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Miscellaneous

Recent advances in aldose reductase inhibitors: potential agents for the treatment of diabetic complications

Pages 621-631 | Published online: 25 Feb 2005

Bibliography

  • KING H, AUBERT RE, HERMAN WH: Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections. Diabetes Care (1998) 21: 1414–1431.
  • PORTE D, SCHWARTZ MW: Glucose complications: why is glucose potentially toxic? Science (1996) 272:699–700.
  • SIMA AAF, SUGIMOTO K: Experimental diabetic neuropathy: an update. Diabetologia (1999) 50:21–33.
  • ••A review describing the pathogenesis ofdiabetic neuropathy.
  • KOYA D, KING GL: Protein kinase C activation and the development of diabetic complications. Diabetes (1998) 47:859–866.
  • ISHII H, JIROUSEK MR, KOYA D et al: Amelioration of vascular dysfunctions in diabetic rats by an oral PKC inhibitor. Science (1996) 272:728–731.
  • FRIEDMAN EA: Advanced glycosylated end products and hyperglycemia in the pathogenesis of diabetic complications. Diabetes Care (1999) 22 (Suppl. 2):B65–B71
  • •A review on the main pathogenic links, especially AGEs, to diabetic complications.
  • BROWNLEE M: Negative consequences of glycation. Metabolism (2000) 49\(Supp1.1):9–13.
  • BAYNES JW, THORPE SR: Role of oxidative stress in diabetic complications. A new perspective on an old paradigm. Diabetes (1999) 48:1–9.
  • BETTERIDGE DJ: What is oxidative stress? Metabolism (2000) 49\(Supp1.1):3–8.
  • YABE-NISHIBURA C: Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol Rev (1998) 50:21–33.
  • ••A review covering the recent findings onaldose reductase and glucose toxicity.
  • TOMLINSON DR, STEVENS EJ, DIEMEL LT: Aldose reductase inhibitors and their potential for the treatment of diabetic complications. Trends Pharmacol Sci. (1994) 15:293–297.
  • CARPER D, WISTOW G, NISHIMURA C et al.: A superfamily of NADPH-dependent reductases in eukaryotes. Esp. Eye Res. (1988) 49:377–388.
  • WILLIAMSON JR, CHANG K, FRANGOS M et al: Hyperglycemic pseudohypoxia and diabetic complications. Diabetes (1993) 42:801–813.
  • TILTON RG, CHANG K, NEYENGAARD JR, VAN DEN ENDEN M, IDO Y, WILLIAMSON JR: Inhibition of sorbitol dehydrogenase. Effects on vascular and neural dysfunctions in streptozotocin-induced diabetic rats. Diabetes (1995) 44:234–242.
  • OBROSOVA JG, FATHALLAH L, LANGHJ, GREENE DA: Evaluation of a sorbitol dehydrogenase inhibitor on diabetic peripheral nerve metabolism: a prevention study. Diabetologia (1999) 42:1187–1194.
  • TSUKUSHI S, KATSUZAKI T, AOYAMA I et al.: Increased erythrocyte 3-DG and AGEs in diabetic hemodialysis patients: role of the polyol pathway. Kidney Int. (1999) 55:1970–1976.
  • HAMADA Y, ARAKI N, KOH N, NAKAMURA J, HORIUCHI S, HOTTA N: Rapid formation of advanced glycation end products by intermediate metabolites of glycolytic pathway and polyol pathway. Biochem. Biophys. Res. Commun. (1996) 228:539–543.
  • COSTANTINO L, RASTELLI G, CIGNARELLA G, VIANELLO P, BARLOCCO D: New aldose reductase inhibitors as potential agents for the prevention of long-term diabetic complications. Expert Opin. Ther. Patents (1997) 7(8):843–858.
  • MYLARI BL, LARSON ER, BEYER TAet al.: Novel, potent aldose reductase inhibitors: 3,4-dihydro-4-oxo-3-[[5-(trifluoromethyl)-2-benzothiazoylimethyll-1-phthalazineacetic acid (zopolrestat) and congeners. J. Med. Chem. (1991) 34:108–122.
  • WROBEL J, MILLEN J, SREDY J et al.:Synthesis of tolrestat analogs containing additional substituents in the ring and their evaluation as aldose inhibitors. Identification of potent, orally active 2-fluoro derivatives. j Med. Chem. (1991) 34:2504–2520.
  • KAWAMURA M, HAMANAKA N: Development of eparlestat (Kinedak), aldose reductase inhibitor. I Synth. Org. Chem. Japan (1997) 37:651–657.
  • COSTANTINO L, RASTELLI G, VIANELLO P, CIGNARELLA G, BARLOCCO D: Diabetes complications and their potential prevention: aldose reductase inhibition and other approaches. Med. Res. Rev (1999) 19:3–23.
  • PREIFER MA, SCHUMER MP, GELBER DA: Aldose reductase inhibitors: the end of an era or the need for different trial designs? Diabetes (1997) 46\(Suppl. 2):S82–89.
  • Zopolrestat. Drugs Future (2000) 25:123.
  • SATO S, KADOR PF: Inhibition of aldehyde reductase by aldose reductase inhibitors. Biochem. Pharmacol (1990) 40:1033–1042.
  • BOHREN KM, BULLOCK B, WERMUTH B, GABBAY KH: The aldo-keto reductase superfamily. CDNAs and deduced amino acid sequences of human aldehyde and aldose reductase. I Biol. Chem. (1989) 264:9547–9551.
  • FEATHER MS, FLYNN TG, MUNRO KA, KUBISESKI TJ, WALTON DJ: Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim. Biophys. Acta (1995) 1244:10–16.
  • VANDER JAGT DL, TORRES JE, HUNSAKER LA, DECK LM, ROYER RE: Physiological substrates of human aldose and aldehyde reductases. Adv. Exp. Med. Biol. (1996) 414:491–497.
  • KURONO M, FUJIWARA I, YOSHIDA K: Stereospecific interaction of a spirosuccinimide type aldose reductase inhibitor, AS-3201, with aldose reductase. Biochemistry (2001) 40:8216–8226.
  • SPIELBERG SP, SHEAR NH, CANNON M, HUTSON NJ, GUNDERSON K: In-vitro assessment of a hypersensitivity syndrome associated with sorbinil. Ann. Intern. Med. (1991) 114:720–724.
  • MAGGS JL, PARK BK: Drug-protein conjugates-XVI. studies of sorbinil metabolism: formation of 2-hydroxysorbinil and unstable protein conjugates. Biochem. Pharmacol (1988) 37:743–748.
  • NEGORO T, MURATA M, UEDA S et al.: Novel, highly potent aldose reductase inhibitors: (A) 0 2 (4 bromo-2-fluorobenzy1)-12,3,4-tetrahydropyrrolo-[1,2-alpyrazine-4-spiro-3'-pyrrolidine-1,2',3,5'-tetrone (AS-3201) and its congeners. J. Med. Chem. (1998) 41:4118–4129.
  • KRENTZ AJ, HONIGSBERGER L, ELLIS SH, HARDMAN M, NATTRASS M: A 12-month randomized controlled study of the aldose reductase inhibitor ponalrestat in patients with chronic symptomatic diabetic neuropathy. Diabetic Med. (1992) 9:463–468
  • GREENE DA, SIMA AAF: Effects of aldose reductase inhibitors on the progression of nerve damage. Diabetic Med. (1993) 10\(Suppl. 2):315–325.
  • WILSON DK, TARLE I, PETRASH JM, QUIOCHO FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. USA (1993) 90:9847–9851.
  • URZHUMTSEV A, IITE-FAVIER F, MITSCHLER A et al.: A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Structure (1997) 5:601–612.
  • BARSKI OA, GABBAY KH, GRIMSHAW CE, BOHREN KM: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry (1995) 34:11264–11275.
  • ASHIZAWA N, AOTSUKA T: Benzothiazole aldose reductase inhibitors. Drugs Future (1998) 23:521–529.
  • HARRISON DH, BOHREN KM, PETSKO GA, RINGE D, GABBAY KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry (1997) 36:16134–16140.
  • NAKAMURA J, HAMADA Y, CHAYA S eta].: Effect of a combination treatment with a low dose of an aldose reductase inhibitor and a protein kinase C-I3 specific inhibitor on diabetic neuropathy in rats. Diabetes (1999) 48 (Suppl. 1):A53.
  • KATO N, MIZUNO K, MAKINO M, SUZUKI T, YAGIHASHI S: Effects of 15-month aldose reductase inhibition with fidarestat on the experimental diabetic neuropathy in rats. Diabetes Res. Clin Practice (2000) 50:77–85.
  • HOTTA N, TOYOTA T, MATSUOKA K eta].: Clinical efficacy of fidarestat, a novel aldose reductase inhibitor, for diabetic peripheral neuropathy. Diabetes Care (2001) 24:1776–1782.
  • OKA M, MATSUMOTO Y, SUGIYAMA S, TSURUTA N, MATSUSHIMA M: A potent aldose reductase inhibitor, (2S,4.9-6-fluoro-2',5'-dioxospirolchroman-4,4'-imidazolidinel-2-carboxamide (fidarestat): its absolute configuration and interactions with the aldose reductase by X-ray crystallography. I Med. Chem. (2000) 43:2479–2483.
  • FRESNEAU P, CUSSAC M, MORAND JM, SZYMONSKI B, TRANQUI D, LECLERC G: Synthesis, activity, and molecular modeling of new 2,4-dioxo-5-(naphthylmethylene)-3-thiazodineacetic 629 acids and 2-thioxo analogues as potent aldose reductase inhibitors. j Med. Chem. (1998) 41:4706–4715.
  • KOMPELLA UB, SUNKARA G, THOMAS E, CLARK R, DERUITER J: Rabbit corneal and conjunctival permeability of the novel aldose reductase inhibitors: N-W1-(benzoylamino)phenyll-sulphonylIglycines and Nbenzoyl-N phenylglycines. I Pharm. Pharmacol (1999) 51:921–927.
  • SUNKARA G, DERUITER J, CLARK R,KOMPELLA UB: In vitro hydrolysis, permeability, and ocular uptake of prodrugs of 1V P1-(benzoylamino)phenylsulphonyll-glycine, a novel aldose reductase inhibitor. Pharm. Pharmacol. (2000) 52:1113–1122.
  • DONKOR 10, ABDEL-GHANY YS, KADOR PF eta].: Synthesis and biological activity of aldose reductase inhibitors with Michael acceptor substituents. Eur. j Med. Chem. (1999) 34:235–243.
  • COTTER MA, MIRRLEES DJ, CAMERON NE: Neurovascular interactions between aldose reductase and angiotensin-converting enzyme inhibition in diabetic rats. Eur. j Pharmacol. (2001) 417:223–230.
  • SAAB NH, DONKER 10, RODRIGUEZ L, KADOR PF, MILLER DD: Phenylsulfonylnitromethanes as potent irreversible inhibitors of aldose reductase. Eur. J. Med. Chem. (1999) 34:745–751.
  • COSTANTINO L, RASTELLI G, GAMBERINI MC et al: 1-Benzopyran-4-one antioxidants as aldose reductase inhibitors. j Med. Chem. (1999) 42:1881–1893.
  • WILSON DK, BOHREN K, GABBAY KH, QUIOCHO FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science (1992) 257:81–84.
  • HARRISON DH, BOHREN KM, RINGE D, PETSKO GA, GABBAY KH: An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry (1994) 33: 2011-2020.
  • DE WINTER HL, VON ITZSTEIN M: Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme. Biochemistry (1995) 34:8299–8308.
  • LEE YS, HODOSCEK M, BROOKS BR, KADORPF: Catalytic mechanism of aldose reductase studied by the combined potentials of quantum mechanics and molecular mechanics. Biophys. Chem. (1998) 70:203–216.
  • BOHREN KM, GRIMSHAW CE, LAI CJ etal.: Tyrosine-48 is the proton donor and histidine-110 directs substrate stereo-chemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33:2021–2032.
  • VARNAI P, WARSHEL A: Computer simulation studies of the catalytic mechanism of human aldose reductase. Am. Chem. Soc. (2000) 122:3849–3860.
  • COSTANTINO L, RASTELLI G, VESCOVINI K et al: Synthesis, activity, and molecular modeling of a new series of tricyclic pyridazinones as selective aldose reductase inhibitors. j Med. Chem. (1996) 39:4396–4405.
  • RASTELLI G, VIANELLO P, BARLOCCO D, COSTANTINO L, CORSO AD, MURA U: Structure-based design of an inhibitor modeled at the substrate active of aldose reductase. Bioorg. Med. Chem. Lett. (1997) 7:1897–1902.
  • RASTELLI G, COSTANTINO L: Molecular dynamics simulations of the structure of aldose reductase complexed with the inhibitor tolrestat. Bioorg. Med. Chem. Lett. (1998) 8:641–646.
  • LEE YS, CHEN Z, KADOR PF: Molecular modeling studies of the binding modes of aldose reductase inhibitors at the active site of human aldose reductase. Bioorg. Med. Chem. (1998) 6:1811–1819.
  • RASTELLI G, COSTANTINO L, VIANELLO P, BARLOCCO D: Free energy perturbation studies of the inhibitor 5, 6- dihydrobenzo [hi cinnolin- 3 (2H)one-2-acetic acid and its methoxylated analogs to aldose reductase. Tetrahedron (1998) 54:9415–9428.
  • SINGH SB, MALAMAS MS, HOHMAN TC, NILAKANTAN R, CARPER DA, KITCHEN D: Molecular modeling of the aldose reductase-inhibitor complex based on the X-ray crystal structure and studies with single-site-directed mutants. j Med. Chem. (2000) 43:1062–1070.
  • WILSON DK, QUIOCHO FA, PETEASH JM: Structural studies of aldose reductase inhibition. In: Structure-Based Drug Design. Veerapandian P (Ed.), Marcel Dekker, Inc., New York (1997):229–246. A book covering a variety of examples of SBDD.
  • KUNTZ ID: Structure-based strategies fordrug design and discovery. Science (1992) 257:1078–1082.
  • IWATA Y, ARISAWA M, HAMADA R et al.: Discovery of novel aldose reductase inhibitors using a protein structure-based approach: 3D-database search followed by design and synthesis. j Med. Chem. (2001) 44:1718–1728.
  • MIZUTANI MY, TOMIOKA N, ITAI A: Rational automatic search method for stable docking models of protein and ligand. Ma Biol. (1994) 243:310–326.
  • IWATA Y, SATORU NAITO, ITAI A, MIYAMOTO S: Protein structure-based de novo design and synthesis of aldose reductase inhibitors. Drug Dec. Discovery (2001) 17:349–359.
  • NISHIBATA Y, ITAI A: Confirmation of usefulness of a structure construction program based on three-dimensional receptor structure for rational lead generation. I Med. Chem. (1993) 36:2921–2928.

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