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Volumn 226, Issue 2, 2013, Pages 305-314

An emerging role of dipeptidyl peptidase 4 (DPP4) beyond glucose control: Potential implications in cardiovascular disease

Author keywords

Atherosclerosis; CD26; DPP4; Inflammation; Type 2 diabetes

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; INCRETIN; LINAGLIPTIN; METFORMIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA AGONIST; PIOGLITAZONE; SAXAGLIPTIN; SITAGLIPTIN; SULFONYLUREA DERIVATIVE; VILDAGLIPTIN;

EID: 84872424922     PISSN: 00219150     EISSN: 18791484     Source Type: Journal    
DOI: 10.1016/j.atherosclerosis.2012.09.012     Document Type: Review
Times cited : (184)

References (104)
  • 1
    • 0033780088 scopus 로고    scopus 로고
    • Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
    • Abbott C.A., Yu D.M., Woollatt E., Sutherland G.R., McCaughan G.W., Gorrell M.D. Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8. Eur J Biochem 2000, 267:6140-6150.
    • (2000) Eur J Biochem , vol.267 , pp. 6140-6150
    • Abbott, C.A.1    Yu, D.M.2    Woollatt, E.3    Sutherland, G.R.4    McCaughan, G.W.5    Gorrell, M.D.6
  • 2
    • 70350328161 scopus 로고    scopus 로고
    • Dipeptidyl peptidase inhibitors, an emerging drug class for inflammatory disease?
    • Yazbeck R., Howarth G.S., Abbott C.A. Dipeptidyl peptidase inhibitors, an emerging drug class for inflammatory disease?. Trends Pharmacol Sci 2009, 30:600-607.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 600-607
    • Yazbeck, R.1    Howarth, G.S.2    Abbott, C.A.3
  • 3
    • 0025349737 scopus 로고
    • Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence
    • McCaughan G.W., Wickson J.E., Creswick P.F., Gorrell M.D. Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence. Hepatology 1990, 11:534-544.
    • (1990) Hepatology , vol.11 , pp. 534-544
    • McCaughan, G.W.1    Wickson, J.E.2    Creswick, P.F.3    Gorrell, M.D.4
  • 4
    • 0031657655 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence
    • Iwaki-Egawa S., Watanabe Y., Kikuya Y., Fujimoto Y. Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence. J Biochem 1998, 124:428-433.
    • (1998) J Biochem , vol.124 , pp. 428-433
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Kikuya, Y.3    Fujimoto, Y.4
  • 5
    • 0034613689 scopus 로고    scopus 로고
    • The binding site of human adenosine deaminase for CD26/dipeptidyl peptidase IV: the Arg142Gln mutation impairs binding to cd26 but does not cause immune deficiency
    • Richard E., Arredondo-Vega F.X., Santisteban I., Kelly S.J., Patel D.D., Hershfield M.S. The binding site of human adenosine deaminase for CD26/dipeptidyl peptidase IV: the Arg142Gln mutation impairs binding to cd26 but does not cause immune deficiency. J Exp Med 2000, 192:1223-1236.
    • (2000) J Exp Med , vol.192 , pp. 1223-1236
    • Richard, E.1    Arredondo-Vega, F.X.2    Santisteban, I.3    Kelly, S.J.4    Patel, D.D.5    Hershfield, M.S.6
  • 6
    • 1642534610 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation
    • Aertgeerts K., Ye S., Tennant M.G., 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, 13:412-421.
    • (2004) Protein Sci , vol.13 , pp. 412-421
    • Aertgeerts, K.1    Ye, S.2    Tennant, M.G.3
  • 7
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat Struct Biol 2003, 10:19-25.
    • (2003) Nat Struct Biol , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 8
    • 0031573556 scopus 로고    scopus 로고
    • Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation
    • Dong R.P., Tachibana K., Hegen M., et al. Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation. J Immunol 1997, 159:6070-6076.
    • (1997) J Immunol , vol.159 , pp. 6070-6076
    • Dong, R.P.1    Tachibana, K.2    Hegen, M.3
  • 9
    • 0000038304 scopus 로고    scopus 로고
    • Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted beta propeller domain
    • Abbott C.A., McCaughan G.W., Levy M.T., Church W.B., Gorrell M.D. Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted beta propeller domain. Eur J Biochem 1999, 266:798-810.
    • (1999) Eur J Biochem , vol.266 , pp. 798-810
    • Abbott, C.A.1    McCaughan, G.W.2    Levy, M.T.3    Church, W.B.4    Gorrell, M.D.5
  • 10
    • 17144404555 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
    • Gorrell M.D. Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clin Sci (Lond) 2005, 108:277-292.
    • (2005) Clin Sci (Lond) , vol.108 , pp. 277-292
    • Gorrell, M.D.1
  • 12
    • 0028090611 scopus 로고
    • Expression and functional role of dipeptidyl peptidase IV (CD26) on human natural killer cells
    • Buhling F., Kunz D., Reinhold D., et al. Expression and functional role of dipeptidyl peptidase IV (CD26) on human natural killer cells. Nat Immun 1994, 13:270-279.
    • (1994) Nat Immun , vol.13 , pp. 270-279
    • Buhling, F.1    Kunz, D.2    Reinhold, D.3
  • 13
    • 0025318818 scopus 로고
    • The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity
    • Hegen M., Niedobitek G., Klein C.E., Stein H., Fleischer B. The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity. J Immunol 1990, 144:2908-2914.
    • (1990) J Immunol , vol.144 , pp. 2908-2914
    • Hegen, M.1    Niedobitek, G.2    Klein, C.E.3    Stein, H.4    Fleischer, B.5
  • 14
    • 0036081143 scopus 로고    scopus 로고
    • GLP-1-(9-36) amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion
    • Deacon C.F., Plamboeck A., Moller S., Holst J.J. GLP-1-(9-36) amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion. Am J Physiol Endocrinol Metab 2002, 282:E873-E879.
    • (2002) Am J Physiol Endocrinol Metab , vol.282
    • Deacon, C.F.1    Plamboeck, A.2    Moller, S.3    Holst, J.J.4
  • 15
    • 2942755813 scopus 로고    scopus 로고
    • The major glucagon-like peptide-1 metabolite, GLP-1-(9-36)-amide, does not affect glucose or insulin levels in mice
    • Rolin B., Deacon C.F., Carr R.D., Ahren B. The major glucagon-like peptide-1 metabolite, GLP-1-(9-36)-amide, does not affect glucose or insulin levels in mice. Eur J Pharmacol 2004, 494:283-288.
    • (2004) Eur J Pharmacol , vol.494 , pp. 283-288
    • Rolin, B.1    Deacon, C.F.2    Carr, R.D.3    Ahren, B.4
  • 16
    • 33751055819 scopus 로고    scopus 로고
    • Effects of sub-chronic exposure to naturally occurring N-terminally truncated metabolites of glucose-dependent insulinotrophic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1), GIP(3-42) and GLP-1(9-36)amide, on insulin secretion and glucose homeostasis in ob/ob mice
    • Parker J.C., Lavery K.S., Irwin N., et al. Effects of sub-chronic exposure to naturally occurring N-terminally truncated metabolites of glucose-dependent insulinotrophic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1), GIP(3-42) and GLP-1(9-36)amide, on insulin secretion and glucose homeostasis in ob/ob mice. J Endocrinol 2006, 191:93-100.
    • (2006) J Endocrinol , vol.191 , pp. 93-100
    • Parker, J.C.1    Lavery, K.S.2    Irwin, N.3
  • 17
    • 75949085811 scopus 로고    scopus 로고
    • C38, equivalent to BM88, is developmentally expressed in maturing retinal neurons and enhances neuronal maturation
    • Wakabayashi T., Kosaka J., Mochii M., et al. C38, equivalent to BM88, is developmentally expressed in maturing retinal neurons and enhances neuronal maturation. J Neurochem 2010, 112:1235-1248.
    • (2010) J Neurochem , vol.112 , pp. 1235-1248
    • Wakabayashi, T.1    Kosaka, J.2    Mochii, M.3
  • 19
    • 1442321740 scopus 로고    scopus 로고
    • Evidence that the major degradation product of glucose-dependent insulinotropic polypeptide, GIP(3-42), is a GIP receptor antagonist in vivo
    • Gault V.A., Parker J.C., Harriott P., Flatt P.R., O'Harte F.P. Evidence that the major degradation product of glucose-dependent insulinotropic polypeptide, GIP(3-42), is a GIP receptor antagonist in vivo. J Endocrinol 2002, 175:525-533.
    • (2002) J Endocrinol , vol.175 , pp. 525-533
    • Gault, V.A.1    Parker, J.C.2    Harriott, P.3    Flatt, P.R.4    O'Harte, F.P.5
  • 20
    • 0031919929 scopus 로고    scopus 로고
    • XVI. International Union of Pharmacology recommendations for the nomenclature of neuropeptide Y, peptide YY, and pancreatic polypeptide receptors
    • Michel M.C., Beck-Sickinger A., Cox H., et al. XVI. International Union of Pharmacology recommendations for the nomenclature of neuropeptide Y, peptide YY, and pancreatic polypeptide receptors. Pharmacol Rev 1998, 50:143-150.
    • (1998) Pharmacol Rev , vol.50 , pp. 143-150
    • Michel, M.C.1    Beck-Sickinger, A.2    Cox, H.3
  • 21
    • 0032566801 scopus 로고    scopus 로고
    • Characterisation of the neuropeptide Y receptor that mediates feeding in the rat: a role for the Y5 receptor?
    • Haynes A.C., Arch J.R., Wilson S., McClue S., Buckingham R.E. Characterisation of the neuropeptide Y receptor that mediates feeding in the rat: a role for the Y5 receptor?. Regul Pept 1998, 75-76:355-361.
    • (1998) Regul Pept , vol.75-76 , pp. 355-361
    • Haynes, A.C.1    Arch, J.R.2    Wilson, S.3    McClue, S.4    Buckingham, R.E.5
  • 22
    • 0032861562 scopus 로고    scopus 로고
    • Normal feeding behavior, body weight and leptin response require the neuropeptide Y Y2 receptor
    • Naveilhan P., Hassani H., Canals J.M., et al. Normal feeding behavior, body weight and leptin response require the neuropeptide Y Y2 receptor. Nat Med 1999, 5:1188-1193.
    • (1999) Nat Med , vol.5 , pp. 1188-1193
    • Naveilhan, P.1    Hassani, H.2    Canals, J.M.3
  • 23
    • 61549105354 scopus 로고    scopus 로고
    • DPP-IV inhibition enhances the antilipolytic action of NPY in human adipose tissue
    • Kos K., Baker A.R., Jernas M., et al. DPP-IV inhibition enhances the antilipolytic action of NPY in human adipose tissue. Diabetes Obes Metab 2009, 11:285-292.
    • (2009) Diabetes Obes Metab , vol.11 , pp. 285-292
    • Kos, K.1    Baker, A.R.2    Jernas, M.3
  • 24
    • 77958195997 scopus 로고    scopus 로고
    • The oral dipeptidyl peptidase-4 inhibitor sitagliptin increases circulating endothelial progenitor cells in patients with type 2 diabetes: possible role of stromal-derived factor-1alpha
    • Fadini G.P., Boscaro E., Albiero M., et al. The oral dipeptidyl peptidase-4 inhibitor sitagliptin increases circulating endothelial progenitor cells in patients with type 2 diabetes: possible role of stromal-derived factor-1alpha. Diabetes Care 2010, 33:1607-1609.
    • (2010) Diabetes Care , vol.33 , pp. 1607-1609
    • Fadini, G.P.1    Boscaro, E.2    Albiero, M.3
  • 25
    • 0027401263 scopus 로고
    • A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase
    • Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P., Houghton A.N. A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J Exp Med 1993, 177:1135-1143.
    • (1993) J Exp Med , vol.177 , pp. 1135-1143
    • Morrison, M.E.1    Vijayasaradhi, S.2    Engelstein, D.3    Albino, A.P.4    Houghton, A.N.5
  • 26
    • 4644325083 scopus 로고    scopus 로고
    • CD26 up-regulates expression of CD86 on antigen-presenting cells by means of caveolin-1
    • Ohnuma K., Yamochi T., Uchiyama M., et al. CD26 up-regulates expression of CD86 on antigen-presenting cells by means of caveolin-1. Proc Natl Acad Sci U S A 2004, 101:14186-14191.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14186-14191
    • Ohnuma, K.1    Yamochi, T.2    Uchiyama, M.3
  • 27
    • 0035824614 scopus 로고    scopus 로고
    • Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule
    • Girardi A.C., Degray B.C., Nagy T., Biemesderfer D., Aronson P.S. Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule. J Biol Chem 2001, 276:46671-46677.
    • (2001) J Biol Chem , vol.276 , pp. 46671-46677
    • Girardi, A.C.1    Degray, B.C.2    Nagy, T.3    Biemesderfer, D.4    Aronson, P.S.5
  • 28
    • 17644400568 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26)
    • Weihofen W.A., Liu J., Reutter W., Saenger W., Fan H. Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26). J Biol Chem 2005, 280:14911-14917.
    • (2005) J Biol Chem , vol.280 , pp. 14911-14917
    • Weihofen, W.A.1    Liu, J.2    Reutter, W.3    Saenger, W.4    Fan, H.5
  • 29
    • 0043092068 scopus 로고    scopus 로고
    • A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis
    • Cheng H.C., Abdel-Ghany M., Pauli B.U. A novel consensus motif in fibronectin mediates dipeptidyl peptidase IV adhesion and metastasis. J Biol Chem 2003, 278:24600-24607.
    • (2003) J Biol Chem , vol.278 , pp. 24600-24607
    • Cheng, H.C.1    Abdel-Ghany, M.2    Pauli, B.U.3
  • 30
    • 0024331402 scopus 로고
    • 1F7, a novel cell surface molecule, involved in helper function of CD4 cells
    • Morimoto C., Torimoto Y., Levinson G., et al. 1F7, a novel cell surface molecule, involved in helper function of CD4 cells. J Immunol 1989, 143:3430-3439.
    • (1989) J Immunol , vol.143 , pp. 3430-3439
    • Morimoto, C.1    Torimoto, Y.2    Levinson, G.3
  • 31
    • 0028790702 scopus 로고
    • Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule
    • Martin M., Huguet J., Centelles J.J., Franco R. Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule. J Immunol 1995, 155:4630-4643.
    • (1995) J Immunol , vol.155 , pp. 4630-4643
    • Martin, M.1    Huguet, J.2    Centelles, J.J.3    Franco, R.4
  • 32
    • 0027270023 scopus 로고
    • The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity
    • Tanaka T., Kameoka J., Yaron A., Schlossman S.F., Morimoto C. The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. Proc Natl Acad Sci U S A 1993, 90:4586-4590.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 4586-4590
    • Tanaka, T.1    Kameoka, J.2    Yaron, A.3    Schlossman, S.F.4    Morimoto, C.5
  • 33
    • 8044233036 scopus 로고    scopus 로고
    • Cross-linking of CD26 by antibody induces tyrosine phosphorylation and activation of mitogen-activated protein kinase
    • Hegen M., Kameoka J., Dong R.P., Schlossman S.F., Morimoto C. Cross-linking of CD26 by antibody induces tyrosine phosphorylation and activation of mitogen-activated protein kinase. Immunology 1997, 90:257-264.
    • (1997) Immunology , vol.90 , pp. 257-264
    • Hegen, M.1    Kameoka, J.2    Dong, R.P.3    Schlossman, S.F.4    Morimoto, C.5
  • 34
    • 0025992545 scopus 로고
    • Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes
    • Torimoto Y., Dang N.H., Vivier E., Tanaka T., Schlossman S.F., Morimoto C. Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. J Immunol 1991, 147:2514-2517.
    • (1991) J Immunol , vol.147 , pp. 2514-2517
    • Torimoto, Y.1    Dang, N.H.2    Vivier, E.3    Tanaka, T.4    Schlossman, S.F.5    Morimoto, C.6
  • 35
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T-cell immune response
    • Morimoto C., Schlossman S.F. The structure and function of CD26 in the T-cell immune response. Immunol Rev 1998, 161:55-70.
    • (1998) Immunol Rev , vol.161 , pp. 55-70
    • Morimoto, C.1    Schlossman, S.F.2
  • 36
    • 78650799604 scopus 로고    scopus 로고
    • Soluble CD26/dipeptidyl peptidase IV enhances human lymphocyte proliferation in vitro independent of dipeptidyl peptidase enzyme activity and adenosine deaminase binding
    • Yu D.M., Slaitini L., Gysbers V., et al. Soluble CD26/dipeptidyl peptidase IV enhances human lymphocyte proliferation in vitro independent of dipeptidyl peptidase enzyme activity and adenosine deaminase binding. Scand J Immunol 2011, 73:102-111.
    • (2011) Scand J Immunol , vol.73 , pp. 102-111
    • Yu, D.M.1    Slaitini, L.2    Gysbers, V.3
  • 37
    • 0035892903 scopus 로고    scopus 로고
    • Soluble CD26/dipeptidyl peptidase IV induces T cell proliferation through CD86 up-regulation on APCs
    • Ohnuma K., Munakata Y., Ishii T., et al. Soluble CD26/dipeptidyl peptidase IV induces T cell proliferation through CD86 up-regulation on APCs. J Immunol 2001, 167:6745-6755.
    • (2001) J Immunol , vol.167 , pp. 6745-6755
    • Ohnuma, K.1    Munakata, Y.2    Ishii, T.3
  • 38
    • 33644521705 scopus 로고    scopus 로고
    • T-cell activation via CD26 and caveolin-1 in rheumatoid synovium
    • Ohnuma K., Inoue H., Uchiyama M., et al. T-cell activation via CD26 and caveolin-1 in rheumatoid synovium. Mod Rheumatol 2006, 16:3-13.
    • (2006) Mod Rheumatol , vol.16 , pp. 3-13
    • Ohnuma, K.1    Inoue, H.2    Uchiyama, M.3
  • 39
    • 0037373183 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXXV. The glucagon receptor family
    • Mayo K.E., Miller L.J., Bataille D., et al. International Union of Pharmacology. XXXV. The glucagon receptor family. Pharmacol Rev 2003, 55:167-194.
    • (2003) Pharmacol Rev , vol.55 , pp. 167-194
    • Mayo, K.E.1    Miller, L.J.2    Bataille, D.3
  • 40
    • 0026775150 scopus 로고
    • Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1
    • Thorens B. Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1. Proc Natl Acad Sci U S A 1992, 89:8641-8645.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8641-8645
    • Thorens, B.1
  • 41
    • 67651173077 scopus 로고    scopus 로고
    • Incretin-based therapies for type 2 diabetes mellitus
    • Lovshin J.A., Drucker D.J. Incretin-based therapies for type 2 diabetes mellitus. Nat Rev Endocrinol 2009, 5:262-269.
    • (2009) Nat Rev Endocrinol , vol.5 , pp. 262-269
    • Lovshin, J.A.1    Drucker, D.J.2
  • 42
    • 80052766495 scopus 로고    scopus 로고
    • Activation of the GLP-1 receptor signalling pathway: a relevant strategy to repair a deficient beta-cell mass
    • Portha B., Tourrel-Cuzin C., Movassat J. Activation of the GLP-1 receptor signalling pathway: a relevant strategy to repair a deficient beta-cell mass. Exp Diabetes Res 2011, 2011:376509.
    • (2011) Exp Diabetes Res , vol.2011 , pp. 376509
    • Portha, B.1    Tourrel-Cuzin, C.2    Movassat, J.3
  • 43
    • 0023683906 scopus 로고
    • Triggering of cytotoxic T lymphocytes and NK cells via the Tp103 pathway is dependent on the expression of the T cell receptor/CD3 complex
    • Fleischer B., Sturm E., De Vries J.E., Spits H. Triggering of cytotoxic T lymphocytes and NK cells via the Tp103 pathway is dependent on the expression of the T cell receptor/CD3 complex. J Immunol 1988, 141:1103-1107.
    • (1988) J Immunol , vol.141 , pp. 1103-1107
    • Fleischer, B.1    Sturm, E.2    De Vries, J.E.3    Spits, H.4
  • 44
    • 0028952382 scopus 로고
    • The cytoplasmic tail of the T cell receptor zeta chain is required for signaling via CD26
    • Mittrucker H.W., Steeg C., Malissen B., Fleischer B. The cytoplasmic tail of the T cell receptor zeta chain is required for signaling via CD26. Eur J Immunol 1995, 25:295-297.
    • (1995) Eur J Immunol , vol.25 , pp. 295-297
    • Mittrucker, H.W.1    Steeg, C.2    Malissen, B.3    Fleischer, B.4
  • 45
    • 0026633296 scopus 로고
    • Cloning and functional expression of the T cell activation antigen CD26
    • Tanaka T., Camerini D., Seed B., et al. Cloning and functional expression of the T cell activation antigen CD26. J Immunol 1992, 149:481-486.
    • (1992) J Immunol , vol.149 , pp. 481-486
    • Tanaka, T.1    Camerini, D.2    Seed, B.3
  • 46
    • 62749133510 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition with MK0431 improves islet graft survival in diabetic NOD mice partially via T-cell modulation
    • Kim S.J., Nian C., Doudet D.J., McIntosh C.H. Dipeptidyl peptidase IV inhibition with MK0431 improves islet graft survival in diabetic NOD mice partially via T-cell modulation. Diabetes 2009, 58:641-651.
    • (2009) Diabetes , vol.58 , pp. 641-651
    • Kim, S.J.1    Nian, C.2    Doudet, D.J.3    McIntosh, C.H.4
  • 47
    • 77954253597 scopus 로고    scopus 로고
    • Sitagliptin (MK0431) inhibition of dipeptidyl peptidase IV decreases nonobese diabetic mouse CD4+ T-cell migration through incretin-dependent and -independent pathways
    • Kim S.J., Nian C., McIntosh C.H. Sitagliptin (MK0431) inhibition of dipeptidyl peptidase IV decreases nonobese diabetic mouse CD4+ T-cell migration through incretin-dependent and -independent pathways. Diabetes 2010, 59:1739-1750.
    • (2010) Diabetes , vol.59 , pp. 1739-1750
    • Kim, S.J.1    Nian, C.2    McIntosh, C.H.3
  • 48
    • 77956976665 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase 4 and attractin expression is increased in circulating blood monocytes of obese human subjects
    • Laudes M., Oberhauser F., Schulte D.M., et al. Dipeptidyl-peptidase 4 and attractin expression is increased in circulating blood monocytes of obese human subjects. Exp Clin Endocrinol Diabetes 2010, 118:473-477.
    • (2010) Exp Clin Endocrinol Diabetes , vol.118 , pp. 473-477
    • Laudes, M.1    Oberhauser, F.2    Schulte, D.M.3
  • 50
    • 23844517430 scopus 로고    scopus 로고
    • CD26 mediates dissociation of Tollip and IRAK-1 from caveolin-1 and induces upregulation of CD86 on antigen-presenting cells
    • Ohnuma K., Yamochi T., Uchiyama M., et al. CD26 mediates dissociation of Tollip and IRAK-1 from caveolin-1 and induces upregulation of CD86 on antigen-presenting cells. Mol Cell Biol 2005, 25:7743-7757.
    • (2005) Mol Cell Biol , vol.25 , pp. 7743-7757
    • Ohnuma, K.1    Yamochi, T.2    Uchiyama, M.3
  • 51
    • 78649730402 scopus 로고    scopus 로고
    • DPP-4 (CD26) inhibitor alogliptin inhibits TLR4-mediated ERK activation and ERK-dependent MMP-1 expression by U937 histiocytes
    • Ta N.N., Li Y., Schuyler C.A., Lopes-Virella M.F., Huang Y. DPP-4 (CD26) inhibitor alogliptin inhibits TLR4-mediated ERK activation and ERK-dependent MMP-1 expression by U937 histiocytes. Atherosclerosis 2010, 213:429-435.
    • (2010) Atherosclerosis , vol.213 , pp. 429-435
    • Ta, N.N.1    Li, Y.2    Schuyler, C.A.3    Lopes-Virella, M.F.4    Huang, Y.5
  • 52
    • 81855222104 scopus 로고    scopus 로고
    • Long-term dipeptidyl-peptidase 4 inhibition reduces atherosclerosis and inflammation via effects on monocyte recruitment and chemotaxis
    • Shah Z., Kampfrath T., Deiuliis J.A., et al. Long-term dipeptidyl-peptidase 4 inhibition reduces atherosclerosis and inflammation via effects on monocyte recruitment and chemotaxis. Circulation 2011, 124:2338-2349.
    • (2011) Circulation , vol.124 , pp. 2338-2349
    • Shah, Z.1    Kampfrath, T.2    Deiuliis, J.A.3
  • 53
    • 67650223772 scopus 로고    scopus 로고
    • GLP-1 therapy: beyond glucose control
    • Hausenloy D.J., Yellon D.M. GLP-1 therapy: beyond glucose control. Circ Heart Fail 2008, 1:147-149.
    • (2008) Circ Heart Fail , vol.1 , pp. 147-149
    • Hausenloy, D.J.1    Yellon, D.M.2
  • 54
    • 77951934948 scopus 로고    scopus 로고
    • DPP-4 inhibition by sitagliptin improves the myocardial response to dobutamine stress and mitigates stunning in a pilot study of patients with coronary artery disease
    • Read P.A., Khan F.Z., Heck P.M., Hoole S.P., Dutka D.P. DPP-4 inhibition by sitagliptin improves the myocardial response to dobutamine stress and mitigates stunning in a pilot study of patients with coronary artery disease. Circ Cardiovasc Imaging 2010, 3:195-201.
    • (2010) Circ Cardiovasc Imaging , vol.3 , pp. 195-201
    • Read, P.A.1    Khan, F.Z.2    Heck, P.M.3    Hoole, S.P.4    Dutka, D.P.5
  • 55
    • 77951168113 scopus 로고    scopus 로고
    • Genetic deletion or pharmacological inhibition of dipeptidyl peptidase-4 improves cardiovascular outcomes after myocardial infarction in mice
    • Sauve M., Ban K., Momen M.A., et al. Genetic deletion or pharmacological inhibition of dipeptidyl peptidase-4 improves cardiovascular outcomes after myocardial infarction in mice. Diabetes 2010, 59:1063-1073.
    • (2010) Diabetes , vol.59 , pp. 1063-1073
    • Sauve, M.1    Ban, K.2    Momen, M.A.3
  • 56
    • 78249259703 scopus 로고    scopus 로고
    • Genetically manipulated progenitor cell sheet with diprotin A improves myocardial function and repair of infarcted hearts
    • Zhang D., Huang W., Dai B., et al. Genetically manipulated progenitor cell sheet with diprotin A improves myocardial function and repair of infarcted hearts. Am J Physiol Heart Circ Physiol 2010, 299:H1339-H1347.
    • (2010) Am J Physiol Heart Circ Physiol , vol.299
    • Zhang, D.1    Huang, W.2    Dai, B.3
  • 57
    • 0028307434 scopus 로고
    • Inflammatory heart disease: pathogenesis, clinical manifestations, and treatment of myocarditis
    • Olinde K.D., O'Connell J.B. Inflammatory heart disease: pathogenesis, clinical manifestations, and treatment of myocarditis. Annu Rev Med 1994, 45:481-490.
    • (1994) Annu Rev Med , vol.45 , pp. 481-490
    • Olinde, K.D.1    O'Connell, J.B.2
  • 60
    • 85027951331 scopus 로고    scopus 로고
    • Adaptive immunity in atherosclerosis: mechanisms and future therapeutic targets
    • Lahoute C., Herbin O., Mallat Z., Tedgui A. Adaptive immunity in atherosclerosis: mechanisms and future therapeutic targets. Nat Rev Cardiol 2011, 8:348-358.
    • (2011) Nat Rev Cardiol , vol.8 , pp. 348-358
    • Lahoute, C.1    Herbin, O.2    Mallat, Z.3    Tedgui, A.4
  • 62
    • 79955604190 scopus 로고    scopus 로고
    • Anti-inflammatory therapeutics for the treatment of atherosclerosis
    • Charo I.F., Taub R. Anti-inflammatory therapeutics for the treatment of atherosclerosis. Nat Rev Drug Discov 2011, 10:365-376.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 365-376
    • Charo, I.F.1    Taub, R.2
  • 63
    • 0030744259 scopus 로고    scopus 로고
    • Inhibitors of dipeptidyl peptidase IV induce secretion of transforming growth factor-beta 1 in PWM-stimulated PBMC and T cells
    • Reinhold D., Bank U., Buhling F., et al. Inhibitors of dipeptidyl peptidase IV induce secretion of transforming growth factor-beta 1 in PWM-stimulated PBMC and T cells. Immunology 1997, 91:354-360.
    • (1997) Immunology , vol.91 , pp. 354-360
    • Reinhold, D.1    Bank, U.2    Buhling, F.3
  • 64
    • 0023632161 scopus 로고
    • The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesis in vitro
    • Schon E., Jahn S., Kiessig S.T., et al. The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesis in vitro. Eur J Immunol 1987, 17:1821-1826.
    • (1987) Eur J Immunol , vol.17 , pp. 1821-1826
    • Schon, E.1    Jahn, S.2    Kiessig, S.T.3
  • 65
    • 0027162195 scopus 로고
    • Dipeptidyl peptidase IV (CD26) on human lymphocytes. Synthetic inhibitors of and antibodies against dipeptidyl peptidase IV suppress the proliferation of pokeweed mitogen-stimulated peripheral blood mononuclear cells, and IL-2 and IL-6 production
    • Reinhold D., Bank U., Buhling F., et al. Dipeptidyl peptidase IV (CD26) on human lymphocytes. Synthetic inhibitors of and antibodies against dipeptidyl peptidase IV suppress the proliferation of pokeweed mitogen-stimulated peripheral blood mononuclear cells, and IL-2 and IL-6 production. Immunobiology 1993, 188:403-414.
    • (1993) Immunobiology , vol.188 , pp. 403-414
    • Reinhold, D.1    Bank, U.2    Buhling, F.3
  • 66
    • 0030952018 scopus 로고    scopus 로고
    • Inhibitors of dipeptidyl peptidase IV (DP IV, CD26) induces secretion of transforming growth factor-beta 1 (TGF-beta 1) in stimulated mouse splenocytes and thymocytes
    • Reinhold D., Bank U., Buhling F., et al. Inhibitors of dipeptidyl peptidase IV (DP IV, CD26) induces secretion of transforming growth factor-beta 1 (TGF-beta 1) in stimulated mouse splenocytes and thymocytes. Immunol Lett 1997, 58:29-35.
    • (1997) Immunol Lett , vol.58 , pp. 29-35
    • Reinhold, D.1    Bank, U.2    Buhling, F.3
  • 67
    • 0033159183 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV: a cell surface peptidase involved in regulating T cell growth (review)
    • Kahne T., Lendeckel U., Wrenger S., Neubert K., Ansorge S., Reinhold D. Dipeptidyl peptidase IV: a cell surface peptidase involved in regulating T cell growth (review). Int J Mol Med 1999, 4:3-15.
    • (1999) Int J Mol Med , vol.4 , pp. 3-15
    • Kahne, T.1    Lendeckel, U.2    Wrenger, S.3    Neubert, K.4    Ansorge, S.5    Reinhold, D.6
  • 68
    • 0036659179 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine
    • Ludwig A., Schiemann F., Mentlein R., Lindner B., Brandt E. Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine. J Leukoc Biol 2002, 72:183-191.
    • (2002) J Leukoc Biol , vol.72 , pp. 183-191
    • Ludwig, A.1    Schiemann, F.2    Mentlein, R.3    Lindner, B.4    Brandt, E.5
  • 69
    • 13144283654 scopus 로고    scopus 로고
    • Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1alpha (SDF-1alpha) and SDF-1beta are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage
    • Shioda T., Kato H., Ohnishi Y., et al. Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1alpha (SDF-1alpha) and SDF-1beta are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage. Proc Natl Acad Sci U S A 1998, 95:6331-6336.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6331-6336
    • Shioda, T.1    Kato, H.2    Ohnishi, Y.3
  • 70
    • 0032530062 scopus 로고    scopus 로고
    • 2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor
    • 2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor. J Immunol 1998, 161:2672-2675.
    • (1998) J Immunol , vol.161 , pp. 2672-2675
    • Struyf, S.1    Proost, P.2    Sozzani, S.3
  • 71
    • 0033548086 scopus 로고    scopus 로고
    • Truncation of macrophage-derived chemokine by CD26/dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction
    • Proost P., Struyf S., Schols D., 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, 274:3988-3993.
    • (1999) J Biol Chem , vol.274 , pp. 3988-3993
    • Proost, P.1    Struyf, S.2    Schols, D.3
  • 72
    • 0033561659 scopus 로고    scopus 로고
    • 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
    • Struyf S., Proost P., Schols D., et al. 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, 162:4903-4909.
    • (1999) J Immunol , vol.162 , pp. 4903-4909
    • Struyf, S.1    Proost, P.2    Schols, D.3
  • 73
    • 0032992914 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: possible mechanism for the switch from innate to acquired immune response
    • Iwata S., Yamaguchi N., Munakata Y., et al. CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: possible mechanism for the switch from innate to acquired immune response. Int Immunol 1999, 11:417-426.
    • (1999) Int Immunol , vol.11 , pp. 417-426
    • Iwata, S.1    Yamaguchi, N.2    Munakata, Y.3
  • 74
    • 84866356839 scopus 로고    scopus 로고
    • Sitagliptin reduces plaque macrophage content and stabilises arteriosclerotic lesions in Apoe (-/-) mice
    • Vittone F., Liberman A., Vasic D., et al. Sitagliptin reduces plaque macrophage content and stabilises arteriosclerotic lesions in Apoe (-/-) mice. Diabetologia 2012, 55:2267-2275.
    • (2012) Diabetologia , vol.55 , pp. 2267-2275
    • Vittone, F.1    Liberman, A.2    Vasic, D.3
  • 75
    • 43249089631 scopus 로고    scopus 로고
    • Cardioprotective and vasodilatory actions of glucagon-like peptide 1 receptor are mediated through both glucagon-like peptide 1 receptor-dependent and -independent pathways
    • Ban K., Noyan-Ashraf M.H., Hoefer J., Bolz S.S., Drucker D.J., Husain M. Cardioprotective and vasodilatory actions of glucagon-like peptide 1 receptor are mediated through both glucagon-like peptide 1 receptor-dependent and -independent pathways. Circulation 2008, 117:2340-2350.
    • (2008) Circulation , vol.117 , pp. 2340-2350
    • Ban, K.1    Noyan-Ashraf, M.H.2    Hoefer, J.3    Bolz, S.S.4    Drucker, D.J.5    Husain, M.6
  • 76
    • 79953320085 scopus 로고    scopus 로고
    • Expression and spatial heterogeneity of dipeptidyl peptidases in endothelial cells of conduct vessels and capillaries
    • Matheeussen V., Baerts L., De Meyer G., et al. Expression and spatial heterogeneity of dipeptidyl peptidases in endothelial cells of conduct vessels and capillaries. Biol Chem 2011, 392:189-198.
    • (2011) Biol Chem , vol.392 , pp. 189-198
    • Matheeussen, V.1    Baerts, L.2    De Meyer, G.3
  • 77
    • 80051795160 scopus 로고    scopus 로고
    • Cardiovascular effects of DPP-4 inhibition: beyond GLP-1
    • Fadini G.P., Avogaro A. Cardiovascular effects of DPP-4 inhibition: beyond GLP-1. Vascul Pharmacol 2011, 55:10-16.
    • (2011) Vascul Pharmacol , vol.55 , pp. 10-16
    • Fadini, G.P.1    Avogaro, A.2
  • 78
    • 0035892681 scopus 로고    scopus 로고
    • Vasorelaxant effect of glucagon-like peptide-(7-36)amide and amylin on the pulmonary circulation of the rat
    • Golpon H.A., Puechner A., Welte T., Wichert P.V., Feddersen C.O. Vasorelaxant effect of glucagon-like peptide-(7-36)amide and amylin on the pulmonary circulation of the rat. Regul Pept 2001, 102:81-86.
    • (2001) Regul Pept , vol.102 , pp. 81-86
    • Golpon, H.A.1    Puechner, A.2    Welte, T.3    Wichert, P.V.4    Feddersen, C.O.5
  • 79
    • 36148932551 scopus 로고    scopus 로고
    • Beneficial effects of GLP-1 on endothelial function in humans: dampening by glyburide but not by glimepiride
    • Basu A., Charkoudian N., Schrage W., Rizza R.A., Basu R., Joyner M.J. Beneficial effects of GLP-1 on endothelial function in humans: dampening by glyburide but not by glimepiride. Am J Physiol Endocrinol Metab 2007, 293:E1289-E1295.
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Basu, A.1    Charkoudian, N.2    Schrage, W.3    Rizza, R.A.4    Basu, R.5    Joyner, M.J.6
  • 80
    • 9944251347 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 relaxes rat conduit arteries via an endothelium-independent mechanism
    • Nystrom T., Gonon A.T., Sjoholm A., Pernow J. Glucagon-like peptide-1 relaxes rat conduit arteries via an endothelium-independent mechanism. Regul Pept 2005, 125:173-177.
    • (2005) Regul Pept , vol.125 , pp. 173-177
    • Nystrom, T.1    Gonon, A.T.2    Sjoholm, A.3    Pernow, J.4
  • 81
    • 80053204667 scopus 로고    scopus 로고
    • Effect of enhanced glycemic control with saxagliptin on endothelial nitric oxide release and CD40 levels in obese rats
    • Mason R.P., Jacob R.F., Kubant R., et al. Effect of enhanced glycemic control with saxagliptin on endothelial nitric oxide release and CD40 levels in obese rats. J Atheroscler Thromb 2011, 18:774-783.
    • (2011) J Atheroscler Thromb , vol.18 , pp. 774-783
    • Mason, R.P.1    Jacob, R.F.2    Kubant, R.3
  • 82
    • 45849115827 scopus 로고    scopus 로고
    • Sitagliptin augments sympathetic enhancement of the renovascular effects of angiotensin II in genetic hypertension
    • Jackson E.K., Mi Z. Sitagliptin augments sympathetic enhancement of the renovascular effects of angiotensin II in genetic hypertension. Hypertension 2008, 51:1637-1642.
    • (2008) Hypertension , vol.51 , pp. 1637-1642
    • Jackson, E.K.1    Mi, Z.2
  • 83
    • 36649012372 scopus 로고    scopus 로고
    • Effects of dipeptidyl peptidase iv inhibition on arterial blood pressure
    • Jackson E.K., Dubinion J.H., Mi Z. Effects of dipeptidyl peptidase iv inhibition on arterial blood pressure. Clin Exp Pharmacol Physiol 2008, 35:29-34.
    • (2008) Clin Exp Pharmacol Physiol , vol.35 , pp. 29-34
    • Jackson, E.K.1    Dubinion, J.H.2    Mi, Z.3
  • 84
    • 80051786501 scopus 로고    scopus 로고
    • The role of incretins in salt-sensitive hypertension: the potential use of dipeptidyl peptidase-IV inhibitors
    • Tanaka T., Nangaku M., Nishiyama A. The role of incretins in salt-sensitive hypertension: the potential use of dipeptidyl peptidase-IV inhibitors. Curr Opin Nephrol Hypertens 2011, 20:476-481.
    • (2011) Curr Opin Nephrol Hypertens , vol.20 , pp. 476-481
    • Tanaka, T.1    Nangaku, M.2    Nishiyama, A.3
  • 85
    • 77955573674 scopus 로고    scopus 로고
    • Efficacy and safety of exenatide once weekly versus sitagliptin or pioglitazone as an adjunct to metformin for treatment of type 2 diabetes (DURATION-2): a randomised trial
    • Bergenstal R.M., Wysham C., Macconell L., et al. Efficacy and safety of exenatide once weekly versus sitagliptin or pioglitazone as an adjunct to metformin for treatment of type 2 diabetes (DURATION-2): a randomised trial. Lancet 2010, 376:431-439.
    • (2010) Lancet , vol.376 , pp. 431-439
    • Bergenstal, R.M.1    Wysham, C.2    Macconell, L.3
  • 86
    • 79955952000 scopus 로고    scopus 로고
    • Sitagliptin, a dipeptidyl peptidase-4 inhibitor, decreases systolic blood pressure in Japanese hypertensive patients with type 2 diabetes
    • Ogawa S., Ishiki M., Nako K., et al. Sitagliptin, a dipeptidyl peptidase-4 inhibitor, decreases systolic blood pressure in Japanese hypertensive patients with type 2 diabetes. Tohoku J Exp Med 2011, 223:133-135.
    • (2011) Tohoku J Exp Med , vol.223 , pp. 133-135
    • Ogawa, S.1    Ishiki, M.2    Nako, K.3
  • 87
    • 41849099939 scopus 로고    scopus 로고
    • Effect of sitagliptin, a dipeptidyl peptidase-4 inhibitor, on blood pressure in nondiabetic patients with mild to moderate hypertension
    • Mistry G.C., Maes A.L., Lasseter K.C., et al. Effect of sitagliptin, a dipeptidyl peptidase-4 inhibitor, on blood pressure in nondiabetic patients with mild to moderate hypertension. J Clin Pharmacol 2008, 48:592-598.
    • (2008) J Clin Pharmacol , vol.48 , pp. 592-598
    • Mistry, G.C.1    Maes, A.L.2    Lasseter, K.C.3
  • 88
    • 65549123794 scopus 로고    scopus 로고
    • Saxagliptin given in combination with metformin as initial therapy improves glycaemic control in patients with type 2 diabetes compared with either monotherapy: a randomized controlled trial
    • Jadzinsky M., Pfutzner A., Paz-Pacheco E., Xu Z., Allen E., Chen R. Saxagliptin given in combination with metformin as initial therapy improves glycaemic control in patients with type 2 diabetes compared with either monotherapy: a randomized controlled trial. Diabetes Obes Metab 2009, 11:611-622.
    • (2009) Diabetes Obes Metab , vol.11 , pp. 611-622
    • Jadzinsky, M.1    Pfutzner, A.2    Paz-Pacheco, E.3    Xu, Z.4    Allen, E.5    Chen, R.6
  • 89
    • 79953213304 scopus 로고    scopus 로고
    • Diet-induced adipose tissue inflammation and liver steatosis are prevented by DPP-4 inhibition in diabetic mice
    • Shirakawa J., Fujii H., Ohnuma K., et al. Diet-induced adipose tissue inflammation and liver steatosis are prevented by DPP-4 inhibition in diabetic mice. Diabetes 2011, 60:1246-1257.
    • (2011) Diabetes , vol.60 , pp. 1246-1257
    • Shirakawa, J.1    Fujii, H.2    Ohnuma, K.3
  • 90
    • 79251541159 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitor sitagliptin reduces local inflammation in adipose tissue and in pancreatic islets of obese mice
    • Dobrian A.D., Ma Q., Lindsay J.W., et al. Dipeptidyl peptidase IV inhibitor sitagliptin reduces local inflammation in adipose tissue and in pancreatic islets of obese mice. Am J Physiol Endocrinol Metab 2011, 300:E410-E421.
    • (2011) Am J Physiol Endocrinol Metab , vol.300
    • Dobrian, A.D.1    Ma, Q.2    Lindsay, J.W.3
  • 91
    • 80051785333 scopus 로고    scopus 로고
    • DPP-4 (CD26) inhibitor alogliptin inhibits atherosclerosis in diabetic apolipoprotein E-deficient mice
    • Ta N.N., Schuyler C.A., Li Y., Lopes-Virella M.F., Huang Y. DPP-4 (CD26) inhibitor alogliptin inhibits atherosclerosis in diabetic apolipoprotein E-deficient mice. J Cardiovasc Pharmacol 2011, 58:157-166.
    • (2011) J Cardiovasc Pharmacol , vol.58 , pp. 157-166
    • Ta, N.N.1    Schuyler, C.A.2    Li, Y.3    Lopes-Virella, M.F.4    Huang, Y.5
  • 92
    • 0018764335 scopus 로고
    • Diabetes and cardiovascular disease. The Framingham study
    • Kannel W.B., McGee D.L. Diabetes and cardiovascular disease. The Framingham study. JAMA 1979, 241:2035-2038.
    • (1979) JAMA , vol.241 , pp. 2035-2038
    • Kannel, W.B.1    McGee, D.L.2
  • 93
    • 0018341014 scopus 로고
    • Diabetes and cardiovascular risk factors: the Framingham study
    • Kannel W.B., McGee D.L. Diabetes and cardiovascular risk factors: the Framingham study. Circulation 1979, 59:8-13.
    • (1979) Circulation , vol.59 , pp. 8-13
    • Kannel, W.B.1    McGee, D.L.2
  • 94
    • 58149335320 scopus 로고    scopus 로고
    • Efficacy and safety of the dipeptidyl peptidase-4 inhibitor alogliptin in patients with type 2 diabetes inadequately controlled by glyburide monotherapy
    • Pratley R.E., Kipnes M.S., Fleck P.R., Wilson C., Mekki Q. Efficacy and safety of the dipeptidyl peptidase-4 inhibitor alogliptin in patients with type 2 diabetes inadequately controlled by glyburide monotherapy. Diabetes Obes Metab 2009, 11:167-176.
    • (2009) Diabetes Obes Metab , vol.11 , pp. 167-176
    • Pratley, R.E.1    Kipnes, M.S.2    Fleck, P.R.3    Wilson, C.4    Mekki, Q.5
  • 95
    • 77950122844 scopus 로고    scopus 로고
    • Dutogliptin, a selective DPP4 inhibitor, improves glycaemic control in patients with type 2 diabetes: a 12-week, double-blind, randomized, placebo-controlled, multicentre trial
    • Pattzi H.M., Pitale S., Alpizar M., et al. Dutogliptin, a selective DPP4 inhibitor, improves glycaemic control in patients with type 2 diabetes: a 12-week, double-blind, randomized, placebo-controlled, multicentre trial. Diabetes Obes Metab 2010, 12:348-355.
    • (2010) Diabetes Obes Metab , vol.12 , pp. 348-355
    • Pattzi, H.M.1    Pitale, S.2    Alpizar, M.3
  • 96
    • 84860708230 scopus 로고    scopus 로고
    • Review of linagliptin for the treatment of type 2 diabetes mellitus
    • Neumiller J.J., Setter S.M. Review of linagliptin for the treatment of type 2 diabetes mellitus. Clin Ther 2012, 34:993-1005.
    • (2012) Clin Ther , vol.34 , pp. 993-1005
    • Neumiller, J.J.1    Setter, S.M.2
  • 97
    • 84859721063 scopus 로고    scopus 로고
    • DPP-4 inhibitors in the management of type 2 diabetes: a critical review of head-to-head trials
    • Scheen A.J. DPP-4 inhibitors in the management of type 2 diabetes: a critical review of head-to-head trials. Diabetes Metab 2012, 38:89-101.
    • (2012) Diabetes Metab , vol.38 , pp. 89-101
    • Scheen, A.J.1
  • 98
    • 84860711211 scopus 로고    scopus 로고
    • Efficacy and tolerability of the DPP-4 inhibitor alogliptin combined with pioglitazone, in metformin-treated patients with type 2 diabetes
    • DeFronzo R.A., Burant C.F., Fleck P., Wilson C., Mekki Q., Pratley R.E. Efficacy and tolerability of the DPP-4 inhibitor alogliptin combined with pioglitazone, in metformin-treated patients with type 2 diabetes. J Clin Endocrinol Metab 2012, 97:1615-1622.
    • (2012) J Clin Endocrinol Metab , vol.97 , pp. 1615-1622
    • DeFronzo, R.A.1    Burant, C.F.2    Fleck, P.3    Wilson, C.4    Mekki, Q.5    Pratley, R.E.6
  • 100
    • 84865492997 scopus 로고    scopus 로고
    • Meta-analysis of effect of dipeptidyl peptidase-4 inhibitors on cardiovascular risk in type 2 diabetes mellitus
    • Patil H.R., Al Badarin F.J., Shami H.A., et al. Meta-analysis of effect of dipeptidyl peptidase-4 inhibitors on cardiovascular risk in type 2 diabetes mellitus. Am J Cardiol 2012.
    • (2012) Am J Cardiol
    • Patil, H.R.1    Al Badarin, F.J.2    Shami, H.A.3
  • 101
    • 33845489598 scopus 로고    scopus 로고
    • Efficacy and safety of the dipeptidyl peptidase-4 inhibitor sitagliptin as monotherapy in patients with type 2 diabetes mellitus
    • Raz I., Hanefeld M., Xu L., Caria C., Williams-Herman D., Khatami H. Efficacy and safety of the dipeptidyl peptidase-4 inhibitor sitagliptin as monotherapy in patients with type 2 diabetes mellitus. Diabetologia 2006, 49:2564-2571.
    • (2006) Diabetologia , vol.49 , pp. 2564-2571
    • Raz, I.1    Hanefeld, M.2    Xu, L.3    Caria, C.4    Williams-Herman, D.5    Khatami, H.6
  • 102
    • 84855849888 scopus 로고    scopus 로고
    • Safety of dipeptidyl peptidase 4 inhibitors for treatment of type 2 diabetes
    • Mikhail N. Safety of dipeptidyl peptidase 4 inhibitors for treatment of type 2 diabetes. Curr Drug Saf 2011, 6:304-309.
    • (2011) Curr Drug Saf , vol.6 , pp. 304-309
    • Mikhail, N.1
  • 103
    • 84864674632 scopus 로고    scopus 로고
    • Elevated amylase and lipase levels in patients using glucagonlike peptide-1 receptor agonists or dipeptidyl-peptidase-4 inhibitors in the outpatient setting
    • Lando H.M., Alattar M., Dua A.P. Elevated amylase and lipase levels in patients using glucagonlike peptide-1 receptor agonists or dipeptidyl-peptidase-4 inhibitors in the outpatient setting. Endocr Pract 2012, 18(4):472-477.
    • (2012) Endocr Pract , vol.18 , Issue.4 , pp. 472-477
    • Lando, H.M.1    Alattar, M.2    Dua, A.P.3
  • 104
    • 82855179439 scopus 로고    scopus 로고
    • Tolerability of dipeptidyl peptidase-4 inhibitors: a review
    • Richard K.R., Shelburne J.S., Kirk J.K. Tolerability of dipeptidyl peptidase-4 inhibitors: a review. Clin Ther 2011, 33:1609-1629.
    • (2011) Clin Ther , vol.33 , pp. 1609-1629
    • Richard, K.R.1    Shelburne, J.S.2    Kirk, J.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.