medigraphic.com
ISSN 1027-2852 (Electronic)
ISSN 0864-4551 (Print)

2014, Number 2

<< Back Next >>

Biotecnol Apl 2014; 31 (2)

Dipeptidyl peptidase IV and its implication in cancer

Arrebola YM, Gómez H, Valiente PA, Chávez MÁ, Pascual I

Language: Spanish
References: 128
Page: 93-101
PDF size: 571.83 Kb.


ABSTRACT

Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5), also known as CD26, is a serine aminopeptidase that preferentially cleaves Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of oligopeptides and processes regulatory peptides in vivo, leading to their biological activation or inactivation. The ezyme is a homodimer and each subunit is formed by a αβ-hydrolase domain and a β-propeller domain, involved in the enzymatic activity and its interaction with other proteins. It has an important role in multiple physiological functions, including the regulation of glucose metabolism being one of the current targets for the treatment of type II diabetes mellitus. This enzyme also regulates immune system responses mediated by CD4+ T lymphocytes, and recently has been identified a high/low DPP-IV activity regarding physiological levels, in pathologies like thyroid, ovarian, lung, skin, prostate cancers and central nervous system tumors. For these reasons this enzyme evolves as a new target of attention for the development of more efficient diagnostics being considering as molecular markers for some pathologies and target for the development of new therapeutic assessments in cancer. Current research interests are focused in depth in the structure-function relation for this enzyme, as a key point for the development of new therapies in pathologies involving DPP-IV activity or its interaction with other proteins.


REFERENCES

  1. Turk B. Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov. 2006;5(9):785-99.

  2. Leung D, Abbenante G, Fairlie DP. Protease inhibitors: current status and future prospects. J Med Chem. 2000;43(3):305-41.

  3. Abbenante G, Fairlie DP. Protease in- hibitors in the clinic. Med Chem. 2005;1(1): 71-104.

  4. Itou M, Kawaguchi T, Taniguchi E, Sata M. Dipeptidyl peptidase-4: a key player in chronic liver disease. World J Gastroenterol. 2013;19(15):2298-306.

  5. Gorrell MD, Wang XM, Park J, Ajami K, Yu DM, Knott H, et al. Structure and function in dipeptidyl peptidase IV and related proteins. Adv Exp Med Biol. 2006; 575:45-54.

  6. Yu DM, Yao TW, Chowdhury S, Nadvi NA, Osborne B, Church WB, et al. The dipeptidyl peptidase IV family in cancer and cell biology. FEBS J. 2010;277(5):1126-44.

  7. Leiting B, Pryor KD, Wu JK, Marsilio F, Patel RA, Craik CS, et al. Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII. Biochem J. 2003;371(Pt 2):525-32.

  8. Hopsu-Havu VK, Glenner GG. A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide. Histochemie. 1966;7(3):197-201.

  9. Palmieri FE, Ward PE. Dipeptidyl(amino) peptidase IV and post proline cleaving enzyme in cultured endothelial and smooth muscle cells. Adv Exp Med Biol. 1989; 247A:305-11.

  10. Hu CX, Huang H, Zhang L, Huang Y, Shen ZF, Cheng KD, et al. A new screening method based on yeast-expressed human dipeptidyl peptidase IV and discovery of novel inhibitors. Biotechnol Lett. 2009;31(7):979-84.

  11. Durinx C, Lambeir AM, Bosmans E, Falmagne JB, Berghmans R, Haemers A, et al. Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/ dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides. Eur J Biochem. 2000;267(17):5608-13.

  12. Stano J, Kovacs P, Kakoniova D, Kirilova ND, Komov VP. Activity of dipeptidyl peptidase IV in gingseng callus culture. Biologia. 1994;49:353-7.

  13. Koreeda Y, Hayakawa M, Ikemi T, Abiko Y. Isolation and characterisation of dipeptidyl peptidase IV from Prevotella loescheii ATCC 15930. Arch Oral Biol. 2001;46(8):759-66.

  14. Davy A, Thomsen KK, Juliano MA, Alves LC, Svendsen I, Simpson DJ. Purification and characterization of barley dipeptidyl peptidase IV. Plant Physiol. 2000;122(2):425-32.

  15. Bauvois B, Djavaheri-Mergny M, Rouillard D, Dumont J, Wietzerbin J. Regulation of CD26/DPPIV gene expression by interferons and retinoic acid in tumor B cells. Oncogene. 2000;19(2):265-72.

  16. de Meester I, Vanhoof G, Lambeir AM, Scharpe S. Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26/dipeptidyl peptidase IV (EC 3.4.14.5). J Immunol Methods. 1996;189(1):99-105.

  17. Wilson MJ, Ruhland AR, Pryor JL, Ercole C, Sinha AA, Hensleigh H, et al. Prostate specific origin of dipeptidylpeptidase IV (CD-26) in human seminal plasma. J Urol. 1998;160(5):1905-9.

  18. Engel M, Hoffmann T, Wagner L, Wermann M, Heiser U, Kiefersauer R, et al. The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc Natl Acad Sci USA. 2003;100(9):5063-8.

  19. Abbott CA, Baker E, Sutherland GR, McCaughan GW. Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene. Immunogenetics. 1994;40(5):331-8.

  20. Bohm SK, Gum JR, Jr., Erickson RH, Hicks JW, Kim YS. Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter. Biochem J. 1995;311(Pt 3): 835-43.

  21. Hong WJ, Petell JK, Swank D, Sanford J, Hixson DC, Doyle D. Expression of dipeptidyl peptidase IV in rat tissues is mainly regulated at the mRNA levels. Exp Cell Res. 1989;182(1):256-66.

  22. Kahne T, Kroning H, Thiel U, Ulmer AJ, Flad HD, Ansorge S. Alterations in structure and cellular localization of molecular forms of DP IV/CD26 during T cell activation. Cell Immunol. 1996;170(1):63-70.

  23. Gorrell MD. Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clin Sci (Lond). 2005;108(4): 277-92.

  24. Yu DM, Ajami K, Gall MG, Park J, Lee CS, Evans KA, et al. The in vivo expression of dipeptidyl peptidases 8 and 9. J Histochem Cytochem. 2009;57(11):1025-40.

  25. Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA. A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion. Blood. 2004;103(10):3783-8.

  26. Ajami K, Abbott CA, McCaughan GW, Gorrell MD. Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity. Biochim Biophys Acta. 2004;1679(1):18-28.

  27. Delacour D, Gouyer V, Leteurtre E, Ait-Slimane T, Drobecq H, Lenoir C, et al. 1-benzyl-2-acetamido-2-deoxy-alpha- D-galactopyranoside blocks the apical biosynthetic pathway in polarized HT-29 cells. J Biol Chem. 2003;278(39):37799-809.

  28. 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(1):19-25.

  29. Duke-Cohan JS, Morimoto C, Rocker JA, Schlossman SF. Serum high molecular weight dipeptidyl peptidase IV (CD26) is similar to a novel antigen DPPT-L released from activated T cells. J Immunol. 1996;156(5):1714-21.

  30. Pascual I, Gomez H, Pons T, Chappe M, Vargas MA, Valdes G, et al. Effect of divalent cations on the porcine kidney cortex membrane-bound form of dipeptidyl peptidase IV. Int J Biochem Cell Biol. 2011;43(3):363-71.

  31. Gomez H, Chappe M, Valiente PA, Pons T, Chavez Mde L, Charli JL, et al. Effect of zinc and calcium ions on the rat kidney membrane-bound form of dipeptidyl peptidase IV. J Biosci. 2013;38(3):461-9.

  32. Thoma R, Loffler B, Stihle M, Huber W, Ruf A, Hennig M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure. 2003;11(8):947-59.

  33. Aertgeerts K, Ye S, Tennant MG, Kraus ML, Rogers J, Sang BC, et al. Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci. 2004;13(2):412-21.

  34. Abbott CA, McCaughan GW, Gorrell MD. Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity. FEBS Lett. 1999;458(3):278-84.

  35. Ajami K, Abbott CA, Obradovic M, Gysbers V, Kahne T, McCaughan GW, et al. Structural requirements for catalysis, expression, and dimerization in the CD26/ DPIV gene family. Biochemistry. 2003; 42(3):694-701.

  36. Chien CH, Huang LH, Chou CY, Chen YS, Han YS, Chang GG, et al. One site mutation disrupts dimer formation in human DPP-IV proteins. J Biol Chem. 2004; 279(50):52338-45.

  37. Varghese JN, Laver WG, Colman PM. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature. 1983;303(5912):35-40.

  38. Vellieux FM, Huitema F, Groendijk H, Kalk KH, Jzn JF, Jongejan JA, et al. Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution. EMBO J. 1989;8(8):2171-8.

  39. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, et al. Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Nature. 1991;350(6313):87-90.

  40. Xia ZX, Dai WW, Xiong JP, Hao ZP, Davidson VL, White S, et al. The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution. J Biol Chem. 1992; 267(31):22289-97.

  41. Murzin AG. Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. Proteins. 1992;14(2):191-201.

  42. Fülöp V, Jones DT. Beta propellers: structural rigidity and functional diversity. Curr Opin Struct Biol. 1999;9(6):715-21.

  43. Paoli M. Protein folds propelled by diversity. Prog Biophys Mol Biol. 2001;76(1-2): 103-30.

  44. Jawad Z, Paoli M. Novel sequences propel familiar folds. Structure. 2002; 10(4):447-54.

  45. Adams J, Kelso R, Cooley L. The kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol. 2000; 10(1):17-24.

  46. Russell RB, Sasieni PD, Sternberg MJ. Supersites within superfolds. Binding site similarity in the absence of homology. J Mol Biol. 1998;282(4):903-18.

  47. Todd AE, Orengo CA, Thornton JM. Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol. 2001;307(4):1113-43.

  48. Pons T, Gomez R, Chinea G, Valencia A. Beta-propellers: associated functions and their role in human diseases. Curr Med Chem. 2003;10(6):505-24.

  49. Love CA, Harlos K, Mavaddat N, Davis SJ, Stuart DI, Jones EY, et al. The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D. Nat Struct Biol. 2003;10(10):843-8.

  50. Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3. Science. 2001; 294(5541):339-45.

  51. Hiramatsu H, Yamamoto A, Kyono K, Higashiyama Y, Fukushima C, Shima H, et al. The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A. Biol Chem. 2004;385(6):561-4.

  52. Oefner C, D’Arcy A, Mac Sweeney A, Pierau S, Gardiner R, Dale GE. High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl] amino)-acetyl]-2-cyano-(S)-pyrrolidine. Acta Crystallogr D Biol Crystallogr. 2003;59(Pt 7):1206-12.

  53. Weihofen WA, Liu J, Reutter W, Saenger W, Fan H. Crystal structure of CD26/ dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface. J Biol Chem. 2004; 279(41):43330-5.

  54. Abbott CA, Gorrell MD. The family of CD26/DPP-IV and related ectopeptidases. In: Langner J, Ansorge S, editors. Ectopeptidases. CD13/aminopeptidase N and CD26/dipeptidylpeptidase IV in medicine and biology. New York: Kluwer Academic / Plenum Publishers; 2002. p. 171-95.

  55. Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100(1):57-70.

  56. Carl-McGrath S, Lendeckel U, Ebert M, Rocken C. Ectopeptidases in tumour biology: a review. Histol Histopathol. 2006; 21(12):1339-53.

  57. Iwata S, Morimoto C. CD26/dipeptidyl peptidase IV in context. The different roles of a multifunctional ectoenzyme in malignant transformation. J Exp Med. 1999; 190(3):301-6.

  58. Wesley UV, Albino AP, Tiwari S, Houghton AN. A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells. J Exp Med. 1999; 190(3):311-22.

  59. Sedo A, Krepela E, Kasafirek E. Dipeptidyl peptidase IV, prolyl endopeptidase and cathepsin B activities in primary human lung tumors and lung parenchyma. J Cancer Res Clin Oncol. 1991;117(3):249-53.

  60. Asada Y, Aratake Y, Kotani T, Marutsuka K, Araki Y, Ohtaki S, et al. Expression of dipeptidyl aminopeptidase IV activity in human lung carcinoma. Histopathology. 1993;23(3):265-70.

  61. Wesley UV, Tiwari S, Houghton AN. Role for dipeptidyl peptidase IV in tumor suppression of human non small cell lung carcinoma cells. Int J Cancer. 2004; 109(6):855-66.

  62. Dimitrova M, Ivanov I, Todorova R, Stefanova N, Moskova-Doumanova V, Topouzova- Hristova T, et al. Comparison of the activity levels and localization of dipeptidyl peptidase IV in normal and tumor human lung cells. Tissue Cell. 2012;44(2):74-9.

  63. Bogenrieder T, Finstad CL, Freeman RH, Papandreou CN, Scher HI, Albino AP, et al. Expression and localization of aminopeptidase A, aminopeptidase N, and dipeptidyl peptidase IV in benign and malignant human prostate tissue. Prostate. 1997;33(4):225-32.

  64. Frohlich E, Maier E, Wahl R. Interspecies differences in membrane-associated protease activities of thyrocytes and their relevance for thyroid cancer studies. J Exp Clin Cancer Res. 2012;31:45.

  65. Kotani T, Asada Y, Aratake Y, Umeki K, Yamamoto I, Tokudome R, et al. Diagnostic usefulness of dipeptidyl aminopeptidase IV monoclonal antibody in paraffin-embedded thyroid follicular tumours. J Pathol. 1992;168(1):41-5.

  66. Tanaka T, Umeki K, Yamamoto I, Sakamoto F, Noguchi S, Ohtaki S. CD26 (dipeptidyl peptidase IV/DPP IV) as a novel molecular marker for differentiated thyroid carcinoma. Int J Cancer. 1995; 64(5):326-31.

  67. Tang AC, Raphael SJ, Lampe HB, Matthews TW, Becks GP. Expression of dipeptidyl aminopeptidase IV activity in thyroid tumours: a possible marker of thyroid malignancy. J Otolaryngol. 1996; 25(1):14-9.

  68. Maruta J, Hashimoto H, Yamashita H, Yamashita H, Noguchi S. Diagnostic applicability of dipeptidyl aminopeptidase IV activity in cytological samples for differentiating follicular thyroid carcinoma from follicular adenoma. Arch Surg. 2004; 139(1):83-8.

  69. Khin EE, Kikkawa F, Ino K, Kajiyama H, Suzuki T, Shibata K, et al. Dipeptidyl peptidase IV expression in endometrial endometrioid adenocarcinoma and its inverse correlation with tumor grade. Am J Obstet Gynecol. 2003;188(3):670-6.

  70. Kikkawa F, Kajiyama H, Ino K, Shibata K, Mizutani S. Increased adhesion potency of ovarian carcinoma cells to mesothelial cells by overexpression of dipeptidyl peptidase IV. Int J Cancer. 2003;105(6):779-83.

  71. Pro B, Dang NH. CD26/dipeptidyl peptidase IV and its role in cancer. Histol Histopathol. 2004;19(4):1345-51.

  72. Goscinski MA, Suo ZH, Nesland JM, Florenes VA, Giercksky KE. Dipeptidyl peptidase IV expression in cancer and stromal cells of human esophageal squamous cell carcinomas, adenocarcinomas and squamous cell carcinoma cell lines. APMIS. 2008;116(9):823-31.

  73. Bauvois B, De Meester I, Dumont J, Rouillard D, Zhao HX, Bosmans E. Constitutive expression of CD26/dipeptidylpeptidase IV on peripheral blood B lymphocytes of patients with B chronic lymphocytic leukaemia. Br J Cancer. 1999;79(7-8):1042-8.

  74. Cro L, Morabito F, Zucal N, Fabris S, Lionetti M, Cutrona G, et al. CD26 expression in mature B-cell neoplasia: its possible role as a new prognostic marker in B-CLL. Hematol Oncol. 2009;27(3):140-7.

  75. Havre PA, Dang LH, Ohnuma K, Iwata S, Morimoto C, Dang NH. CD26 expression on T-anaplastic large cell lymphoma (ALCL) line Karpas 299 is associated with increased expression of versican and MT1-MMP and enhanced adhesion. BMC cancer. 2013;13:517.

  76. Stremenova J, Krepela E, Mares V, Trim J, Dbaly V, Marek J, et al. Expression and enzymatic activity of dipeptidyl peptidase-IV in human astrocytic tumours are associated with tumour grade. Int J Oncol. 2007;31(4):785-92.

  77. Stremenova J, Mares V, Lisa V, Hilser M, Krepela E, Vanickova Z, et al. Expression of dipeptidyl peptidase-IV activity and/or structure homologs in human meningiomas. Int J Oncol. 2010;36(2):351-8.

  78. Arscott WT, LaBauve AE, May V, Wesley UV. Suppression of neuroblastoma growth by dipeptidyl peptidase IV: relevance of chemokine regulation and caspase activation. Oncogene. 2009;28(4):479-91.

  79. Dinjens WN, Ten Kate J, Kirch JA, Tanke HJ, Van der Linden EP, Van den Ingh HF, et al. Adenosine deaminase complexing protein (ADCP) expression and metastatic potential in prostatic adenocarcinomas. J Pathol. 1990; 160(3):195-201.

  80. Wesley UV, McGroarty M, Homoyouni A. Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway. Cancer Res. 2005;65(4):1325-34.

  81. Urade M, Komatsu M, Yamaoka M, Fukasawa K, Harada M, Mima T, et al. Serum dipeptidyl peptidase activities as a possible marker of oral cancer. Cancer. 1989;64(6):1274-80.

  82. de la Haba-Rodriguez J, Macho A, Calzado MA, Blazquez MV, Gomez MA, Munoz EE, et al. Soluble dipeptidyl peptidase IV (CD-26) in serum of patients with colorectal carcinoma. Neoplasma. 2002;49(5):307-11.

  83. Cordero OJ, Imbernon M, Chiara LD, Martinez-Zorzano VS, Ayude D, de la Cadena MP, et al. Potential of soluble CD26 as a serum marker for colorectal cancer detection. World J Clin Oncol. 2011;2(6):245-61.

  84. Gonzalez-Gronow M, Misra UK, Gawdi G, Pizzo SV. Association of plasminogen with dipeptidyl peptidase IV and Na+/H+ exchanger isoform NHE3 regulates invasion of human 1-LN prostate tumor cells. J Biol Chem. 2005;280(29):27173-8.

  85. Gorrell MD, Gysbers V, McCaughan GW. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand J Immunol. 2001;54(3):249-64.

  86. Cheng HC, Abdel-Ghany M, Pauli BU. A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis. J Biol Chem. 2003;278(27):24600-7.

  87. Cheng HC, Abdel-Ghany M, Elble RC, Pauli BU. Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin. J Biol Chem. 1998;273(37):24207-15.

  88. Korach S, Poupon MF, Du Villard JA, Becker M. Differential adhesiveness of rhabdomyosarcoma- derived cloned metastatic cell lines to vascular endothelial monolayers. Cancer Res. 1986;46(7):3624-9.

  89. Kato Y, Saijo N. Developed new agents for lung cancer. Nihon Geka Gakkai zasshi. 2002;103(2):218-23.

  90. Mentlein R, Dahms P, Grandt D, Kruger R. Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul Pept. 1993;49(2):133-44.

  91. Ghersi G, Chen W, Lee EW, Zukowska Z. Critical role of dipeptidyl peptidase IV in neuropeptide Y-mediated endothelial cell migration in response to wounding. Peptides. 2001;22(3):453-8.

  92. Mathew S, Morrison ME, Murty VV, Houghton AN, Chaganti RS. Assignment of the DPP4 gene encoding adenosine deaminase binding protein (CD26/dipeptidylpeptidase IV) to 2q23. Genomics. 1994;22(1):211-2.

  93. Otsuka T, Kohno T, Mori M, Noguchi M, Hirohashi S, Yokota J. Deletion mapping of chromosome 2 in human lung carcinoma. Genes Chromosomes Cancer. 1996;16(2):113-9.

  94. Shiseki M, Kohno T, Nishikawa R, Sameshima Y, Mizoguchi H, Yokota J. Frequent allelic losses on chromosomes 2q, 18q, and 22q in advanced non-small cell lung carcinoma. Cancer Res. 1994;54(21):5643-8.

  95. Morrison H, Sherman LS, Legg J, Banine F, Isacke C, Haipek CA, et al. The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44. Genes Dev. 2001;15(8):968-80.

  96. Yan P, Muhlethaler A, Bourloud KB, Beck MN, Gross N. Hypermethylation-mediated regulation of CD44 gene expression in human neuroblastoma. Genes Chromosomes Cancer. 2003;36(2):129-38.

  97. Kajiyama H, Kikkawa F, Maeda O, Suzuki T, Ino K, Mizutani S. Increased expression of dipeptidyl peptidase IV in human mesothelial cells by malignant ascites from ovarian carcinoma patients. Oncology. 2002;63(2):158-65.

  98. Ware JL. Growth factor network disruption in prostate cancer progression. Cancer Metastasis Rev. 1998;17(4):443-7.

  99. Giri D, Ropiquet F, Ittmann M. Alterations in expression of basic fibroblast growth factor (FGF) 2 and its receptor FGFR-1 in human prostate cancer. Clin Cancer Res. 1999;5(5): 1063-71.

  100. Dow JK, deVere White RW. Fibroblast growth factor 2: its structure and property, paracrine function, tumor angiogenesis, and prostate-related mitogenic and oncogenic functions. Urology. 2000;55(6):800-6.

  101. Feldman BJ, Feldman D. The development of androgen-independent prostate cancer. Nat Rev Cancer. 2001;1(1):34-45.

  102. Isaacs JT, Isaacs WB. Androgen receptor outwits prostate cancer drugs. Nat Med. 2004; 10(1):26-7.

  103. Boonacker E, Van Noorden CJ. The multifunctional or moonlighting protein CD26/ DPPIV. Eur J Cell Biol. 2003;82(2):53-73.

  104. Proost P, Struyf S, Schols D, Opdenakker G, Sozzani S, Allavena P, et al. Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction. J Biol Chem. 1999;274(7):3988-93.

  105. Nakamoto T, Chang CS, Li AK, Chodak GW. Basic fibroblast growth factor in human prostate cancer cells. Cancer Res. 1992; 52(3):571-7.

  106. Gioeli D, Mandell JW, Petroni GR, Frierson HF, Jr., Weber MJ. Activation of mitogen-activated protein kinase associated with prostate cancer progression. Cancer Res. 1999;59(2):279-84.

  107. Pintucci G, Moscatelli D, Saponara F, Biernacki PR, Baumann FG, Bizekis C, et al. Lack of ERK activation and cell migration in FGF-2-deficient endothelial cells. FASEB J. 2002;16(6):598-600.

  108. Giuliani R, Bastaki M, Coltrini D, Presta M. Role of endothelial cell extracellular signal- regulated kinase1/2 in urokinase-type plasminogen activator upregulation and in vitro angiogenesis by fibroblast growth factor- 2. J Cell Sci. 1999;112 (Pt 15):2597-606.

  109. Rabbani SA, Mazar AP. The role of the plasminogen activation system in angiogenesis and metastasis. Surg Oncol Clin N Am. 2001;10(2):393-415.

  110. Bugler B, Amalric F, Prats H. Alternative initiation of translation determines cytoplasmic or nuclear localization of basic fibroblast growth factor. Mol Cell Biol. 1991;11(1):573-7.

  111. Bikfalvi A, Klein S, Pintucci G, Rifkin DB. Biological roles of fibroblast growth factor-2. Endocr Rev. 1997;18(1):26-45.

  112. Delrieu I. The high molecular weight isoforms of basic fibroblast growth factor (FGF-2): an insight into an intracrine mechanism. FEBS Lett. 2000;468(1):6-10.

  113. Arwert EN, Mentink RA, Driskell RR, Hoste E, Goldie SJ, Quist S, et al. Upregulation of CD26 expression in epithelial cells and stromal cells during wound-induced skin tumour formation. Oncogene. 2012;31(8):992-1000.

  114. Ehtesham M, Winston JA, Kabos P, Thompson RC. CXCR4 expression mediates glioma cell invasiveness. Oncogene. 2006;25(19): 2801-6.

  115. Christopherson KW, 2nd, Hangoc G, Broxmeyer HE. Cell surface peptidase CD26/ dipeptidylpeptidase IV regulates CXCL12/stromal cell-derived factor-1 alpha-mediated chemotaxis of human cord blood CD34+ progenitor cells. J Immunol. 2002;169(12):7000-8.

  116. Vangoitsenhoven R, Mathieu C, Van der Schueren B. GLP1 and cancer: friend or foe? Endocr Relat Cancer. 2012;19(5):F77-88.

  117. Korner M, Stockli M, Waser B, Reubi JC. GLP-1 receptor expression in human tumors and human normal tissues: potential for in vivo targeting. J Nucl Med. 2007;48(5):736-43.

  118. Koehler JA, Drucker DJ. Activation of glucagon-like peptide-1 receptor signaling does not modify the growth or apoptosis of human pancreatic cancer cells. Diabetes. 2006; 55(5):1369-79.

  119. Girman CJ, Kou TD, Cai B, Alexander CM, O’Neill EA, Williams-Herman DE, et al. Patients with type 2 diabetes mellitus have higher risk for acute pancreatitis compared with those without diabetes. Diabetes Obes Metab. 2010;12(9):766-71.

  120. Garg R, Chen W, Pendergrass M. Acute pancreatitis in type 2 diabetes treated with exenatide or sitagliptin: a retrospective observational pharmacy claims analysis. Diabetes Care. 2010;33(11):2349-54.

  121. Dore DD, Bloomgren GL, Wenten M, Hoffman C, Clifford CR, Quinn SG, et al. A cohort study of acute pancreatitis in relation to exenatide use. Diabetes Obes Metab. 2011; 13(6):559-66.

  122. Nyborg NC, Molck AM, Madsen LW, Knudsen LB. The human GLP-1 analog liraglutide and the pancreas: evidence for the absence of structural pancreatic changes in three species. Diabetes. 2012;61(5):1243-9.

  123. Bjerre Knudsen L, Madsen LW, Andersen S, Almholt K, de Boer AS, Drucker DJ, et al. Glucagon-like Peptide-1 receptor agonists activate rodent thyroid C-cells causing calcitonin release and C-cell proliferation. Endocrinology. 2010;151(4):1473-86.

  124. Waser B, Beetschen K, Pellegata NS, Reubi JC. Incretin receptors in non-neoplastic and neoplastic thyroid C cells in rodents and humans: relevance for incretin-based diabetes therapy. Neuroendocrinology. 2011; 94(4):291-301.

  125. Roman S, Lin R, Sosa JA. Prognosis of medullary thyroid carcinoma: demographic, clinical, and pathologic predictors of survival in 1252 cases. Cancer. 2006;107(9):2134-42.

  126. Koehler JA, Kain T, Drucker DJ. Glucagon- like peptide-1 receptor activation inhibits growth and augments apoptosis in murine CT26 colon cancer cells. Endocrinology. 2011; 152(9):3362-72.

  127. Ligumsky H, Wolf I, Israeli S, Haimsohn M, Ferber S, Karasik A, et al. The peptide-hormone glucagon-like peptide-1 activates cAMP and inhibits growth of breast cancer cells. Breast Cancer Res Treat. 2012;132(2):449-61.

  128. Xia Z, Dickens M, Raingeaud J, Davis RJ, Greenberg ME. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 1995;270(5240):1326-31.




2020     |     www.medigraphic.com