From immune response to cancer: A spot on the low molecular weight protein tyrosine phosphatase

Cellular and Molecular Life Sciences

Volumn 66, Issue 7, 2009, Pages 1140-1153

  Souza, A C S ^a   Azoubel, S ^a   Queiroz, K C S ^b   Peppelenbosch, M P ^b   Ferreira, C V ^a  

^a UNIVERSITY OF CAMPINAS   (Brazil)

^b UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

Author keywords

Cancer; Immune system; Inflammation; Low molecular weight protein tyrosine phosphatase

Indexed keywords

4 (5 ARYLIDENE 2,4 DIOXOTHIAZOLIDIN 3 YL)METHYLBENZOIC ACID; BENZOIC ACID DERIVATIVE; BETA CATENIN; EPHRIN A2; EPHRIN RECEPTOR A2; FERRUGINOL; FLAVONOID; FOCAL ADHESION KINASE; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; INSULIN RECEPTOR; JANUS KINASE 2; LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE; MITOGEN ACTIVATED PROTEIN KINASE; MORIN; NATURAL PRODUCT; PROTEIN P190; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SOMATOMEDIN C; STAT5 PROTEIN; UNCLASSIFIED DRUG;

BREAST CANCER; CANCER CELL; CANCER INVASION; CARCINOGENESIS; CELL FUNCTION; CELL GROWTH; CELL MIGRATION; CELL PROLIFERATION; CELLULAR IMMUNITY; COLON CANCER; COMPETITIVE INHIBITION; DISEASE PREDISPOSITION; DRUG ACTIVITY; DRUG POTENTIATION; DRUG TARGETING; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; GENETIC ANALYSIS; GENETIC POLYMORPHISM; HUMAN; IMMUNE RESPONSE; IMMUNOCOMPETENT CELL; NEOPLASM; NEUROBLASTOMA; NONHUMAN; PROSTATE CANCER; PROTEIN PHOSPHORYLATION; RESPIRATORY BURST; REVIEW; T LYMPHOCYTE ACTIVATION; TUMOR IMMUNITY; UPREGULATION;

CELL MOVEMENT; GENETIC PREDISPOSITION TO DISEASE; HUMANS; IMMUNE SYSTEM; IMMUNE SYSTEM DISEASES; LYMPHOCYTE ACTIVATION; NEOPLASMS; PHOSPHORYLATION; PHOSPHOTYROSINE; POLYMORPHISM, GENETIC; PROTEIN TYROSINE PHOSPHATASES; PROTO-ONCOGENE PROTEINS; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION;

EUKARYOTA;

EID: 63449129930     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8501-8     Document Type: Review

References (85)

1. Hunter, T., (1987) A thousand and one protein kinases. Cell 50, 823-829.
2. Krebs, E. G. and Beavo, J. A. (1979) Phosphorylationdephosphorylation of enzymes. Annu. Rev. Biochem. 48, 923-959.
3. Ferreira, C. V., Justo, G. Z., Souza, A. C. S., Queiroz, K. C., Zambuzzi, W. F., Aoyama, H. and Peppelenbosch M. P. (2006) Natural compounds as a source of protein tyrosine phosphatase inhibitors: application to the rational design of small-molecule derivatives. Biochimie 88, 1859-1873.
4. Andersen, J. N., Jansen, P. G., Echwald, S. M., Mortensen, O. H., Fukada, T., Del Vecchio, R., Tonks, N. K. and Moller, N. P. (2004) A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage. FASEB J. 18, 8-30.
5. Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J. and Mustelin, T. (2004) Protein tyrosine phosphatases in the human genome. Cell 117, 699-711.
6. Raugei, G., Ramponi, G. and Chiarugi, P. (2002) Low molecular weight protein tyrosine phosphatases: small but smart. Cell. Mol. Life Sci. 59, 941 - 949.
7. Modesti, A., Marzocchini, R., Raugei, G., Chiti, F., Sereni, A., Magherini, F. and Ramponi, G. (1998) Cloning, expression and characterization of a new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing. FEBS Lett. 431, 111-115.
8. Dissing, J., Johnsen, A. H. and Sensabaugh, G. F. (1991) Human red cell acid phosphatase (ACP1). J. Biol. Chem. 266, 20619-20625.
9. Wo, Y. Y., McCormack, A. L., Shabanowitz, J., Hunt, D. F., Davis, J. P., Mitchell, G. L. and Van Etten, R. L. (1992) Sequencing, cloning, and expression of human, red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. J. Biol. Chem. 267, 10856-10865.
10. Bryson, G. L., Massa, H., Trask, B. J. and Van Etten, R. L. (1995) Gene structure, sequence and chromosomal localization of the human red cell-type-low-molecular-acid phosphotyrosil phosphatase gene, ACP1. Genomics 30, 133-140.
11. Cirri, P., Fiaschi, T., Chiarugi, P., Camici, G., Manao, G. and Raugei, G. and Ramponi, G. (1996) The molecular basis of differing kinetic behavior of the two low molecular mass phosphotyrosine protein phosphatase isoforms. J. Biol. Chem. 271, 2604-2067.
12. Tailor, P., Gilman, J., Williams, S. and Mustelin, T. (1999) A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing. Eur. J. Biochem. 262, 277-282.
13. den Hertog, J., Ostman, A. and Böhmer, F. D. (2008) Protein tyrosine phosphatases: regulatory mechanisms. FEBS J. 275, 831-847.
14. Bucciantini, M., Chiarugi, P., Cirri, P., Taddei, L., Stefani, M., Raugei, G., Nordlund, P. and Ramponi, G. (1999) The low Mr phosphotyrosine protein phosphatase behaves differently when, phosphorylated at Tyr.131. or Tyr132 by Src kinase. FEBS Lett. 456, 73-78.
15. Tailor, P., Gilman, J., Williams, S., Couture, C. and Mustelin, T. (1997) Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132. J. Biol. Chem. 272, 5371-5374.
16. Chiarugi, P. and Buricchi, F. (2007) Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslation modifications. Antioxid. Redox Signal. 9, 1-24.
17. Monteiro, H. P., Arai, R. J and Travassos, L. R. (2008) Protein tyrosine phosphorylation and protein tyrosine nitration in redox signaling. Antioxid. Redox Signal. 10, 843-889.
18. Chiarugi, P. (2005) PTPs versus PTKs: the redox side of the coin. Free Radic. Res. 39, 353-364.
19. Chiarugi, P. and Giannoni, E. (2005) Anchorage-dependent cell growth: tyrosine kinases and phosphatases meet redox regulation. Antioxid. Redox. Signal. 7, 578-592.
20. 2, a necessary evil for cell signaling. Science 312, 1882-1883.
21. Sangrar, W., Gao, Y., Scott, M., Truesdell, P., and Greer, P. A. (2007) Fer-mediated cortactin phosphorylation is associated with efficient fibroblast migration and is dependent on reactive oxygen species generation during integrin-mediated cell adhesion. Mol. Cell Biol. 27, 6140-6152.
22. Chiarugi P. (2008) Src Redox Regulation: There Is More Than Meets the Eye. Mol Cells. 26(4) [Epub ahead of print].
23. Catarzi, S., Biagioni, C., Giannoni, E., Favilli, F., Marcucci, T., Iantomasi, T. and Vicenzini, M. A. (2005) Redox regulation of platellet-derived-growth-factor-receptor: Role of NADPH-oxidase and c-Src tyrosine kinase. Biochim. Biophys. Acta 1745, 166-175.
24. Chiarugi, P., Fiaschi, T., Taddei, M. L., Talini, D., Giannoni, E., Raugei, G. and Ramponi, G. (2001) Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation, J. Biol. Chem. 276, 33478-33487.
25. Parri, M., Buricchi, F., Taddei, M. L., Giannoni, E., Raugei, G., Ramponi, G. and Chiarugi, P. (2005) EphrinA1 repulsive response is regulated by an EphA2 tyrosine phosphatase. J. Biol. Chem. 280, 34008-34018.
26. Cirri, P., Chiarugi, P., Taddei, L., Raugei, G., Camici, G., Manao, G. and Ramponi, G. (1998) Low molecular weight protein-tyrosine phosphatase tyrosine phosphorylation by c-Src during platelet-derived growth factor-induced mitogenesis correlates with its subcellular targeting. J. Biol. Chem. 273, 32522-32527.
27. Caselli, A., Taddei, M. L., Bini, C., Camici, G., Manao, G., Cirri, P. and Ramponi, G. (2007) Low molecular weight protein tyrosine phosphatase and caveolin-1: interaction and isoenzyme-dependent regulation. Biochemistry 46, 6383-6392.
28. Caselli, A., Taddei, M. L., Manao, G., Camici, G. and Ramponi, G (2001) Tyrosine-phosphorylated caveolin is a physiological substrate of the low M(r) protein-tyrosine phosphatase. J. Biol. Chem. 276, 18849-18854.
29. Bottini, E., Bergamaschi, A., Magrini, A., Spina, C., Ammendola, L., Grassi, S., Bottini, N. and Gloria-Bottini, F. (2007) Allergy and ACP1 genetic polymorphism. Allergy Asthma Proc. 28, 87-92.
30. Bottini, N., Bottini, E., Gloria-Bottini, F. and Mustelin, T. (2002) Low-molecular-weight protein tyrosine phosphatase and human disease: in search of biochemical mechanisms. Arch. Immunol. Ther. Exp. (Warsz) 50, 94-104.
31. Bottini, N., Gloria-Bottini, F., Lucarini, N., Ronchetti, P. G. and Fontana, L. (2000) Inflammatory bowel disease: Are there gender differences in the genetics of signal transduction? A preliminary study of cytosolic low molecular weight protein tyrosine phosphatase. Dis. Markers 16, 163-166.
32. Malentacchi, F., Marzocchini, R., Gelmini, S., Orlando, C., Serio, M., Ramponi G. and Raugei, G. (2005) Up-regulated expression of low molecular weight protein tyrosine phosphatases in different human cancers. Biochem. Biophys. Res. Commun. 334, 875-883.
33. Griffths, H. R. (2005) ROS as signaling molecules in T cells evidence for abnormal redox signaling in the autoimmune disease, rheumatoid arthritis. Redox Rep. 10, 273-280.
34. Bottini, N., Ammendola, M. and Gloria-Bottini, F. (2002) ACP1 is associated with allergy. Allergy 57, 651-652.
35. Rigacci, S., Rovida, E., Dello Sbarba, P. and Berti, A. (2002) Low Mr phosphoprotein tyrosine phosphatase associates and dephosphorylates p125 focal adhesion kinase, interfering with cell motility and spreading. J. Biol. Chem. 277, 41631-41636.
36. Giannoni, E., Chiarugi, P., Cozzi, G., Magnellis, L., Taddei, M. L., Fiaschi, T., Buricchi, F., Raugei, G. and Ramponi, G. (2003) Lymphocyte function-associated antigen-1-mediated T. cell adhesion is impaired by low molecular weight phosphotyrosine phosphatase-dependent inhibition of FAK activity. J. Biol. Chem. 38, 36763-36776.
37. Zeyda, M., Poglitsch, M., Geyeregger, R., Smolen, J. S., Zlabinger, G. J., Hörl, W. H., Waldhäusl, W., Stulnig, T. M. and Säemann, M. D. (2005) Disruption of the interaction of T cells with antigen-presenting cells by the active leflunomide metabolite teriflunomide. Arthritis Rheum. 52, 2730-27399.
38. Zeyda, M., Geyeregger, R., Poglitsch, M., Weichhart, T., Zlabinger, G. J., Koyasu, S., Hörl, W. H., Stulnig, T. M., Watschinger, B. and Säemann, M. D. (2007) Impairment of T cell interactions with antigen-presenting cells by immunosuppressive drugs reveals involvement of calcineurin and NF-kappaB in immunological synapse formation. J. Leukoc. Biol. 81, 319-327.
39. Bottini, N., Stefanini, L., Williams, S., Alonso, A., Jascur, T., Abraham, R. T., Couture, C. and Mustelin, T. (2002) Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMWPTP). J. Biol. Chem. 277, 24220-24224.
40. Ohnuma, K., Inoue, H., Uchiyama, M., Yamochi, T., Hosono, O., Dang, N. H. and Morimoto, C. (2006) T cell activation via CD26 and caveolin-1 in rheumatoid synovium. Mod. Rheumatol. 16, 3-13.
41. Ohnuma, K., Uchiyama, M., Yamochi, T., Nishibashi, K., Hosono, O., Takahashi, N., Kina, S., Tanaka, H., Lin, X., Dang, N. H. and Morimoto, C. (2007) Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1, J. Biol. Chem. 282, 10117-10131.
42. Heneberg, P. and Dráber, P. (2005) Regulation of Cys-based protein tyrosine phosphatases via reactive oxygen and nitrogen species in mast cells and basophils. Curr. Med. Chem. 12, 763-771.
43. Murakami, K., Sato, S., Nagasawa, S. and Yamashita, T. (2000) Regulation of mast cell signaling through high-affinity IgE receptor by CD45 protein tyrosine phosphatases. Int. Immunol. 12, 169-176.
44. Heneberg, P. and Dráber, P. (2002) Nonreceptor protein tyrosine and lipid phosphatases in type I fc(epsilon) receptor-mediated activation of mast cells and basophils. Int. Arch. Allergy Immunol. 128, 253-263.
45. Mancini, F., Rigacci, S., Berti, A., Balduini, C., and Torti, M. (2007) The low molecular weight phosphotyrosine phosphatase is a negative regulator of FcγRIIA-mediated cell activation, Blood 110, 1871-1878.
46. Meloni, G., Bottini, N., Borgiani, P., Lucarelli, P., Meloni, T. and Bottini, E. (2003) Association of the ACP1 genotype with metabolic parameters upon initial diagnosis of type 1 diabetes. Med. Sci. Monit. 9, 105-108.
47. Spencer, N., Hopkinson, D. A. and Harris, H. (1964) Quantitative differences and gene dosage in the human red cell acid phosphatase polymorphism. Nature 201, 299-300.
48. Gloria-Bottini, F., Bottini, N. and Bottini, E. (2006) Effect of ACP1*C on early life viability. Hum, Biol. 78, 365-369.
49. Bottini, N., Meloni, G. F., Lucarelli, P., Amante, A., Saccucci, P., Gloria-Bottini, F. and Bottini, E. (2005) Risk of type 1 diabetes in childhood and maternal age at delivery, interaction with ACP1 and sex. Diabetes Metab. Res. Rev. 21, 353-358.
50. Bingley, P. J., Douek, I. F, Rogers, C. A. and Gale, E. A. M. (2000) Influence of maternal age at delivery and birth order on risk of type 1 diabetes in childhood: prospective population based family study. BMJ 321, 420-424.
51. Pandey, S. K., Yu, X. X., Watts, L. M., Michael, M. D., Sloop, K. W., Rivard, A. R., Leedom, T. A., Manchem, V. P., Samadzadeh, L., McKay, R., Monia, B. P. and Bhanot, S. (2007) Reduction of low molecular weight protein-tyrosine phosphatase expression improves hyperglycemia and insulin sensitivity in obese mice. J. Biol. Chem. 282, 14291-14299.
52. Bottini, N., Otsu, A., Borgiani, P., Saccucci, P., Stefanini, L., Greco, E., Fontana, L., Hopkins, J. M., Mao, X. Q. and Shirakawa, T. (2003) Genetic control of serum IgE levels: a study of low molecular weight protein tyrosine phosphatase. Clin. Genet. 63, 228-231.
53. Bottini, N., Mao, X. Q., Borgiani, P., Saccucci, P., Stefanini, L., Greco, E., Fontana L., Shirakawa, T. and Hopkin, J. M. (2002) Low molecular weight PTP-IL4RA interaction in atopy predisposition. Allergy 57, 10-12.
54. Gloria-Bottini, F., Bottini, N., Renzetti, G. and Bottini, E. (2007) ACP1 and Th class of immunological disease: evidence of interaction with gender. Int. Arch. Allergy Immunol. 143, 170-176.
55. Marzocchini, R., Malentacchi, F., Biagini, M., Cirelli, D., Luceri, C., Caderni, G. and Raugei, G. (2008) The expression of low molecular weight protein tyrosine phosphatase is upregulated in 1,2-dimethylhydrazine-induced colon tumours in rats. Int. J. Cancer 122, 1675-1678.
56. Chiarugi, P., Cirri, P., Raugei, G., Camici, G., Dolfi, F., Berti, A. and Ramponi, G. (1995) PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 372, 49-53.
57. Lee, J., Edderkaoui, M., Truong, P., Ohno, I., Jang, K., Berti, A., Pandol, S. and Gukovskaya, A. (2007) NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases. Gastroenterology 133, 1637 -1648.
58. Rigacci, S., Talini, D. and Berti, A. (2003) LMW-PTP associates and dephosphorylates STAT5 interacting with its C-terminal domain. Biochem. Biophys. Res. Commun. 312, 360-366.
59. Rigacci, S., Guidotti, V., Parri, M. and Berti, A. (2008) Modulation of STAT5 interaction with LMW-PTP during early megakaryocyte differentiation, Biochemistry 47, 1482-1489.
60. Kikawa, K. D., Vidale, D. R., Van Etten, R. L. and Kinch, M. S. (2002) Regulation of EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation. J. Biol. Chem. 277, 39274-39279.
61. Chiarugi, P., Cirri, P., Marra, F., Raugei, G., Camici, G., Manao, G. and Ramponi, G. (1997) LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signaling. Biochem. Biophys. Res. Commun. 238, 676-682.
62. Taddei, M. L., Chiarugi, P., Cirri, P., Buricchi, F., Fiaschi, T., Giannoni, E., Talini, D., Cozzi, G., Formigli, L., Raugei, G. and Ramponi, G. (2002) Beta-catenin interacts with low-molecular-weight protein tyrosine phosphatase leading to cadherin-mediated cell-cell adhesion increase. Cancer Res. 62, 6489-649.
63. Ramponi, G., andM. Stefani. (1997a) Structural, catalytic, and functional properties of low M(r) phosphotyrosine protein phosphatases. Evidence of a long evolutionary history. Int. J. Biochem. Cell Biol. 29, 279-292.
64. Ramponi, G., and M. Stefani. (1997b) Structure and function of the low Mr phosphotyrosine protein phosphatases. Biochim. Biophys. Acta. 1341, 137-156.
65. Park, E. K.; Warner, N.; Mood, K.; Pawson, T. and Daar, I.O. (2002) Low-molecular weight tyrosine phosphatase is a positive component of the fibroblast growth, factor receptor signaling pathway. Mol. Cell Biol. 22, 3404-3414.
66. Walker-Daniels, J., Hess, A. R., Hendrix, M. J. and Kinch, M. S. (2003) Differential regulation of EphA2 in normal and malignant cells. Am. J. Pathol. 162, 1037-1042.
67. Chiarugi, P., Taddei, M. L., Schiavone, N., Papucci, L., Giannoni, E., Fiaschi, T., Capaccioli, S., Raugei, G. and Ramponi, G. (2004) LMW-PTP is a positive regulator of tumor onset and growth. Oncogene 23, 3905-3914.
68. Kullander, K. and Klein, R. (2002) Mechanisms and functions of Eph and ephrin signaling. Nat. Rev. Mol. Cell. Biol. 3, 475-486.
69. Fang, W. B., Ireton, R. C., Zhuang, G., Takahashi, T., Reynolds, A. and Chen, J. (2008) Overexpression of EPHA2 receptor destabilizes adherens junctions via a RhoA-dependent mechanism. J. Cell Sci, 121, 358-368.
70. Chiarugi, P., Pani, G., Giannoni, E., Taddei, L., Colavitti, R., Raugei, G., Symons, M., Borrelo, S., Galeotti, T. and Ramponi, G. (2003) Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J. Cell Biol. 161, 933-944.
71. Shinoara, M., Shang, W. H., Kubodera, M., Harada, S., Mitsushita, J., Kato, M., Miyazaki, H., Sumimoto, H. and Kamata, T. (2007) Nox1 redox signaling mediates oncogenic Ras-induced disruption of stress fibers and focal adhesions by down-regulating Rho. J. Biol. Chem. 282, 17640-17648.
72. Nimnual, A. S., Taylor, L. J. and Bar-Sagi, D. (2003) Redox-dependent downregulation of Rho by Rac. Nat. Cell Biol. 5, 236-241.
73. Chiarugi, P., (2008) From anchorage dependent proliferation to survival: lessons from redox signalling. IUBMB Life. 60, 301-307.
74. Yu, H. and Jove, R. (2004) The STATs of cancer new molecular targets come of age. Nat. Rev. Cancer 4, 97-105.
75. Giannoni, E., Raugei, G., Chiarugi, P. and Ramponi, G. (2006) A novel redox- based switch: LMW-PTP oxidation enhances Grb2 binding and leads to ERK activation. Biochem. Bioph. Res. Comm. 348, 367-373.
76. Toyokuni, S., Okamoto, K., Yodoi, J. and Hiai, H. (1995) Persistent oxidative stress in cancer. FEBS Lett. 358, 1-3.
77. Szatrowski, T. P. and Nathan, C. F. (1991) Production of Large Amounts of Hydrogen Peroxide by Human Tumor Cells. Cancer Res. 51, 794-798.
78. Boivin, B., Zhang, S., Arbiser, J. L., Zhang, Z. Y. and Tonks, N. K. (2008) A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells. Proc. Natl. Acad. Sci. U S A. 105, 9959-9964.
79. Streit, S., Ruhe, J. E., Knyazev, P., Knyazeva, T., Iacobelli, S., Peter, S., Hoefler, H. and Ullrich, A. (2006) PTP-PEST phosphatase variations in human cancer. Cancer Genet. Cytogenet. 170, 48-53.
80. Tautz, L. and Mustelin, T. (2007) Strategies for developing protein tyrosine phosphatase inhibitors. Methods 42, 250-260.
81. Tautz L., Pellecchia, M. and Mustelin, T. (2006) Targeting the PTPome in human disease. Expert Opin. Ther. Targets 10, 157-177.
82. Zabell, A. P., Corden, S., Helquist, P., Stauffacher, C. V. and Wiest, O. (2004) Inhibition studies with rationally designed inhibitors of the human low molecular weight protein tyrosine phosphatase. Bioorg. Med. Chem. 12, 1867-1880.
83. Miranda, M. A., Okamoto, A. K., Ferreira, C. V., Silva, T. L., Granjeiro, J.M. and Aoyama, H. (2006) Differential effects of flavonoids on bovine kidney low molecular mass protein tyrosine phosphatase. J. Enzyme Inhib. Med. Chem. 21, 419-425.
84. Bispo de Jesus, M., Zambuzzi, W. F., Ruela de Sousa, R. R., Areche, C., Santos de Souza, A. C., Aoyama, H., Schmeda-Hirschmann, G., Rodriguez, J. A., Monteiro de Souza Brito, A. R., Peppelenbosch, M. P., den Hertog, J., de Paula, E. and Ferreira, C.V. (2008) Ferruginol suppresses survival signaling pathways in androgen-independent human prostate cancer cells. Biochimie. 90, 843-854.
85. Maccari, R., Paoli, P., Ottanà, R., Jacomelli, M., Ciurleo, R., Manao, G., Steindl, T., Langer, T., Vigorita, M. G. and Camici, G. (2007) 5-Arylidene-2,4-thiazolidinediones as inhibitors of protein tyrosine phosphatases. Bioorg. Med. Chem. 15, 5137-5149.