[1]
Giovannucci, E.; David, M.H.; Michael, C.A.; Richard, M.B.; Susan, M.G.; Laurel, A.H. Michael. P.; Regensteiner, J.G.; Douglas, Y. Diabetes and Cancer. A consensus report. Diabetes Care, 2010, 33(7), 1674-1685.
[2]
Guojing, L.; Hong, L.; and Hongyun, L. Glucagon‐like peptide‐1(GLP‐1) receptor agonists: potential to reduce fracture risk in diabetic patients? J. Clin. Pharmacol., 2016, 81(1), 78-88.
[3]
Chinmay, S.M.; Christopher, K.R.; Karen, L.J.; Michael, H. Diabetes Care, 2013, 36(5), 1396-1405.
[4]
Kieffer, T.J.; Mclntosh, C.H.; Pederson, R.A. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagonlike peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology, 1995, 136, 3585-3596.
[5]
Meier, J.J.; Nauck, M.A.; Schmidt, W.E.; Gallwitz, B. Gastric inhibitory polypeptide: The neglected incretin revisited. Regul. Pept., 2002, 107(1-3), 1-13.
[6]
Egan, J.M.; Bulotta, A.; Hui, H.; Perfetti, R. GLP-1 receptor agonists are growth and differentiation factors for pancreatic islet beta cells. Diabetes Metab. Res. Rev., 2003, 19(2), 115-123.
[7]
Murphy, K.G.; Dhillo, W.S.; Bloom, S.R. Gut peptides in the regulation of food intake and energy homeostasis. Endocr. Rev., 2006, 27(7), 719-727.
[8]
Mclntosh, C.H.S. Dipeptidyl peptidase IV inhibitors and diabetes therapy. Front. Biosci Landmark Ed., 2008, 13, 1753-1773.
[9]
Matteucci, E.; Giampietro, O. Dipeptidyl peptidase-4 (CD26): knowing the functionbefore inhibiting the enzyme. Curr. Med. Chem., 2009, 16(23), 2943-2951.
[10]
aKshirsagar, A.D.; Aggarwal, A.S.; Harle, U.N.; Deshpande, A.D. DPP IV inhibitors: Successes, failures and future prospects. Diabetes Metab. Syndr., 2011, 5, 105-112.
bAbbott, C.A.; Baker, E.; Sutherland, G.R.; McCaughan, G.W. Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene. Immunogenetics, 1994, 40, 31-38.
[11]
Cheng, H.C.; Abdel-Ghany, M.; Elble, R.C.; Pauli, B.U. 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), 24207-24215.
[12]
Pethiyagoda, C.L.; Welch, D.R.; Fleming, T.P. Dipeptidyl peptidase IV (DPPIV) inhibits cellular invasion of melanoma cells. Clin. Exp. Metastasis, 2000, 18(5), 391-400.
[13]
Aytac, U.; Claret, F.X.; Ho, L.; Sato, K.; Ohnuma, K.; Mills, G.B.; Cabanillas, F.; Morimoto, C.; Dang, N.H. Expression of CD26 and its associated dipeptidyl peptidase IV enzyme activity enhances sensitivity to doxorubicin-induced cell cycle arrest at the G(2)/M checkpoint. Cancer Res., 2001, 61(19), 7204-7210.
[14]
Wesley, U.V.; Albino, A.P.; Tiwari, S.; Houghton, A.N. A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells. J. Exp. Med., 1999, 190(3), 311-322.
[15]
Engel, M.; Hoffmann, T.; Manhart, S.; Heiser, U.; Chambre, S.; Huber, R.; Demuth, H.U.; Bode, W. Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV. J. Mol. Biol., 2006, 355(4), 768-783.
[16]
Kuhn, B.; Hennig, M.; Mattei, P. Molecular recognition of ligands in dipeptidyl peptidase IV. Curr. Top. Med. Chem., 2007, 7(6), 609-619.
[17]
Watanabe, Y.S.; Yasuda, Y.; Kojima, Y.; Okada, S.; Motoyama, T.; Takahashi, R.; Oka, M. Anagliptin, a potent dipeptidyl peptidase IV inhibitor: Its single-crystal structure and enzyme interactions. J. Enzyme Inhib. Med. Chem., 2015, 30(6), 981-988.
[18]
Lucienne, J.J. Dipeptidyl Peptidase IV and Its Inhibitors: Therapeutics for Type 2 Diabetes and What Else? J. Med. Chem., 2014, 57(6), 2197-2212.
[19]
Rotella, D.P. Novel Second-Generation approaches for the control of type 2 diabetes. J. Med. Chem., 2004, 47(17), 4111-4112.
[20]
Weber, A.E. Dipeptidyl Peptidase IV Inhibitors for the treatment of Diabetes. J. Med. Chem., 2004, 47(17), 4135-4141.
[21]
Gorrell, M.D. Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clin. Sci. (Lond.), 2005, 108(4), 277-292.
[22]
Struyf, S.; Proost, P.; Schols, D. E.D.; Clercq, E.D.; Opdenakker, G.; Jean-Pierre, L.; Detheux, M.; Parmentier, M.; Meester, I.D.; Simmon, S.; Damme, J.V. CD26/Dipeptidyl-peptidase IV down-regulates the eosinophil chemotactic potency, but not the anti-HIV activity of human eotaxin by affecting its interaction with CC chemokine receptor 3. J. Immunol., 1999, 162(8), 4903-4909.
[23]
Sedo, A.; Duke-Cohan, J. S.; Balaziova, E.; Sedova, L, R. Dipeptidyl peptidase IV activity and/or structure homologs: Contributing factors in the pathogenesis of rheumatoid arthritis? Arthritis Res. Ther., 2005, 7, 253-269.
[24]
Detel, D.; Kehler, T.; Buljevic, S.; Pavacic, I.; Pucar, L.B.; Varljen, N.; Varljen, J. Is dipeptidyl peptidase IV (DPP IV) associated with inflammation present in human spondyloarthritides and rheumatoid arthritis. Croat. Chem. Acta, 2012, 85(2), 231-238.
[25]
Gotoh, H.; Haglhara, M.; Nagateu, T.; Iwata, H.; Mlura, T. Activities of dipeptidyl peptidase II and dipeptidyl peptidase IV in synovial fluid from patients with rheumatoid arthritis and osteoarthritis. Clin. Chem., 1989, 35(6), 1016-1018.
[26]
Rossi, D.; Zlotnik, A. The biology of chemokines and their receptors. Annu. Rev. Immunol., 2000, 18, 217-242.
[28]
Villhauer, E.B.; Brinkman, J.A.; Naderi, G.B.; Burkey, B.N.F.; Dunning, B.E.; Prasad, K.; Mangold, B.L.; Russell, M.E.; Hughes, T.E. 1-3[(3-Hydroxy-1-adamantyl)amino] acetyl-2-cyano-(S)-pyrrolidine, a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. J. Med. Chem., 2003, 46(13), 2774-2789.
[29]
Augeri, D.J.; Robl, J.A.; Khanna, A.; Robertson, J.G.; Wang, A.; Simpkins, L.M.; Taunk, P.; Huang, Q.; Han, S.P.; Abboa-Offei, B.; Cap, M.; Xin, L.; Tao, L.; Tozzo, E.; Welzel, G.E.; Egan, D.M.; Marcinkeviciene, J.; Chang, S.Y.; Biller, S.A.; Kirby, M.S.; Parker, R.A.; Hamann, L.G. Discovery and preclinical profile of saxagliptin (BMS-477118): A highly potent, long-acting, orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes. J. Med. Chem., 2005, 48(15), 5025-5037.
[30]
Feng, J.; Zhang, Z.; Wallace, M.; Stafford, J.; Kaldor, S.; Kassel, D.; Navre, M.; Shi, L. Discovery of alogliptin: A potent, selective, bioavailable, and efficacious inhibitor of dipeptidyl peptidase IV. J. Med. Chem., 2007, 50(10), 2297-2300.
[31]
Eckhardt, M.; Langkop, E.; Mark, M.; Tadayyon, M.; Thomas, L.; Nar, H.; Pfengle, W.; Guth, B.; Lotz, R.; Siegel, P.; Fuchs, H.; Himmelsbach, E. 8-[(3R)-3-aminopiperidin-1-yl]-7-(but-2-yn-1-yl)-3- methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine- 2,6-dione (BI-1356) a highly potent, selective, long-acting, and orally bioavailable DPP-4 inhibitor for the treatment of type-2 diabetes. J. Med. Chem., 2007, 50(26), 6450-6453.
[32]
Lim, K.S.; Cho, J.Y.; Kim, B.H.; Kim, J.R.; Kim, H.S.; Kim, D.K.; Kim, S.H.; Yim, H.J.; Lee, S.H.; Shin, S.G.; Jang, I.J.; Yu, K.S. Pharmacokinetics and pharmacodynamics of LC15-0444, a novel dipeptidyl peptidase IV inhibitors, after multiple dosing in healthy volunteers. Br. J. Clin. Pharmacol., 2009, 68(6), 883-890.
[33]
Yang, S.J.; Min, K.W.; Gupta, S.K.; Park, J.Y.; Shivane, V.K.; Pitale, S.U.; Agarwal, P.K.; Sosale, A.; Gandhi, P.; Dharmalingam, M.; Mohan, V.; Makesh, U.; Kim, D.M.; Kim, J.A.; Kim, P.K.; Baik, S.H. A multicentre, multinational, randomized, placebo-controlled, doubleblind, phase 3 trial to evaluate the efficacy and safety of gemigliptin (LC15-0444) in patients with type 2 diabetes. Diabetes Obes. Metab., 2013, 15(5), 410-416.
[34]
Kim, M.K.; Chae, Y.N.; Kim, H.D.; Yang, E.K.; Cho, E.J.; Choi, S.H.; Cheong, Y.H.; Kim, H.S.; Kim, H.J.; Jo, Y.W.; Son, M.H.; Kim, S.H.; Shin, C.Y. DA-1229, a novel and potent DPP4 inhibitor, improves insulin resistance and delays the onset of diabetes. Life Sci., 2012, 90, 21-29.
[36]
Miyamoto, Y.; Banno, Y.; Yamashita, T.; Fujimoto, T.; Oi, S.; Moritoh, Y.; Asakawa, T.; Kataoka, O.; Takeuchi, K.; Suzuki, N.; Ikedo, K.; Kosaka, T.; Tsubotani, S.; Tani, A.; Sasaki, M.; Funami, M.; Amano, M.; Yamamoto, Y.; Aertgeerts, K.; Yano, J. A.H. Discovery of a 3-pyridylacetamide derivative (TAK-100) as a potent, selective and orally active dipeptidyl peptidase IV (DPP-IV) inhibitor. J. Med. Chem., 2011, 54(3), 831-850.
[37]
Gwaltney, S.L. Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase IV. Curr. Top. Med. Chem., 2008, 8(17), 1545-1552.
[38]
M, Pal. Havale, S.H. Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes. Bioorg. Med. Chem., 2009, 17(5), 1783-1802.
[39]
Liu, Y.; Hu, Y.; Liu, T. Recent advances in non-peptidomimetic dipeptidyl peptidase 4 inhibitors: medicinal chemistry and preclinical aspects. Curr. Med. Chem., 2012, 19(23), 3982-3999.
[40]
Brandt, L.; Joossens, J.; Chen, X.; Maes, M.B.; Scharpe, S.; Lambeir, A.M. Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by vildagliptin ((2S)-[(3-hydroxyadamantan- 1-yl) amino] acetyl-pyrrolidine-2-carbonitrile). Biochem. Pharmacol., 2005, 70(1), 134-143.
[42]
Brock, C.M. DPP-4 Inhibitors: What is their place in therapy? Diabetes, 2010, 35(5), 8-13.
[43]
Xourgia, E.; Papazafiropoulou, A.K.; Karampousli, E.; Melidonis, A. DPP-4 Inhibitors vs. SGLT-2 Inhibitors. J. Ren. Med, 2017, 1(2-7), 1-7.
[44]
Liotta, L.A.; Kohn, E.C. The microenvironment of the tumour-host interface. Nature, 2001, 411, 375-379.
[45]
Vanhoof, G.; Goossens, F.; Meester, De. I.; Hendriks, D.; Scharpe, S. Proline motifs in peptides and their biological processing. FASEB J., 1995, 9(9), 736-744.
[46]
Šedo, A.; Malik, R. Dipeptidyl peptidase IV-like molecules: Homologous proteins or homologous activities? Biochim. Biophy. Acta (BBA)-. Protein Struct. Mol. Enzymol., 2001, 1550(2), 107-116.
[47]
Meester, D.I.; Durinx, C.; Bal, G.; Proost, P.; Struyf, S.; Goossens, F.; Augustyns, K.; Scharpe, S. Natural substrates of dipeptidyl peptidase IV. Adv. Experiment. Med. Biol., 2000, 477, 67-87.
[48]
Lambeir, A.M.; Durinx, C.; Proost, P.; Van Damme, J.; Scharpe, S.; Meester, D.I. Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett., 2001, 507(3), 327-330.
[49]
Mentlein, R. Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regulat. Pept., 1999, 85(1), 9-24.
[50]
Van. Damme, J. Struyf, S.; Wuyts, A.; Van.Coillie, E.; Menten, P.; Schols, D.; Sozzani, S.; Meester, De. I.; Proost, P. The role of CD26/DPP IV in chemokine processing. Chem. Immunol., 1999, 72, 42-56.
[51]
Dang, N.H.; Morimoto, C. CD26: An expanding role in immune regulation and cancer. Histol. Histopathol., 2002, 17(4), 1213-1226.
[52]
Iwata, S.; Morimoto, C. CD26/dipeptidyl peptidase IV in context. The different roles of a multifunctional ectoenzyme in malignant transformation. J. Exper. Med., 1999, 190(3), 301-306.
[53]
Kajiyama, H.; Kikkawa, F.; Suzuki, T.; Shibata, K.; Ino, K.; Mizutani, S. Prolonged survival and decreased invasive activity attributable to dipeptidyl peptidase IV overexpression in ovarian carcinoma. Cancer Res., 2002, 62, 2753-2757.
[54]
Fiore, M.; de Filippo, S.; Pozzi, N.; Tamasi, S.; Pignata, C. Occupancy of dipeptidyl peptidase IV activates an associated tyrosine kinase and triggers an apoptotic signal in human hepatocarcinoma cells. Hepatology, 1998, 27(4), 934-942.
[55]
Ho, L.; Aytac, U.; Stephens, L.C.; Ohnuma, K.; Mills, G.B.; McKee, K.S.; Neumann, C.; LaPushin, R.; Cabanillas, F.; Abbruzzese, J.L.; Morimoto, C.; Dang, N.H. In vitro and in vivo antitumor effect of the anti-CD26 monoclonal antibody 1F7 on human CD30+ anaplastic large cell T-cell lymphoma Karpas 299. Clin. Cancer Res., 2001, 7(7), 2031-2040.
[56]
Gonzalez-Gronow, M.; Grenett, H.E.; Weber, M.R.; Gawdi, G.; Pizzo, S.V. Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells. Biochem. J., 2001, 355(Pt 2), 397-407.
[57]
Ohnuma, K.; Munakata, Y.; Ishii, T.; Iwata, S.; Kobayashi, S.; Hosono, O.; Kawasaki, H.; Dang, N.H.; Morimoto, C. Soluble CD26/dipeptidyl peptidase IV induces T-cell proliferation through CD86 up-regulation on APCs. J. Immunol., 2001, 167(12), 6745-6755.
[58]
Scanlan, M.J.; Raj, B.K.; Calvo, B.; Garin-Chesa, P.; Sanz-Moncasi, M.P.; Healey, J.H.; Old, L.J.; Rettig, W.J. Molecular cloning of fibroblast activation protein. a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers. Proc. Nat. Acad. Sci. USA, 1994, 91(12), 5657-5661.
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