carr. Pharm. Des. (2001) 7:1399–1412.
   PubMed Web of Science ®Google Scholar
• DEACON CE HUGHES TE, HOLST JJ: Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes (1998) 47:764–769.
   PubMed Web of Science ®Google Scholar
• MARGUET D, BAGGIO L, KOBAYASHI T et al.: Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Proc. Nat. Acad. Std. USA (2000) 97:6874–6879.
   PubMed Web of Science ®Google Scholar
• NAGAKURA T, YASUDA N, aYAMAZAKI K et al.: Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient fischer rats. Biochem. Biophys. Res. Comm. (2001) 284:501–506.
   PubMed Web of Science ®Google Scholar
• YASUDA N, NAGAKURA T, YAMAZAKI K, INOUE T, TANAKA I: Improvement of high fat-diet-induced insulin resistance in dipeptidyl peptidase IV-deficient Fischer rats. Life Sci. (2002) 71:227–238.
   PubMed Web of Science ®Google Scholar
• SEDO A, MALIK R: Dipeptidylpeptidase IV-like molecules: homologous proteins or homologous activities? Biochim. Biophys. Acta (2001) 1550:107–116.
   PubMed Web of Science ®Google Scholar
• SCHON E, BORN I, DEMUTH HU et a/.: Dipeptidyl peptidase IV in the immune system: effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes. Biol. Chem. Hoppe Seyler (1991) 372:305–311.
   Google Scholar
• •One of the first papers describing the effects of DPP IV inhibitors.
   Google Scholar
• AUGUSTYNS K, LAMBEIR AM, BORLOO M et al: Pyrrolidides: synthesis and structure-activity relationship as inhibitors of dipeptidyl peptidase IV. Ear: Med. Chem. (1997) 32:301–309.
   Google Scholar
• ASH WORTH DM, ATRASH B, BAKER GR et al: 2-cyanopyrrolidides as potent, stable inhibitors of dipeptidyl peptidase IV. Bioorg. Med. Chem. Lett. (1996) 6:1163–1166.
   Google Scholar
• •This paper describes an extensive structure-activity relationship of aminoacyl pyrrolidides and 2-cyanopyrrolidides as DPP IV inhibitors.
   Google Scholar
• LI J, WILK E, WILK S: Aminoacylpyrrolidine-
   Google Scholar
• -nitriles: potent and stable inhibitors of dipeptidyl-peptidase IV (CD 26). Arch. Biochem. Biophys. (1995) 323:148–154.
   Google Scholar
• ••The first paper on 2-cyanopyrrolidides asDPP IV inhibitors.
   Google Scholar
• SUDRE B, BROQUA P, WHITE RB et al:Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male Zucker diabetic fatty rats. Diabetes (2002) 51:1461–1469.
   PubMed Web of Science ®Google Scholar
• ASHWORTH DM, ATRASH B, BAKER GR et al.: 4-cyanothiazolididies as very potent, stable inhibitors of dipeptidyl peptidase IV Bioorg. Med. Chem. Lett. (1996) 6:2745–2748.
   Google Scholar
• GUTHEIL WG, BACHOVCHIN WW: Separation of L-Pro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV. Biochemistry (1993) 32:8723–8731.
   PubMedGoogle Scholar
• FLENTKE GR, MUNOZ E, HUBER BT, PLAUT AG, KETTNER CA, BACHOVCHIN WW: 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. Proc. Natl. Acad. Sci. USA (1991) 88:1556–1559.
   PubMed Web of Science ®Google Scholar
• DEMUTH HU, NEUMANN U, BARTH A: Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: mechanistic investigations. I Enzym. Inhibit. (1989) 2:239–248.
   PubMedGoogle Scholar
• BODUSZEK B, OLEKSYSZYN J, KAM CM, SELZLER J, SMITH RE, POWERS JC: Dipeptide phosphonates as inhibitors of dipeptidyl peptidase IV. I Med. Chem. (1994) 37:3969–3976.
   PubMed Web of Science ®Google Scholar
• LAMBEIR AM, BORLOO M, DE MEESTER I et al.: Dipeptide-derived diphenyl phosphonate esters: mechanism-based inhibitors of dipeptidyl peptidase IV. Biochim. Biophys. Acta (1996) 1290:76–82.
   Google Scholar
• DE MEESTER I, BELYAEV A, LAMBEIR AM et al.: In vivo inhibition of dipeptidyl peptidase IV activity by pro-pro-diphenyl-phosphonate (Prodipine). Biochem. Pharmacol (1997) 54:173–179.
   PubMedGoogle Scholar
• STOCKEL MA, MRESTANI-KLAUS C, STIEBITZ B, DEMUTH HU, NEUBERT K: Thioxo amino acid pyrrolidides and thiazolidides: new inhibitors of proline specific peptidases. Biochim. Biophys. Acta (2000) 1479:15–31.
   PubMedGoogle Scholar
• SENTEN K, VAN DER VEKEN P, BAL G et al.: Development of potent and selective dipeptidyl peptidase II inhibitors. Bioorg. Med. Chem. Lett. (2002) 12:2825–2828.
   Google Scholar
• HUGHES TE, MONE MD, RUSSELL ME, WELD ON SC, VILLHAUER EB: NVP-DPP728: (1-[[[2-[(5-cyanopyridin-2-Aamino]ethyflaminolacety11-2-cyano-(5)-ryrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV Biochemistry (1999) 38:11597–11603.
   Google Scholar
• ••This paper describes the mechanism ofaction of one of the most potent and selective DPP IV inhibitors described today.
   Google Scholar
• VILLHAUER EB, BRINKMAN JA, NADERI GB et al.:1- [2-[(5-cyanopyridin-2-yl) amino] -ethylamino] acetyl- 2-(5) - pyrrolidine-carbonitrile: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. .1. Med. Chem. (2002) 45:2362–2365.
   Google Scholar
• HUGHES TE, RUSSELL ME, BOLOGNESE L: NVP-LAF237, a highly selective and long-acting dipeptidyl peptidase IV inhibitor. Diabetes (2002) 51 (Supp1.2):A67.
   Google Scholar
• ZHAO K, LIM DS, FUNAKI T, WELCH JT: Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1-fluoro-propylidene)- cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic. Bioorg. Med. Chem. (2003) 11:207–215.
   PubMedGoogle Scholar
• LIN J, TOSCANO PJ, WELCH JT: Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidy1-0-hydroxylamine peptidomimetics. Proc. Natl. Acad. Sci. USA (1998) 95:14020–14024.
   PubMedGoogle Scholar
• BELYAEV A, ZHANG XM, AUGUSTYNS K et al.: Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors. Med. Chem. (1999) 42:1041–1052.
   Google Scholar
• NO AUTHORS LISTED: BDPX. Drug Data Report (2002) 24:620.
   Google Scholar
• YAMADA M, OKAGAKI C, HIGASHIJIMA T, TANAKA S, OHNUKI T, SUGITA T: A potent dipeptide inhibitor of dipeptidyl peptidase IV. Bioorg. Med. Chem. Lett. (1998) 8:1537–1540.
   PubMedGoogle Scholar
• OHNUKI T, YAMADA M, SUGITA T: Novel dipeptidyl peptidase IV inhibitors with antiarthritic effects. Drugs of the Future (1999) 24:665–670.
   Google Scholar
• COPPOLA GM, ZHANG YL, SCHUSTER HF, RUSSELL ME, HUGHES TE: 1-aminomethylisoquinoline-4-carboxylates as novel dipeptidylpeptidase IV inhibitors. Bioorg. Med. Chem. Lett. (2000) 10:1555–1558.
   PubMedGoogle Scholar
• PAULY RP, DEMUTH HU, ROSCHE F et al.: Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor ile-thiazolidide. Metabolism (1999) 48:385–389.
   PubMed Web of Science ®Google Scholar
• PEDERSON RA, WHITE HA, SCHLENZIG D, PAULY RP, MCINTOSH CHS, DEMUTH HU: Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes (1998) 47:1253–1258.
   PubMed Web of Science ®Google Scholar
• POSPISILIK JA, STAFFORD SG, DEMUTH HU et al: Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and I3-cell glucose responsiveness in VDF (fa/fa) Zucker rats. Diabetes (2002) 51:943–950.
   PubMed Web of Science ®Google Scholar
• SORBERA LA, REVEL L, CASTANERJ: P32/98. Antidiabetic, dipeptidyl-peptidase IV inhibitor. Drugs of the Future (2001) 26:859–864.
   Web of Science ®Google Scholar
• DEACON CF, DANIELSEN P, KLARSKOV L, OLESEN M, HOLST JJ: Dipeptidyl peptidase IV inhibition reduces the degradation and clearance of GIP and potentiates its insulinotropic and antihyperglycemic effects in anesthetized pigs. Diabetes (2001) 50:1588–1597.
   PubMed Web of Science ®Google Scholar
• AHREN B, HOLST JJ, MARTENSSON H,BALKAN B: Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice. Eur. I Pharmacol (2000) 404:239–245.
   PubMed Web of Science ®Google Scholar
• BALKAN B, KWASNIK L, MISERENDINO R, HOLST JJ, LI X: Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 [7-36 amide] concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia (1999) 42:1324–1331.
   PubMed Web of Science ®Google Scholar
• AHREN B, SIMONSSON E, LARSSON H et al.: Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in Type 2 diabetes. Diabetes Care (2002) 25:869–875.
   PubMed Web of Science ®Google Scholar
• •This paper describes the potential application of a DPP IV inhibitor in Type 2 diabetic patients.
   Google Scholar
• DEACON CF, WAMBERG S, BIE P, HUGHES TE, HOLST JJ: Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs. .1. Endocrinol (2002) 172:355–362.
   PubMed Web of Science ®Google Scholar
• REIMER MK, HOLST JJ, AHREN B: Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice. Eur. Endocrinol. (2002) 146:717–727.
   PubMed Web of Science ®Google Scholar
• MITANI H, TAKIMOTO M, HUGHES TE, KIMURA M: Dipeptidyl peptidase IV inhibition improves impaired glucose tolerance in high-fat diet-fed rats: study using a Fischer 344 rat substrain deficient in its enzyme activity. fpn..1. Phannacol. (2002) 88:442–450.
   Google Scholar
• MITANI H, TAKIMOTO M, KIMURA M: Dipeptidyl peptidase IV inhibitor NVP-DPP728 ameliorates early insulin response and glucose tolerance in aged rats but not in aged Fischer 344 rats lacking its enzyme activity. Jpn.j Phannacol. (2002) 88:451–458.
   PubMedGoogle Scholar
• RASMUSSEN HB, BRANNER S, WIBERG FC, WAGTMANN N: Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. (2003) 10:19–25.
   PubMedGoogle Scholar
• ••The very recent publication of the crystal structure of DPP IV will certainly enhance the rational development of new DPP IV inhibitors.
   Google Scholar