Protein tyrosine phosphatase 1B inhibitors for diabetes (original) (raw)
Zimmet, P., Alberti, K. G. M. M. & Shaw, J. Global and societal implications of the diabetes epidemic. Nature414, 782–787 (2001).An excellent overview of the epidemiology of diabetes. CASPubMed Google Scholar
Sinha, R. et al. Prevalence of impaired glucose tolerance among children and adolescents with marked obesity. N. Engl. J. Med.346, 802–810 (2002). CASPubMed Google Scholar
Rocchini, A. P. Childhood obesity and a diabetes epidemic. N. Engl. J. Med.346, 854–855 (2002). PubMed Google Scholar
Dunstan, D. W. et al. The rising prevalence of diabetes and impaired glucose tolerance. The Australian diabetes, obesity and lifestyle study. Diabetes Care25, 829–834 (2002). PubMed Google Scholar
Groop, L. & Orho-Melander, M. The dysmetabolic syndrome. J. Int. Med.250, 105–120 (2001). CAS Google Scholar
Poitout, V. & Robertson, P. R. Minireview: secondary β-cell failure in type 2 diabetes – a convergence of glucotoxity and lipotoxicity. Endocrinology143, 339–342 (2002). CASPubMed Google Scholar
Weyer, C., Tartanni, P. A., Bogardus, C. & Pratley, R. E. Insulin resistance and insulin secretory dysfunction are independent predictors of worsening of glucose tolerance during each stage of type 2 diabetes development. Diabetes Care24, 89–94 (2001). CASPubMed Google Scholar
Stumvoll, M., Fritsche, A. & Haring, H. U. Clinical characterization of insulin secretion as the basis for genetic analyses. Diabetes51 (Suppl. 1), S122–S129 (2002). CASPubMed Google Scholar
Uusitupa, M. et al. The Finnish Diabetes Prevention Study. Br. J. Nutr.83 (Suppl. 1), S137–S142 (2000). CASPubMed Google Scholar
The Diabetes Prevention Study Group. Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin. N. Engl. J. Med.346, 393–403 (2002).
Heine, R. J. & Dekker, J. M. Beyond postprandial hyperglycaemia: metabolic factors associated with cardiovascular disease. Diabetologia45, 461–475 (2002). CASPubMed Google Scholar
Marx, J. Unraveling the causes of diabetes. Science296, 686–689 (2002). CASPubMed Google Scholar
Saltiel, A. R. & Kahn, C. R. Insulin signaling and the regulation of glucose and lipid metabolism. Nature414, 799–806 (2001).An excellent overview of metabolic insulin signal transduction. CASPubMed Google Scholar
Obici, S., Feng, Z., Karkanias, G., Baskin, D. G. & Rossetti, L. Decreasing hypothalamic insulin receptors causes hyperphagia and insulin resistance in rats. Nature Neurosci.5, 566–572 (2002).This article shows the role of the insulin receptor at the level of the CNS. CASPubMed Google Scholar
Saltiel, A. R. & Pessin, J. E. Insulin signaling pathways in time and space. Trends Cell Biol.12, 65–71 (2002). CASPubMed Google Scholar
Bryant, N. J., Govers, R. & James, D. E. Regulated transport of the glucose transporter GLUT4. Nature Rev. Mol. Cell Biol.3, 267–277 (2002). CAS Google Scholar
Smith, U. Impaired ('diabetic') insulin signaling and action occur in fat cells long before glucose intolerance – is insulin resistance initiated in the adipose tissue? Int. J. Obes. Relat. Metab. Disord.26, 897–904 (2002). CASPubMed Google Scholar
Ostman, A. & Bohmer, F. D. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol.11, 258–266 (2001). CASPubMed Google Scholar
Cheng, A., Dube, N., Gu, F. & Tremblay, M. L. Coordinated action of protein tyrosine phosphatases in insulin signal transduction. Eur. J. Biochem.269, 1050–1059 (2002). CASPubMed Google Scholar
Goldstein, B. J., Bittner-Kowalczyk, A., White, M. F. & Harbeck, M. Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the GRB2 adaptor protein. J. Biol. Chem.275, 4283–4289 (2000). CASPubMed Google Scholar
Wu, X. et al. Depot-specific variation in protein-tyrosine phosphatase activities in human omental and subcutaneous adipose tissue: a potential contribution to differential insulin sensitivity. J. Clin. Endocrinol. Metab.86, 5973–5980 (2001). CASPubMed Google Scholar
Cheung, A. et al. Marked impairment of protein tyrosine phosphatase 1B activity in adipose tissue of obese subjects with and without type 2 diabetes mellitus. J. Lab. Clin. Med.134, 115–123 (1999). CASPubMed Google Scholar
Forsell, P. K. A. L., Boie, Y., Montalibet, J., Collins, S. & Kennedy, B. P. Genomic characterization of the human and mouse protein tyrosine phosphatase-1B genes. Gene260, 145–153 (2000). CASPubMed Google Scholar
Mok, A. et al. A single nucleotide polymorphism in protein tyrosine phosphatase PTP1B is associated with protection from diabetes or impaired glucose tolerance in Oji–Cree. J. Clin. Endocrinol. Metab.87, 724–727 (2002). CASPubMed Google Scholar
Di Paola, R. et al. A variation in 3′UTR of hPTP1B increases specific gene expression and associates with insulin resistance. Am. J. Hum. Genet.70, 806–812 (2002). CASPubMedPubMed Central Google Scholar
Echwald, S. M. et al. A P387L variant in protein tyrosine phosphatase-1B (PTP1B) is associated with type 2 diabetes and impaired serine phosphorylation of PTP1B in vitro. Diabetes51, 1–6 (2002). CASPubMed Google Scholar
Goldstein, B. J. Protein tyrosine phosphatase 1B (PTP1B): a novel therapeutic target for type 2 diabetes mellitus, obesity and related states of insulin resistance. Curr. Drug Targets Immune Endocr. Metab. Disord.1, 265–275 (2001). CAS Google Scholar
Ukkola, O. & Santaniemi, M. Protein tyrosine phosphatase 1B: a new target for the treatment of obesity and associated co-morbidities. J. Int. Med.251, 467–475 (2002).References27and28review the importance of PTP1B in insulin signalling. CAS Google Scholar
Egawa, K. et al. Protein-tyrosine phosphatase-1B negatively regulates insulin signaling in l6 myocytes and Fao hepatoma cells. J. Biol. Chem.276, 10207–10211 (2001). CASPubMed Google Scholar
Chen, H. et al. Protein-tyrosine phosphatases PTP1B and SYP are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. J. Biol. Chem.272, 8026–8031 (1997). CASPubMed Google Scholar
Venable, C. L. et al. Overexpression of protein-tyrosine phosphatase-1B in adipocytes inhibits insulin-stimulated phosphoinositide 3-kinase activity without altering glucose transport or Akt/Protein kinase B activation. J. Biol. Chem.275, 18318–18326 (2000). CASPubMed Google Scholar
Mahadev, K. et al. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J. Biol. Chem.276, 48662–48669 (2001). CASPubMed Google Scholar
Tao, J., Malbon, C. C. & Wang, H. Insulin stimulates tyrosine phosphorylation and inactivation of protein tyrosine phosphatase 1B in vivo. J. Biol. Chem.276, 29520–29525 (2001). CASPubMed Google Scholar
Salmeen, A., Andersen, J. N., Myers, M. P., Tonks, N. K. & Barford, D. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol. Cell7, 615–621 (2001). Google Scholar
Barford, D. The mechanism of protein kinase regulation by protein phosphatases. Biochem. Soc. Trans.29, 385–391 (2001) CASPubMed Google Scholar
Xie, L., Zhang, Y. L. & Zhang, Z. Y. Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant. Biochemistry41, 4032–4039 (2002). CASPubMed Google Scholar
Myers, M. P. et al. TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B. J. Biol. Chem.276, 47771–47774 (2001). CASPubMed Google Scholar
Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G. & Bastiaens, P. I. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science295, 1708–1711 (2002). CASPubMed Google Scholar
Gill, G. N. A pit stop at the ER. Science295, 1654–1655 (2002).Reference39is a commentary about reference38that brings into perspective how PTP1B might have roles in regulating various RTKs. CASPubMed Google Scholar
Dadke, S. & Chernoff, J. Interaction of protein tyrosine phosphatase (PTP) 1B with its substrates is influenced by two distinct binding domains. Biochem. J.364, 377–383 (2002). CASPubMedPubMed Central Google Scholar
Elchebly, M. et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science283, 1544–1548 (1999). CASPubMed Google Scholar
Klaman, L. D. et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol.20, 5479–5489 (2000). CASPubMedPubMed Central Google Scholar
Kaszubska, W. et al. The role of PTP1B in leptin signalling. Keystone Symposia: Diabetes Mellitus: Molecular Mechanisms, Genetics and New Therapies Jan 10–16226, 81 (2002).PTP1B has been implicated in negatively regulating insulin signal transduction, and this role is extended to include negative regulation of leptin signal transduction. Google Scholar
Zabolotny, J. M. et al. PTP1B regulates leptin signal transduction in vivo. Dev. Cell2, 489–495 (2002). CASPubMed Google Scholar
Cook, W. S. & Unger, R. H. Protein tyrosine phosphatase 1B: a potential leptin resistance factor of obesity. Dev. Cell2, 385–387 (2002). CASPubMed Google Scholar
Cheng, A. et al. Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B. Dev. Cell2, 497–503 (2002). CASPubMed Google Scholar
Zinker, B. A. et al. Reduction of protein tyrosine phosphatase 1B normalizes glucose and improves insulin sensitivity in diabetic mice. Proc. Natl Acad. Sci. USA99, 11357–11362 (2002). CASPubMedPubMed Central Google Scholar
Tonks, N. K., Diltz, C. D. & Fischer, E. H. Purification of the major protein-tyrosine phosphatases of human placenta. J. Biol. Chem.263, 6722–6730 (1988). CASPubMed Google Scholar
Barford, D., Flint, A. J. & Tonks, N. K. Crystal structure of human protein tyrosine phosphatase 1B. Science263, 1397–1404 (1994). CASPubMed Google Scholar
Jia, Z., Barford, D., Flint, A. J. & Tonks, N. K. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science268, 1754–1758 (1998). Google Scholar
Groves, M. R., Yao, Z. J., Roller, P. P., Burke, T. R. Jr & Barford, D. Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics. Biochemistry37, 17773–17783 (1998). CASPubMed Google Scholar
Pannifer, A. D. B., Flint, A. J., Tonks, N. K. & Barford, D. Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography. J. Biol. Chem.273, 10454–10462 (1998). CASPubMed Google Scholar
Puius, Y. A. et al. Identification of a second aryl phosphate binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design. Proc. Natl Acad. Sci. USA94, 13420–13425 (1997). CASPubMedPubMed Central Google Scholar
Hadjuk, P. J., Meadows, R. P. & Fesik, S. W. Discovering high affinity ligands for proteins. Science278, 497–499 (1997). Google Scholar
Iversen, L. F. et al. Structure based design of a low molecular weight, non-phosphorous, non-peptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B. J. Biol. Chem.275, 10300–10307 (2000).This paper describes the structure-based design of PTP1B inhibitors. CASPubMed Google Scholar
Asante-Appiah, E. et al. The YRD motif is a major determinant of substrate and inhibitor specificity in T-cell protein-tyrosine phosphatase. J. Biol. Chem.276, 26036–26043 (2001). CASPubMed Google Scholar
Peters, G. H. et al. Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and α. J. Biol. Chem.275, 18201–18209 (2000). CASPubMed Google Scholar
Iversen, L. F. et al. Steric hindrance as a basis for structure-based design of selective inhibitors of protein tyrosine phosphatases. Biochemistry40, 14812–14820 (2001). CASPubMed Google Scholar
Iversen, L. F. et al. Structure determination of T cell protein-tyrosine phosphatase. J. Biol. Chem.277, 19982–19990 (2002). CASPubMed Google Scholar
Ibarra-Sanchez, M. D. et al. Murine embryonic fibroblasts lacking TC-PTP display delayed G1 phase through defective NF-κB activation. Oncogene20, 4728–4739 (2001). CASPubMed Google Scholar
You-Ten, K. E. et al. Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice. J. Exp. Med.18, 683–693 (1997).A review of PTP inhibitors from a medicinal chemistry perspective that provides a detailed analysis of the inhibitors identified so far. Google Scholar
Blaskovitch, M. A. & Kim, H.-O. Recent advances in discovery and development of protein tyrosine phosphatase inhibitors. Expert Opin. Ther. Patents12, 871–905 (2002). Google Scholar
Burke, T. R., Kole, H. K. & Roller, P. P. Potent inhibition of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F2Pmp. Biochem. Biophys. Res. Commun.204, 129–134 (1994). CASPubMed Google Scholar
Burke, T. R. Jr et al. Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design. Biochemistry35, 15989–15996 (1996). CASPubMed Google Scholar
Taing, M. et al. Potent and highly selective inhibitors of the protein tyrosine phosphatase 1B. Biochemistry38, 3793–3803 (1999). CASPubMed Google Scholar
Jia, Z. et al. Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine mimetics. J. Med. Chem.44, 4584–4594 (2001). CASPubMed Google Scholar
Bayly, C. & Ohkubo, M. Sulfur substituted aryldifluoromethylphosphonic acids as PTP1B inhibitors. Patent WO 01/70754 (2001).
Leblanc, Y., Dufresne, C., Gauthier, J. Y. & Young, R. Aromatic phosphonates as protein tyrosine phosphatase 1B (PTP1B) inhibitors. Patent WO 01/46204 (2001).
Shen, K. et al. Acquisition of a specific and potent PTP1B inhibitor from a novel combinatorial library and screening procedure. J. Biol. Chem.276, 47311–47319 (2001). CASPubMed Google Scholar
Leblanc, Y., Dufresne, C., Roy, P. & Wang, Z. Phosphonic and carboxylic acid derivatives as inhibitors of protein tyrosine phosphatase-1B. Patent WO 00/69889 (2000).
Burke T. R. Jr et al. Enantioselective synthesis of nonphosphorous-containing phosphotyrosyl mimetics and their use in the preparation of tyrosine phophatase inhibitory peptides. Tetrahedron54, 9981–9994 (1998). CAS Google Scholar
Bleasdale, J. E. et al. Small molecule peptidomimetics containing a novel phosphotyrosine bioisostere inhibit protein tyrosine phosphatase 1B and augment insulin action. Biochemistry40, 5642–5654 (2001). CASPubMed Google Scholar
Larsen, S. D. et al. Synthesis and biological activity of a novel class of small molecular weight peptidomimetic competitive inhibitors of protein tyrosine phosphatase 1B. J. Med. Chem.45, 598–622 (2002). CASPubMed Google Scholar
Liljebris, C., Larsen, S. D., Ogg, D., Palazuk, B. J. & Bleasedale, J. E. Investigation of potential bioisosteric replacements for the carboxyl groups of peptidomimetic inhibitors of protein tyrosine phosphatase 1B: identification of a tetrazole-containing inhibitor with cellular activity. J. Med. Chem.45, 1785–1798 (2002).This article describes the production of inhibitors with improved physico-chemical properties. CASPubMed Google Scholar
Andersen, et al. 2-(Oxalylamino)benzoic acid is a general, competitive inhibitor of protein tyrosine phosphatases. J. Biol. Chem.275, 7101–7108 (2000). CASPubMed Google Scholar
Iversen, L. F. et al. Structure based design of a low molecular weight, non-phosphorous, non-peptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B. J. Biol. Chem.275, 10300–10307 (2000). CASPubMed Google Scholar
Andersen, H. S. Method of inhibiting protein tyrosine phosphatase 1B and/or T-cell protein tyrosine phosphatase and/or other PTPases with Asp residue at position 48. Patent WO 01/17516 (2001).
Lui, G. et al. Discovery of competitive, potent, and selective protein tyrosine phosphatase 1B inhibitors. 223rd American Chemical Society National Meeting, Orlando, Florida, April 7–11, 2002 MEDI–002 (2002). Google Scholar
Wrobel, J. et al. PTP1B inhibition and antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[_b_]naphtha[2,3-_d_]furans and 11-arylbenzo[_b_]naphto[2,3-_d_]thiophenes. J. Med. Chem.42, 3199–3202 (1999). CASPubMed Google Scholar
Reuters Business Report. (10 Jun 2002).
McGovern, S. L., Caselli, E., Grigorieff, N. & Shoichet, B. K. A common mechanism underlying promiscuous inhibitors from virtual and high throughput screening. J. Med. Chem.45, 1712–1722 (2002). CASPubMed Google Scholar
Doman, T. N. et al. Molecular docking and high throughput screening for novel inhibitors of protein tyrosine phosphatase-1B. J. Med. Chem.45, 2213–2221 (2002).The establishment of robust assay systems to determine activity and mechanism. CASPubMed Google Scholar
Lubben, T., Clampit, J., Stashko, M., Trevillyan, J. & Jirousek, M. R. in Current Protocols in Pharmacology Vol. 8 Ch. 3 (Emma, S. I. et al.) 1–18 (John Wiley, New York, 2001). Google Scholar
Cornish-Bowden, A. Fundamentals of Enzyme Kinetics (Portland Press, London, 1995). Google Scholar
Copeland, R. A. Enzymes: a Practical Introduction to Structure, Mechanism, and Data Analysis 2nd edn (Wiley–VCH, New York, 2000). Google Scholar
Bieth, J. G. Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol.248, 59–84 (1995). CASPubMed Google Scholar
Zhang, Y. L., Keng, Y. F., Zhao, Y., Wu, L. & Zhang, Z. Y. Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases. J. Biol. Chem.273, 12281–12287 (1998). CASPubMed Google Scholar
Lu, B. et al. Enhanced sensitivity of insulin-resistant adipocytes to vanadate is associated oxidative stress and decreased reduction of vanadate (+5) to vanadyl (+4). J. Biol. Chem.276, 35589–35598 (2001). CASPubMed Google Scholar
Huyer, G. et al. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem.272, 843–851 (1997). CASPubMed Google Scholar
Crans, D., Bunch, R. L. & Theisen, L. A. Interaction of trace levels of vanadium (IV) and vanadium (V) in biological systems. J. Am. Chem. Soc.111, 7597–7607 (1989). CAS Google Scholar
Lipinski, C. A., Lombardo, F., Dominy, B. W. & Feeney, P. J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev.23, 3–25 (1997). CAS Google Scholar
Palm, K., Stenberg, P., Luthman, K. & Artursson, P. Polar molecular surface properties predict the intestinal absorption of drugs in humans. Pharm. Res.14, 568–571 (1997). CASPubMed Google Scholar
Veber, D. F. et al. Molecular properties that influence the oral bioavailability of drug candidates. J. Med. Chem.45, 2615–2623 (2002). CASPubMed Google Scholar
Pei, Z. et al. (2_R_)-2-(2′,6′-dichloro-4′-dibenzo(b,d)furan-4″-ylphenoxy)-3-phenylpropanoic acid (A-321842) as a protein tyrosine phosphatase 1B (PTP1B) inhibitor with anti-diabetic effects in ob/ob mice. Diabetes50 (Suppl. 1), 1524-P (2001). Google Scholar
Burkey, B. F. et al. Pharmacogenomic evaluation of a putative orally active PTP1B inhibitor using ob/ob mice reveals an alternative mechanism of action. Diabetes51 (Suppl. 2), 138-OR (2002). Google Scholar