26
Views
0
CrossRef citations to date
0
Altmetric
Review

Patent focus on antidiabetic agents: September 1999 - February 2000

Pages 787-801 | Published online: 25 Feb 2005

Bibliography

  • THE DIABETES CONTROL AND COMPLICATIONS TRIALRESEARCH GROUP: The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. N Engl. J. Med. (1993) 329:977–986.
  • UNITED KINGDOM PROSPECTIVE DIABETES GROUP:Intensive blood-glucose control with sulfonylureas or insulin compared with conventional treatment and risk of complications in patients with Type 2 diabetes (UKPDS 33). Lancet (1998) 352:837–853.
  • SHINKAI H: Novel antidiabetic agents. Exp. Opin. Ther. Patents (2000) 10:59–66.
  • REAVEN G: Role of insulin resistance in human disease. Diabetes (1988) 37:1595–1607.
  • LEHMANN JM, MOORE LB, SMITH-OLIVER TA, WILKISON WO, WILLSON TM, KLIEWER SA: An antidiabetic thiazolidinedione is a high affinity ligand for peroxi-some proliferator-activated receptor y (PPARy). J. Biol. Chem. (1995) 270:12953–12956.
  • ••First report indicating that PPARy is the molecular target forTZDs and is associated with antidiabetic actions.
  • LENHARD JM, KLIEWER SA, PAULIK MA, PLUNKET KD, LEHMANN JM, WEIEL JE: Effects of troglitazone and metformin on glucose and lipid metabolism. Biochem. Pharmacol. (1997) 54:801–808.
  • MANGLESDORF DJ, EVANS RM: The RXR heterodimers and orphan receptors. Cell (1995) 83:841–850.
  • ROSE ML, PAULIK MA, LENHARD JM: Therapeutic approaches to Type 2 diabetes mellitus. Exp. Opin. Ther. Patents (1999) 9:1223–1236.
  • •Comprehensive and timely overview covering PPARy, RXR, I33-adrenoceptors and uncoupling proteins as anabolic and catabolic targets for treating diabetes.
  • BRUN RP, SPIEGELMAN BM: Obesity and the adipocyte. PPARy and the molecular control of adipogenesis. J. Endocrinol. (1997) 155:217–218.
  • SPIEGELMAN BM: PPAR-y: adipogenic regulator and thiazolidinedione receptor. Diabetes (1998) 47:507–514.
  • HULIN B, NEWTON LS, LEWIS DM et al: Hypoglycemic activity of a series of a-alkylthio and a-alkoxy carboxylic, acids related to ciglitazone. J. Med. Chem. (1996) 39:3897–3907.
  • BUCKLE DR, CANTELLO BCC, CAWTHORNE MA et al.:Non thiazolidinedione antihyperglycemic agents. 1: a-heteroatom substituted p-phenylpropanoic acids. Bioorg. Med. Chem. Lett. (1996) 6:2121–2126.
  • MUKHERJEE R, DAVIES PJA, CROMBIE DL et al.: Sensitiza-tion of diabetic and obese mice to insulin by retinoid X receptor agonists. Nature (1997) 386:407–410.
  • ••RXR agonists are suggested to be effective antidiabeticagents.
  • HARING HU: The insulin receptor: signalingmechanism and contribution to the pathogenesis of insulin resistance. Diabetologia (1991) 34:848–861.
  • WHITE MF, KAHN CR: The insulin signaling system. J.Biol. Chem. (1994) 269:1–4.
  • BACKER JM, MYERS MG JR, SHOELSON SE et al: Thephosphatidylinositol 3-kinase is activated by associa-tion with IRS-1 during insulin stimulation. EMBO J. (1992) 11:3469–3479.
  • CROSS DAE, ALESSI DR, COHEN P, ANDJELKOVICH M, HEMMINGS BA: Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature (1995) 378:785–789.
  • KOHN AD, SUMMERS SA, BIRNBAUM MJ, ROTH RA: Expression of a constitutively active Akt ser/thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter translocation. J. Biol. Chem. (1996) 271:31372–31378.
  • KENNER KA, ANYANWU E, OLEFSKY JM, KUSARI J: Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. (1996) 271:19810–19816.
  • ELCHEBLY M, PAYETTE P, MICHALISZYN E et al: Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science (1999) 283:1544–1548.
  • ••PTP-1B knockout mice demonstrate phenotype indicativeof an essential role of PTP-1B in insulin resistance.
  • EVANS JL, JALLAL B: Protein tyrosine phosphatases: their, role in insulin action and potential as drug targets. Exp. Opin. Invest. Drugs (1999) 8:139-160.•Excellent review of PTPases, especially PTP- IB as it relates to diabetes therapy.
  • WROBEL J, SREDY J, MOXHAM C eta].: PTP1B inhibition and, antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[b]naphtho[2,3-d]furans and 11-arylbenzo[b]naphtho[2,3-4thiophenes. J. Med. Chem. (1999) 42:3199–3202.
  • ••First demonstration of an orally-active, small moleculePTP-1B inhibitor.
  • MALAMAS MS, SREDY J, GUNAWAN I et al.: New azolidin- diones, as inhibitors of protein tyrosine phosphatase 1B with antihyperglycemic properties. J. Med. Chem. (2000) 43:995–1010.
  • LAWRENCE JC, JR., ROACH PJ: New insights into the role and mechanism of glycogen synthase activation by insulin. Diabetes (1997) 46:541–547.
  • ELDAR-FINKELMAN H, KREBS EG: Phosphorylation of insulin receptor substrate-1 by glycogen synthase kinase-3 impairs insulin action. Proc. Natl. Acad. Sci. USA (1997) 94:9660–9664.
  • CONSOLI A: Role of liver pathophysiology of NIDDM. Diabetes Care (1992) 15:430–441.
  • PILKIS SJ, GRANNER DK: Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Ann. Rev. Physiol. (1992) 54:885–909.
  • •Excellent review of the gluconeogenic and glycolytic pathways in the liver.
  • STALMANS W, DE WULF H, HUE L, HERS HG: The sequen- tial, inactivation of glycogen phosphorylase and activation of glycogen synthase in liver after admini-stration of glucose to mice and rats. The mechanism of the hepatic threshold to glucose. Int. J. Biochem. (1974) 41:127–134.
  • ROTHMAN D, MAGNUSSON I, KATZ L, SHULMAN R, SHULMAN G: Quantitation of hepatic glycogenolysis and gluconeogenesis in fasting humans with 13C NMR. Science (1991) 254:573–575.
  • NORDLIE RC, BODE AM, FOSTER JD: Recent advances in hepatic glucose-6-phosphatase regulation and function. Proc. Soc. Exp. Biol. Med. (1993) 203:274–285.
  • SUKALSKI KA, NORDLIE RC: Glucose-6-phosphatase: two concepts of membrane-function relationship. Adv. Enzymol. Relat. Areas Mol. Biol. (1989) 62:93–117.
  • BURGER HJ, ARION WJ, SWAMY KS, KNAUF M, VERTESY L, HERLING AW: Kodiastatin, a new inhibitor from Aspergillus terreus of the hepatic glucose-6-phophatase system. Diabetes (1999) Suppl. I:A260.
  • HERLING AW, BURGER HJ, SCHWAB D, HEMMERLE H, BELOW P, SCHUBERT G: Pharmacodynamic profile of a novel inhibitor of the hepatic glucose-6-phophatase system. Diabetes (1998) Suppl. I:A293.
  • SCHINDLER PW, BELOW P, HEMMERLE H et al.: Identifi-cation of two new inhibitors of the hepatic glucose-6-phosphatase system. Drug Dev. Res. (1998) 44:34–30.
  • HEMMERLE H, BURGER HJ, BELOW P et al.: Chlorogenic acids and synthetic chlorogenic acid derivatives: novel inhibitors of hepatic glucose-6-phosphate translocase. J. Med. Chem. (1997) 40:137–145.
  • HERLING AW, BURGER HJ, SCHWAB D, HEMMERLE H, BELOW P, SCHUBERT G: Pharmacodynamic profile of a novel inhibitor of the hepatic glucose-6-phophatase system. Am. J. Physol. (1998) 274:G1087–G1093.
  • PARKER JC, VANVOLKENBURG MA, LEVY CB et al.: Plasma glucose levels are reduced in rats and mice treated with an inhibitor of glucose-6-phosphatase translocase. Diabetes (1998) 47: 1630-1636.
  • WESTERGAARD N, BRAND CL, LEWINSKY RH et al.: Peroxyvanadium compounds inhibit glucose-6-phosphatase activity and glucagon-stimulated hepatic glucose output. Arch. Biochem. Biophys. (1999) 366:55–60.
  • HERS HG: Mechanisms of blood glucose homeostasis. J.Inherited Metab. Dis. (1990) 13:395–410.
  • VINCENT MF, MARANGOS PJ, GRUBER HE, VAN DEN BERGHE G: Inhibition by AICA riboside of gluconeo-genesis in isolated rat hepatocytes. Diabetes (1991) 40:1259–1266.
  • VINCENT MF, ERION MD, GRUBER HE, VAN DEN BERGHEG: Hypoglycaemic effect of AICAriboside in mice. Diabetologia (1996) 39:1148–1155.
  • VAN POELJE PD, COLBY TJ, POTTER SC, ERION MD: Fructose-1,6-bisphophatase inhibition lowers blood glucose in rodent models of diabetes. Diabetes (1999) Suppl. 1:A436.
  • SLEE D: Parallel synthesis of a spatially diverse library for high-throughput screening with fructose bis (1,6-phosphatase) (FBPase). Exploiting Molecular Diversity: Refining Small Molecule Libraries and High Throughput Organic Synthesis. San Diego, USA (2000).
  • NEWGARD CB, HWANG PK, FLETTERICK RJ: The family of glycogen phosphoylases: structure and function. Grit. Rev. Biochem. Mol. Biol. (1989) 24:69–99.
  • BOARD M, HADWEN M, JOHNSON LN: Effects of novelanalogues of D-glucose on glycogen phosphorylase activities in crude extracts of liver and skeletal muscle. Eur. Biochem. (1995) 228:753–761.
  • JAKOBSEN P, LUNDBECK J, PAWLAS J, CANDELA MPT: Azasugars as potential liver glycogen phosphorylase inhibitors. In: AFMC/AIMECS '99 International Medicinal Chemistry Symposium. Beijing, China (1999).
  • MITCHELL EP, WITHERS SG, ERMERT P et al.: Ternary complex crystal structures of glycogen phosphorylase with the transition state analog nojirimycin tetrazole and phosphate in the T and R states. Biochemistry (1996) 35:7341–7355.
  • ZAGRAPHOS SE, OIKONOMAKOS NG, TSITSANOU KE et al.: The structure of glycogen phosphorylase b with an alkyl-dihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor. Structure (1997) 5:1413–1425.
  • KASVINSKY PJ, MADSEN NB, SYGUSCH J, FLETTERICK RJ: The regulation of glycogen phosphorylase a by nucleotide derivatives. Kinetic and x-ray crystallo-graphic studies. J. Biol. Chem. (1978) 253:3343–3351.
  • MARTIN WH, HOOVER DJ, ARMENTO SJ et al.: Discovery of a human liver glycogen phosphorylase inhibitor that lowers blood glucose in vivo. Proc. Natl. Acad. Sci. USA (1998) 95:1776–1781.
  • ••First demonstration of an orally-active GP inhibitor thatlowers blood glucose in ob/ob mice.
  • HOOVER DJ, LEFTKOWITZ-SNOW S, BURGESS-HENRY JLet al.: Indole-2-carboxamide inhibitors of human liver glycogen phosphorylase. J. Med. Chem. (1998) 41:2934–2938.
  • MONDON CE, JONES IR, AZHAR S, HOLLENBECK CB, REAVEN GM: Lactate production and pyruvate dehydrogenase activity in fat and skeletal muscle from diabetic rats. Diabetes (1992) 41:1547–1554.
  • MATTEVI A, DE KOK A, PERHAM RN: The pyruvate dehydrogenase multienzyme complex. Curr. Opin. Struct. Biol. (1992) 2:877–887.
  • LINN TC, PETTIT FH, REED LJ: a-Keto acid dehydroge-nase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphory-lation. Proc. Natl. Acad. Sci. USA (1969) 62:234–241.
  • STACPOOLE PW, MOORE GW, KORNHAUSER DM: Metabolic effects of dichloroacetate in patients with diabetes mellitus and hyperlipoproteinemia. N Engl. J. Med. (1978) 298:526–530.
  • YOUNT EA, FELTEN SY, O'CONNOR BL et al.: Comparison of the metabolic and toxic effects of 2-chloroproprionate and dichloroacetate. J. Pharmacol. Exp. Ther. (1982) 222:501–508.
  • KATZ R, TAI CN, DIENER RM, MCCONNELL RF, SEMONICK DE: Dichloroacetate, sodium: 3-month oral toxicity studies in rats and dogs. Toxicol. Appl. Pharmacol. (1987) 57:273–287.
  • TOTH GP, KELTY KC, GEORGE EL, READ EJ, SMITH MK:Adverse male reproductive effects following subchronic exposure of rats to sodium dichloroace-tate. Fundam. Appl. Toxicol. (1992) 19:57–63.
  • AICHER TD, ANDERSON RC, BEBERNITZ GR et al.: (R)-3, 3,3 -Trifluoro-2 -hydroxy-2 -methyl-propionamides are orally active inhibitors of pyruvate dehydrogenase kinase. J. Med. Chem. (1999) 42:2741–2746.
  • AICHER TD, ANDERSON RC, GAO J et al.: Secondary amides of (R)-3,3,3-trifluoro-2-hydroxy-2-methyl-propionic acid as inhibitors of pyruvate dehydroge-nase kinase. J. Med. Chem. (2000) 43:236–249.
  • KAHN SE, PORTE D: Islet dysfunction in non-insulin-dependent diabetes mellitus. Am. J. Med. (1988) 85:4–8.
  • GROOP LC: Sulfonylureas in NIDDM. Diabetes Care (1992) 15:737–754.
  • BABENKO AP, AGUILAR-BRYAN L, BRYAN J: A view of SUR/Km6.x, KATI, channels. Ann. Rev. Physiol. (1998) 60:667–687.
  • THORENS B, WAEBER G: Glucagon-like peptide-1 and the control of insulin secretion in the normal state and in NIDDM. Diabetes (1993) 42:1219–1225.
  • NAUCK MA, HEIMESAAT MM, ORSKOV C, HOLST JJ, EBERT R, CREUTZFELDT W: Preserved incretin activity of glucagon-like peptide-1 (7-36 amide) but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus. J. Clin. Invest. (1993) 91:301–307.
  • YARON A, NAIDER F: Proline-dependent structural and biological properties of peptides and proteins. Grit. Rev. Biochem. Mol. Biol. (1993) 28:31–81.
  • KIEFFER TJ, MCINTOSH CHS, PEDERSON RA: Degrada-tion of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology (1995) 136:3585–3596.
  • KNUDSEN LB, PRIDAL L: Glucagon-like peptide-1 (9-36)amide is a major metabolite of glucagon-like peptide-1 (7-36)amide after in vivo administration in dogs and acts as an antagonist on the pancreatic receptor. Eur. j Pharmacol (1996) 318:429–435.
  • HOLST JJ, DEACON CF: Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for Type 2 diabetes. Diabetes (1998) 47: 1663-1670.
  • •Excellent overview of pros and cons for targeting DPP IV inhibition as a treatment for diabetes.
  • PEDERSON RA, WHITE HA, SCHLENZIG D, PAULY RP, MCINTOSH CHS, DEMUTH H-D: Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes (1998) 47:1253–1258.
  • HUGHES TE, MONE MD, RUSSELL ME, WELDON SC, VILLHAUER EB: NVP-DPP728 (1-[[[245- cyanopyridin-2-y0amino]ethyllaminolacety11-2-cyano-(8)-pyrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV. Biochemistry (1999) 38: 11597-11603.
  • 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.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.