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Volumn 12, Issue 1, 2003, Pages 87-100

Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes

Author keywords

Diabetes; Drugs; Enzyme inhibitors; GIP; GLP 1; Glucagon like peptides; Glucose; Incretin; Inhibitor; Peptidase; Peptide

Indexed keywords

6 [[2 [[2 (2 CYANO 1 PYRROLIDINYL) 2 OXOETHYL]AMINO]ETHYL]AMINO]NICOTINONITRILE; APROTININ; BETA CASOMORPHINE; BRADYKININ; DIPEPTIDYL PEPTIDASE IV; ENDOMORPHIN 2; ENTEROSTATIN; ENZYME INHIBITOR; EOTAXIN; GASTRIN RELEASING PEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 2; INSULIN; INTERLEUKIN 2; ISOLEUCINE; MACROPHAGE DERIVED CHEMOKINE; MONOCYTE CHEMOTACTIC PROTEIN 1; MONOCYTE CHEMOTACTIC PROTEIN 2; MONOCYTE CHEMOTACTIC PROTEIN 3; NEUROPEPTIDE Y; PHOSPHORUS 32; PROTEIN INHIBITOR; PYRROLIDINE DERIVATIVE; RANTES; SOMATOMEDIN; STROMAL CELL DERIVED FACTOR 1ALPHA; STROMAL CELL DERIVED FACTOR 1BETA; THIAZOLIDINE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALINE;

EID: 0037234531     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.12.1.87     Document Type: Review
Times cited : (236)

References (159)
  • 1
    • 0001095690 scopus 로고    scopus 로고
    • Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in Type 2 diabetic patients
    • VILSBOLL T, KRARUP T, DEACON CF, MADSBAD S, HOLST JJ: Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in Type 2 diabetic patients. Diabetes (2001) 50:609-613.
    • (2001) Diabetes , vol.50 , pp. 609-613
    • Vilsboll, T.1    Krarup, T.2    Deacon, C.F.3    Madsbad, S.4    Holst, J.J.5
  • 2
    • 0035462466 scopus 로고    scopus 로고
    • Impaired incretin response after a mixed meal is associated with insulin resistance in nondiabetic men
    • RASK E, OLSSON T, SODERBERG S et al.: Impaired incretin response after a mixed meal is associated with insulin resistance in nondiabetic men. Diabetes Care (2001) 24:1640-1645.
    • (2001) Diabetes Care , vol.24 , pp. 1640-1645
    • Rask, E.1    Olsson, T.2    Soderberg, S.3
  • 3
    • 0015791989 scopus 로고
    • Stimulation of insulin secretion by gastric inhibitory polypeptide in man
    • DUPRE J, ROSS SA,WATSON D, BROWN JC: Stimulation of insulin secretion by gastric inhibitory polypeptide in man. J. Clin. Endocrinol. Metab. (1973) 37:826-828.
    • (1973) J. Clin. Endocrinol. Metab. , vol.37 , pp. 826-828
    • Dupre, J.1    Ross, S.A.2    Watson, D.3    Brown, J.C.4
  • 4
    • 0037098963 scopus 로고    scopus 로고
    • Gastric Inhibitory Polypeptide: The neglected incretin revisited
    • MEIER JJ, NAUCK MA, SCHMIDT WE, GALLWITZ B: Gastric Inhibitory Polypeptide: the neglected incretin revisited. Regul. Pept. (2002) 107:1-13.
    • (2002) Regul. Pept. , vol.107 , pp. 1-13
    • Meier, J.J.1    Nauck, M.A.2    Schmidt, W.E.3    Gallwitz, B.4
  • 5
    • 0033744922 scopus 로고    scopus 로고
    • GLP-1 but not GIP regulates fasting and non-enteral glucose clearance in mice
    • BAGGIO L, KIEFFER TJ, DRUCKER DJ: GLP-1 but not GIP regulates fasting and non-enteral glucose clearance in mice. Endocrinology (2000) 141:3703-3709.
    • (2000) Endocrinology , vol.141 , pp. 3703-3709
    • Baggio, L.1    Kieffer, T.J.2    Drucker, D.J.3
  • 6
    • 0033744913 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide confers early phase insulin release to oral glucose in rats: Demonstration by a receptor antagonist
    • LEWIS JT, DAYANANDAN B, HABENER JF, KIEFFER TJ: Glucose-dependent insulinotropic polypeptide confers early phase insulin release to oral glucose in rats: demonstration by a receptor antagonist. Endocrinology (2000) 141:3710-3716.
    • (2000) Endocrinology , vol.141 , pp. 3710-3716
    • Lewis, J.T.1    Dayanandan, B.2    Habener, J.F.3    Kieffer, T.J.4
  • 7
    • 0007866067 scopus 로고    scopus 로고
    • Glucose intolerance caused by a defect in the entero-insular axis: A study in gastric inhibitory polypeptide receptor knockout mice
    • MIYAWAKI K, YAMADA Y, YANO H et al.: Glucose intolerance caused by a defect in the entero-insular axis: A study in gastric inhibitory polypeptide receptor knockout mice. Proc. Natl. Acad. Sci. USA (1999) 96:14843-14847.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14843-14847
    • Miyawaki, K.1    Yamada, Y.2    Yano, H.3
  • 8
    • 0033520869 scopus 로고    scopus 로고
    • GIP biology and fat metabolism
    • YIP RG, WOLFE MM: GIP biology and fat metabolism. Life Sci. (2000) 66:91-103.
    • (2000) Life Sci. , vol.66 , pp. 91-103
    • Yip, R.G.1    Wolfe, M.M.2
  • 9
    • 0036068322 scopus 로고    scopus 로고
    • Inhibition of gastric inhibitory polypeptide signaling prevents obesity
    • MIYAWAKI K, YAMADA Y, BAN N et al.: Inhibition of gastric inhibitory polypeptide signaling prevents obesity. Nat. Med. (2002) 8:738-742.
    • (2002) Nat. Med. , vol.8 , pp. 738-742
    • Miyawaki, K.1    Yamada, Y.2    Ban, N.3
  • 10
    • 0035041250 scopus 로고    scopus 로고
    • Defective glucose-dependent insulinotropic polypeptide receptor expression in diabetic fatty Zucker rats
    • LYNN FC, PAMIR N, NG EH, MCINTOSH CH, KIEFFER TJ, PEDERSON RA. Defective glucose-dependent insulinotropic polypeptide receptor expression in diabetic fatty Zucker rats. Diabetes (2001) 50:1004-1011.
    • (2001) Diabetes , vol.50 , pp. 1004-1011
    • Lynn, F.C.1    Pamir, N.2    Ng, E.H.3    Mcintosh, C.H.4    Kieffer, T.J.5    Pederson, R.A.6
  • 11
    • 0023243048 scopus 로고
    • The effects of glucose-dependent insulinotropic polypeptide infused at physiological concentrations in normal subjects and Type 2 (non-insulin- dependent) diabetic patients on glucose tolerance and B-cell secretion
    • JONES IR, OWENS DR, MOODY AJ, LUZIO SD, MORRIS T, HAYES TM: The effects of glucose-dependent insulinotropic polypeptide infused at physiological concentrations in normal subjects and Type 2 (non-insulin- dependent) diabetic patients on glucose tolerance and B-cell secretion. Diabetologia (1987) 30:707-712.
    • (1987) Diabetologia , vol.30 , pp. 707-712
    • Jones, I.R.1    Owens, D.R.2    Moody, A.J.3    Luzio, S.D.4    Morris, T.5    Hayes, T.M.6
  • 12
    • 0027391607 scopus 로고
    • Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus
    • NAUCK MA, HEIMESAAT MM, ORSKOV C, HOIST JJ, EBERT R, CREUTZFELDT W: Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus. J. Clin. Invest. (1993) 91:301-307.
    • (1993) J. Clin. Invest. , vol.91 , pp. 301-307
    • Nauck, M.A.1    Heimesaat, M.M.2    Orskov, C.3    Hoist, J.J.4    Ebert, R.5    Creutzfeldt, W.6
  • 13
    • 0028224617 scopus 로고
    • The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7-37) in normal and diabetic subjects
    • ELAHI D, MCALOON-DYKE M, FUKAGAWA NK et al.:The insulinotropic actions of glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (7-37) in normal and diabetic subjects. Regul. Pept. (1994) 51:63-74.
    • (1994) Regul. Pept. , vol.51 , pp. 63-74
    • Elahi, D.1    Mcaloon-Dyke, M.2    Fukagawa, N.K.3
  • 14
    • 0036373430 scopus 로고    scopus 로고
    • Defective amplification of the late phase insulin response to glucose by GIP in obese Type II diabetic patients
    • VILSBOLL T, KRARUP T, MADSBAD S, HOLST JJ: Defective amplification of the late phase insulin response to glucose by GIP in obese Type II diabetic patients. Diabetologia (2002) 45:1111-1119.
    • (2002) Diabetologia , vol.45 , pp. 1111-1119
    • Vilsboll, T.1    Krarup, T.2    Madsbad, S.3    Holst, J.J.4
  • 15
    • 0035512742 scopus 로고    scopus 로고
    • Reduced insulinotropic effect of gastric inhibitory polypeptide in first-degree relatives of patients with type 2 diabetes
    • MEIER JJ, HUCKING K, HOLST JJ, DEACON CF, SCHMIEGEL WH, NAUCK MA: Reduced insulinotropic effect of gastric inhibitory polypeptide in first-degree relatives of patients with type 2 diabetes. Diabetes (2001) 50:2497-2504.
    • (2001) Diabetes , vol.50 , pp. 2497-2504
    • Meier, J.J.1    Hucking, K.2    Holst, J.J.3    Deacon, C.F.4    Schmiegel, W.H.5    Nauck, M.A.6
  • 16
    • 0036383414 scopus 로고    scopus 로고
    • Improved stability, insulin-releasing activity and antidiabetic potential of two novel N-terminal analogues of gastric inhibitory polypeptide: N-acetyl-GIP and pGlu-GIP
    • O'HARTE FP, GAULT VA, PARKER JC et al.: Improved stability, insulin-releasing activity and antidiabetic potential of two novel N-terminal analogues of gastric inhibitory polypeptide: N-acetyl-GIP and pGlu-GIP. Diabetogia (2002) 45:1281-1291.
    • (2002) Diabetogia , vol.45 , pp. 1281-1291
    • O'Harte, F.P.1    Gault, V.A.2    Parker, J.C.3
  • 17
    • 0036216683 scopus 로고    scopus 로고
    • Evidence for early impairment of glucagon-like peptide 1-induced insulin secretion in human Type 2 (non insulin-dependent) diabetes
    • LUGARI R, DEI CAS A, UGOLOTTI D et al.: Evidence for early impairment of glucagon-like peptide 1-induced insulin secretion in human Type 2 (non insulin-dependent) diabetes. Horm. Metab. Res. (2002) 34:150-154.
    • (2002) Horm. Metab. Res. , vol.34 , pp. 150-154
    • Lugari, R.1    Dei Cas, A.2    Ugolotti, D.3
  • 19
    • 0027135184 scopus 로고
    • Renal catabolism of truncated glucagon-like peptide 1
    • RUIZ-GRANDE C, ALARCON C, ALCANTARA A et al.: Renal catabolism of truncated glucagon-like peptide 1. Horm. Metab. Res. (1993) 25:612-616.
    • (1993) Horm. Metab. Res. , vol.25 , pp. 612-616
    • Ruiz-Grande, C.1    Alarcon, C.2    Alcantara, A.3
  • 20
    • 0027215348 scopus 로고
    • Dipepridyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • MENTLEIN R, GALLWITZ B, SCHMIDT WE: Dipepridyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. (1993) 214:829-835.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 21
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • KIEFFER TJ, MCINTOSH CH, PEDERSON RA: Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology (1995) 136:3585-3596.
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    Mcintosh, C.H.2    Pederson, R.A.3
  • 22
    • 0028803336 scopus 로고
    • Both subcutaneously and intravenously administered glucagon-like peptide 1 are rapidly degraded from the NH2-terminus in Type II diabetic patients and in healthy subjects
    • DEACON CF, NAUCK MA, TOFT-NIELSEN M, PRIDAL L, WILLMS B, HOLST JJ: Both subcutaneously and intravenously administered glucagon-like peptide 1 are rapidly degraded from the NH2-terminus in Type II diabetic patients and in healthy subjects. Diabetes (1995) 44:1126-1131.
    • (1995) Diabetes , vol.44 , pp. 1126-1131
    • Deacon, C.F.1    Nauck, M.A.2    Toft-Nielsen, M.3    Pridal, L.4    Willms, B.5    Holst, J.J.6
  • 23
    • 0029111540 scopus 로고
    • Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1 (7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides
    • HUPE-SODMANN K, MCGREGOR GP, BRIDENBAUGH R et al: Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1 (7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides. Regul. Pept. (1995) 58:149-156.
    • (1995) Regul. Pept. , vol.58 , pp. 149-156
    • Hupe-Sodmann, K.1    Mcgregor, G.P.2    Bridenbaugh, R.3
  • 24
    • 0344357096 scopus 로고
    • Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line
    • DRUCKER DJ, PHILIPPE J, MOJSOV S, CHICK WL, HABENER JF: Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line. Proc. Natl. Acad. Sci. USA (1987) 84:3434-3438.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3434-3438
    • Drucker, D.J.1    Philippe, J.2    Mojsov, S.3    Chick, W.L.4    Habener, J.F.5
  • 25
    • 0023107555 scopus 로고
    • Insulinotropin: Glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas
    • MOJSOV S, WEIR GC, HABENER JF: Insulinotropin: Glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas. J. Clin. Invest. (1987) 79:616-619.
    • (1987) J. Clin. Invest. , vol.79 , pp. 616-619
    • Mojsov, S.1    Weir, G.C.2    Habener, J.F.3
  • 26
    • 0023758530 scopus 로고
    • Effect of truncated glucagon-like peptide-1 [proglucagon-(78-107) amide] on endocrine secretion from pig pancreas, antrum, and nonantral stomach
    • ORSKOV C, HOLST JJ, NIELSEN OV: Effect of truncated glucagon-like peptide-1 [proglucagon-(78-107) amide] on endocrine secretion from pig pancreas, antrum, and nonantral stomach. Endocrinology (1988) 123:2009-2013.
    • (1988) Endocrinology , vol.123 , pp. 2009-2013
    • Orskov, C.1    Holst, J.J.2    Nielsen, O.V.3
  • 27
    • 0027473729 scopus 로고
    • Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1(7-37)
    • HOLZ GG, KUHTREIBER WM, HABENER JF: Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1(7-37). Nature (1993) 361:362-365.
    • (1993) Nature , vol.361 , pp. 362-365
    • Holz, G.G.1    Kuhtreiber, W.M.2    Habener, J.F.3
  • 28
    • 0028885121 scopus 로고
    • Glucagon-like peptide-1 affects gene transcription and messenger ribonucleic acid stability of components of the insulin secretory system in RIN 104-638 cells
    • WANG Y, EGAN JM, RAYGADA M, NADIV O, ROTH J, MONTROSE-RAFIZADEH C: Glucagon-like peptide-1 affects gene transcription and messenger ribonucleic acid stability of components of the insulin secretory system in RIN 104-638 cells. Endocrinology (1995) 136(11):4910-4917.
    • (1995) Endocrinology , vol.136 , Issue.11 , pp. 4910-4917
    • Wang, Y.1    Egan, J.M.2    Raygada, M.3    Nadiv, O.4    Roth, J.5    Montrose-Rafizadeh, C.6
  • 29
    • 0026535588 scopus 로고
    • Insulinotropic hormone glucagon-like peptide-I(7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 ca
    • FEHMANN H-C, HABENER JF: Insulinotropic hormone glucagon-like peptide-I(7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 ca. Endocrinology (1992) 130:159-166.
    • (1992) Endocrinology , vol.130 , pp. 159-166
    • Fehmann, H.-C.1    Habener, J.F.2
  • 30
    • 0030913210 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 can reverse the age-related decline in glucose tolerance in rats
    • WANG Y, PERFETTI R, GREIG NH et al.: Glucagon-like peptide-1 can reverse the age-related decline in glucose tolerance in rats. J. Clin. Invest. (1997) 99:2883-2889.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2883-2889
    • Wang, Y.1    Perfetti, R.2    Greig, N.H.3
  • 31
    • 0030068620 scopus 로고    scopus 로고
    • Gastric emptying, glucose responses, and insulin secretion after a liquid test meal: Effects of exogenous glucagon-like peptide-1 (GLP-1)-(7-36)amide in Type 2 (non-insulin dependent) diabetic patients
    • WILLMS B, WERNER J, HOIST JJ, ORSKOV C, CREUTZFELDT W, NAUCK MA. Gastric emptying, glucose responses, and insulin secretion after a liquid test meal: effects of exogenous glucagon-like peptide-1 (GLP-1)-(7-36)amide in Type 2 (non-insulin dependent) diabetic patients. J. Clin. Endocrinol, Metab. (1996) 81:327-332.
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 327-332
    • Willms, B.1    Werner, J.2    Hoist, J.J.3    Orskov, C.4    Creutzfeldt, W.5    Nauck, M.A.6
  • 32
    • 0030667056 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 inhibition of gastric emptying outweighs its insulinotropic effects in healthy humans
    • NAUCK MA, NIEDEREICHHOLZ U, ETTLER R et al.: Glucagon-like peptide 1 inhibition of gastric emptying outweighs its insulinotropic effects in healthy humans. Am. J. Physiol. (1997) 273:E981-E988.
    • (1997) Am. J. Physiol. , vol.273
    • Nauck, M.A.1    Niedereichholz, U.2    Ettler, R.3
  • 33
    • 0025678133 scopus 로고
    • Effects of truncated glucagon-like peptide-1 on pancreatic hormone release in normal conscious dogs
    • KAWAI K, SUZUKI S, OHASHI S, MUKAI H, MURAYMA Y, YAMASHITA K: Effects of truncated glucagon-like peptide-1 on pancreatic hormone release in normal conscious dogs. Acta Endocrinol. (Copenh.) (1990) 123:661-667.
    • (1990) Acta Endocrinol. (Copenh.) , vol.123 , pp. 661-667
    • Kawai, K.1    Suzuki, S.2    Ohashi, S.3    Mukai, H.4    Murayma, Y.5    Yamashita, K.6
  • 34
    • 0035824548 scopus 로고    scopus 로고
    • Critical role of cAMP-GEFII/Rim2 complex in incretin-potentiated insulin secretion
    • KASHIMA Y, MIKI T, SHIBASAKI T et al.: Critical role of cAMP-GEFII/Rim2 complex in incretin-potentiated insulin secretion. J. Biol. Chem. (2001) 276:46046-46053.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46046-46053
    • Kashima, Y.1    Miki, T.2    Shibasaki, T.3
  • 35
    • 0028978243 scopus 로고
    • 2+-signaling pathway in pancreatic b-cells by the insulinotropic hormone glucagon-like peptide-1
    • 2+-signaling pathway in pancreatic b-cells by the insulinotropic hormone glucagon-like peptide-1. J. Biol Chem. (1995) 270:17749-17757.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17749-17757
    • Holz, G.G.1    Leech, C.A.2    Habener, J.F.3
  • 36
    • 0036718447 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 inhibits pancreatic ATP-sensitive potassium channels via a protein kinase A- and ADP-dependent mechanism
    • LIGHT PE, MANNING FOX JE, RIEDEL MJ, WHEELER MB: Glucagon-like peptide-1 inhibits pancreatic ATP-sensitive potassium channels via a protein kinase A- and ADP-dependent mechanism. Mol. Endocrinol. (2002) 16:2135-2144.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2135-2144
    • Light, P.E.1    Manning Fox, J.E.2    Riedel, M.J.3    Wheeler, M.B.4
  • 37
    • 0032908809 scopus 로고    scopus 로고
    • Initiation of increased pancreatic islet growth in young normoglycemic mice (Umea +/?)
    • EDVELL A, LINDSTROM P: Initiation of increased pancreatic islet growth in young normoglycemic mice (Umea +/?). Endocrinology (1999) 140:778-783.
    • (1999) Endocrinology , vol.140 , pp. 778-783
    • Edvell, A.1    Lindstrom, P.2
  • 38
    • 0033513455 scopus 로고    scopus 로고
    • Exendin-4 stimulates both beta-cell replication and neogenesis, resulting in increased beta-cell mass and improved glucose tolerance in diabetic rats
    • XU G, STOFFERS DA, HABENER JE, BONNER-WEIR S: Exendin-4 stimulates both beta-cell replication and neogenesis, resulting in increased beta-cell mass and improved glucose tolerance in diabetic rats. Diabetes (1999) 48:2270-2276.
    • (1999) Diabetes , vol.48 , pp. 2270-2276
    • Xu, G.1    Stoffers, D.A.2    Habener, J.E.3    Bonner-Weir, S.4
  • 39
    • 0034032317 scopus 로고    scopus 로고
    • Insulinotropic glucagon-like peptide-1 agonists stimulate expression of homeodomain protein IDX-1 and increase β-cell mass in mouse pancreas
    • STOFFERS DA, KIEFFER TJ, HUSSAIN MA et al.: Insulinotropic glucagon-like peptide-1 agonists stimulate expression of homeodomain protein IDX-1 and increase β-cell mass in mouse pancreas. Diabetes (2000) 49:741-748.
    • (2000) Diabetes , vol.49 , pp. 741-748
    • Stoffers, D.A.1    Kieffer, T.J.2    Hussain, M.A.3
  • 40
    • 0033512486 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 and exendin-4 convert pancreatic AR42J cells into glucagon- and insulin-producing cells
    • ZHOU J, WANG X, PINEYRO MA, EGAN JM: Glucagon-like peptide 1 and exendin-4 convert pancreatic AR42J cells into glucagon- and insulin-producing cells. Diabetes (1999) 48:2358-2366.
    • (1999) Diabetes , vol.48 , pp. 2358-2366
    • Zhou, J.1    Wang, X.2    Pineyro, M.A.3    Egan, J.M.4
  • 41
    • 0035084164 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 induces differentiation of islet duodenal homeobox-1-positive pancreatic ductal cells into insulin-secreting cells
    • HUI H, WRIGHT C, PERFETTI R. Glucagon-like peptide 1 induces differentiation of islet duodenal homeobox-1-positive pancreatic ductal cells into insulin-secreting cells. Diabetes (2001) 50:785-796.
    • (2001) Diabetes , vol.50 , pp. 785-796
    • Hui, H.1    Wright, C.2    Perfetti, R.3
  • 42
    • 0037312818 scopus 로고    scopus 로고
    • Glucagon-like peptides: Regulators of cell proliferation, differentiation and apoptosis
    • (In press)
    • DRUCKER DJ: Glucagon-like peptides: Regulators of cell proliferation, differentiation and apoptosis. Mol. Endocrinol. (2003) 17 (In press).
    • (2003) Mol. Endocrinol. , vol.17
    • Drucker, D.J.1
  • 43
    • 0032521530 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 stimulates luteinizing hormone releasing hormone secretion in a rodent hypothalamic neuronal cell line (GT1-7)
    • BEAK SA, HEATH MM, SMALL CJ et al.: Glucagon-like peptide-1 stimulates luteinizing hormone releasing hormone secretion in a rodent hypothalamic neuronal cell line (GT1-7). J. Clin. Invest. (1998) 101:1334-1341.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1334-1341
    • Beak, S.A.1    Heath, M.M.2    Small, C.J.3
  • 44
    • 0029761505 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) releases thyrotropin (TSH): Characterization of binding sites for GLP-1 on alpha-TSH cells
    • BEAK SA, SMALL CJ, ILOVAISKAIA I et al.: Glucagon-like peptide-1 (GLP-1) releases thyrotropin (TSH): characterization of binding sites for GLP-1 on alpha-TSH cells. Endocrinology (1996) 137:4130-4138.
    • (1996) Endocrinology , vol.137 , pp. 4130-4138
    • Beak, S.A.1    Small, C.J.2    Ilovaiskaia, I.3
  • 45
    • 0030967436 scopus 로고    scopus 로고
    • Central administration of glucagon-like peptide-1 activates hypothalamic neuroendocrine neurons in the rat
    • LARSEN PJ, TANG-CHRISTENSEN M, JESSOP DS: Central administration of glucagon-like peptide-1 activates hypothalamic neuroendocrine neurons in the rat. Endocrinology (1997) 138:4445-4455.
    • (1997) Endocrinology , vol.138 , pp. 4445-4455
    • Larsen, P.J.1    Tang-Christensen, M.2    Jessop, D.S.3
  • 46
    • 13344282056 scopus 로고    scopus 로고
    • A role for glucagon-like peptide-1 in the central regulation of feeding
    • TURTON MD, O'SHEA D, GUNN I et al.: A role for glucagon-like peptide-1 in the central regulation of feeding. Nature (1996) 379:69-72.
    • (1996) Nature , vol.379 , pp. 69-72
    • Turton, M.D.1    O'Shea, D.2    Gunn, I.3
  • 47
    • 0031964636 scopus 로고    scopus 로고
    • Intraventricular GLP-1 reduces short- but not long-term food intake or bodyweight in lean and obese rats
    • DONAHEY JCK, VAN DIJK G, WOODS SC, SEELEY RJ: Intraventricular GLP-1 reduces short- but not long-term food intake or bodyweight in lean and obese rats. Brain Res. (1998) 779:75-83.
    • (1998) Brain Res. , vol.779 , pp. 75-83
    • Donahey, J.C.K.1    Van Dijk, G.2    Woods, S.C.3    Seeley, R.J.4
  • 48
    • 0032908654 scopus 로고    scopus 로고
    • Glucose-lowering and insulin-sensitizing actions of exendin-4: Studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta)
    • YOUNG AA, GEDULIN BR, BHAVSAR S et al: Glucose-lowering and insulin-sensitizing actions of exendin-4: studies in obese diabetic (ob/ob, db/db) mice, diabetic fatty Zucker rats, and diabetic rhesus monkeys (Macaca mulatta). Diabetes (1999) 48:1026-1034.
    • (1999) Diabetes , vol.48 , pp. 1026-1034
    • Young, A.A.1    Gedulin, B.R.2    Bhavsar, S.3
  • 49
    • 0035516188 scopus 로고    scopus 로고
    • Systemic administration of the long-acting GLP-1 derivative NN2211 induces lasting and reversible weight loss in both normal and obese rats
    • LARSEN PJ, FLEDELIUS C, KNUDSEN LB, TANG-CHRISTENSEN M: Systemic administration of the long-acting GLP-1 derivative NN2211 induces lasting and reversible weight loss in both normal and obese rats. Diabetes (2001) 50:2530-2539.
    • (2001) Diabetes , vol.50 , pp. 2530-2539
    • Larsen, P.J.1    Fledelius, C.2    Knudsen, L.B.3    Tang-Christensen, M.4
  • 50
    • 17944365214 scopus 로고    scopus 로고
    • A meta-analysis of the effect of glucagon-like peptide-1 (7-36) amide on ad libitum energy intake in humans
    • VERDICH C, FLINT A, GUTZWILLER JP et al.: A meta-analysis of the effect of glucagon-like peptide-1 (7-36) amide on ad libitum energy intake in humans. J. Clin. Endocrinol, Metab. (2001) 86:4382-4389.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 4382-4389
    • Verdich, C.1    Flint, A.2    Gutzwiller, J.P.3
  • 51
    • 0037045845 scopus 로고    scopus 로고
    • Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in Type 2 diabetes: A parallel-group study
    • ZANDER M, MADSBAD S, MADSEN JL, HOLST JJ: Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in Type 2 diabetes: a parallel-group study. Lancet (2002) 359:824-830.
    • (2002) Lancet , vol.359 , pp. 824-830
    • Zander, M.1    Madsbad, S.2    Madsen, J.L.3    Holst, J.J.4
  • 53
    • 0028883257 scopus 로고
    • Reduction of the incretin effect in rats by the glucagon-like peptide 1 receptor antagonist exendin (9-39) amide
    • KOLLIGS F, FEHMANN H-C, GOKE R, GOKE B: Reduction of the incretin effect in rats by the glucagon-like peptide 1 receptor antagonist exendin (9-39) amide. Diabetes (1995) 44:16-19.
    • (1995) Diabetes , vol.44 , pp. 16-19
    • Kolligs, F.1    Fehmann, H.-C.2    Goke, R.3    Goke, B.4
  • 54
    • 0032960834 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 has a physiological role in the control of postprandial glucose in humans: Studies with the antagonist exendin 9-39
    • EDWARDS CM, TODD JF, MAHMOUDI M et al.: Glucagon-like peptide 1 has a physiological role in the control of postprandial glucose in humans: studies with the antagonist exendin 9-39. Diabetes (1999) 48:86-93.
    • (1999) Diabetes , vol.48 , pp. 86-93
    • Edwards, C.M.1    Todd, J.F.2    Mahmoudi, M.3
  • 55
    • 0000385121 scopus 로고    scopus 로고
    • Exendin (9-39)amide is an antagonist of glucagon-like peptide-1(7- 36)amide in humans
    • SCHIRRA J, STURM K LEICHT P, ARNOLD R, GOKE B, KATSCHINSKI M: Exendin (9-39)amide is an antagonist of glucagon-like peptide-1(7- 36)amide in humans. J. Clin. Invest. (1998) 101:1421-1430.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1421-1430
    • Schirra, J.1    Sturm, K.2    Leicht, P.3    Arnold, R.4    Goke, B.5    Katschinski, M.6
  • 56
    • 0029958404 scopus 로고    scopus 로고
    • Glucose intolerance but normal satiety in mice with a null mutation in the glucagon-like peptide receptor gene
    • SCROCCHI LA, BROWN TJ, MACLUSKY N et al.: Glucose intolerance but normal satiety in mice with a null mutation in the glucagon-like peptide receptor gene. Nat. Med. (1996) 2:1254-1258.
    • (1996) Nat. Med. , vol.2 , pp. 1254-1258
    • Scrocchi, L.A.1    Brown, T.J.2    Maclusky, N.3
  • 57
    • 0032940582 scopus 로고    scopus 로고
    • Repeated intracerebroventricular administration of glucagon-like pepride-1-(7-36) amide or exendin-(9-39) alters body weight in the rat
    • MEERAN K, O'SHEA D, EDWARDS CM et al.: Repeated intracerebroventricular administration of glucagon-like pepride-1-(7-36) amide or exendin-(9-39) alters body weight in the rat. Endocrinology (1999) 140:244-250.
    • (1999) Endocrinology , vol.140 , pp. 244-250
    • Meeran, K.1    O'Shea, D.2    Edwards, C.M.3
  • 58
    • 0031731090 scopus 로고    scopus 로고
    • Effects of aging and a high fat diet on body weight and glucose control in GLP-1R-/- mice
    • SCROCCHI LA, DRUCKER DJ: Effects of aging and a high fat diet on body weight and glucose control in GLP-1R-/- mice. Endocrinology (1998) 139:3127-3132.
    • (1998) Endocrinology , vol.139 , pp. 3127-3132
    • Scrocchi, L.A.1    Drucker, D.J.2
  • 59
    • 0035069103 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 receptor signaling influences topography of islet cells in mice
    • LING Z, WU D, ZAMBRE Y et al.: Glucagon-like peptide 1 receptor signaling influences topography of islet cells in mice. Virchows Arch. (2001) 438:382-387.
    • (2001) Virchows Arch. , vol.438 , pp. 382-387
    • Ling, Z.1    Wu, D.2    Zambre, Y.3
  • 60
    • 0033857422 scopus 로고    scopus 로고
    • Elimination of GLP-1R signaling does not modify weight gain and islet adaptation in mice with combined disruption of leptin and GLP-1 action
    • SCROCCHI LA, HILL ME, SALEH J, PERKINS B, DRUCKER DJ: Elimination of GLP-1R signaling does not modify weight gain and islet adaptation in mice with combined disruption of leptin and GLP-1 action. Diabetes (2000) 49:1552-1560.
    • (2000) Diabetes , vol.49 , pp. 1552-1560
    • Scrocchi, L.A.1    Hill, M.E.2    Saleh, J.3    Perkins, B.4    Drucker, D.J.5
  • 61
    • 0031747107 scopus 로고    scopus 로고
    • Enhanced glucose-dependent insulinotropic polypeptide secretion and insulinotropic action in glucagon-like peptide 1 receptor -/- mice
    • PEDERSON RA, SATKUNARAJAH M, MCINTOSH CH et al.: Enhanced glucose-dependent insulinotropic polypeptide secretion and insulinotropic action in glucagon-like peptide 1 receptor -/- mice. Diabetes (1998) 47:1046-1052.
    • (1998) Diabetes , vol.47 , pp. 1046-1052
    • Pederson, R.A.1    Satkunarajah, M.2    Mcintosh, C.H.3
  • 62
    • 0026596851 scopus 로고
    • Antidiabetogenic effect of glucagon-like peptide-1 (7-36)amide in normal subjects and patients with diabetes mellitus
    • GUTNIAK M, ORSKOV C, HOLST JJ, AHREN B, EFENDIC S: Antidiabetogenic effect of glucagon-like peptide-1 (7-36)amide in normal subjects and patients with diabetes mellitus. N. Engl. J. Med. (1992) 326:1316-1322.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1316-1322
    • Gutniak, M.1    Orskov, C.2    Holst, J.J.3    Ahren, B.4    Efendic, S.5
  • 63
    • 0034814047 scopus 로고    scopus 로고
    • Exendin-4 reduces fasting and postprandial glucose and decreases energy intake in healthy volunteers
    • EDWARDS CM, STANLEY SA, DAVIS R et al.: Exendin-4 reduces fasting and postprandial glucose and decreases energy intake in healthy volunteers. Am. J. Physiol. Endocrinol Metab. (2001) 281:E155-E161.
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281
    • Edwards, C.M.1    Stanley, S.A.2    Davis, R.3
  • 64
    • 0028071448 scopus 로고
    • Subcutaneous injection of the incretin hormone glucagon-like peptide 1 abolishes postprandial glycemia in NIDDM
    • GUTNIAK MK, LINDE B, HOLST JJ, EFENDIC S: Subcutaneous injection of the incretin hormone glucagon-like peptide 1 abolishes postprandial glycemia in NIDDM. Diabetes Care (1994) 17:1039-1044.
    • (1994) Diabetes Care , vol.17 , pp. 1039-1044
    • Gutniak, M.K.1    Linde, B.2    Holst, J.J.3    Efendic, S.4
  • 65
    • 0029909112 scopus 로고    scopus 로고
    • Normalization of insulin responses to glucose by overnight infusion of glucagon-like peptide 1(7-36)amide in patients with NIDDM
    • RACHMAN J, GRIBBLE FM, BARROW BA, LEVY JC, BUCHANAN KD, TURNER RC: Normalization of insulin responses to glucose by overnight infusion of glucagon-like peptide 1(7-36)amide in patients with NIDDM. Diabetes (1996) 45:1524-1530.
    • (1996) Diabetes , vol.45 , pp. 1524-1530
    • Rachman, J.1    Gribble, F.M.2    Barrow, B.A.3    Levy, J.C.4    Buchanan, K.D.5    Turner, R.C.6
  • 66
    • 0029954211 scopus 로고    scopus 로고
    • Glucagonostatic actions and reduction of fasting hyperglycemia by exogenous glucagon-like peptide I(7-36) amide in Type I diabetic patients
    • CREUTZFELD WO, KLEINE N, WILLMS B, ORSKOV C, HOLST JJ, NAUCK MA. Glucagonostatic actions and reduction of fasting hyperglycemia by exogenous glucagon-like peptide I(7-36) amide in Type I diabetic patients. Diabetes Care (1996) 19:580-586.
    • (1996) Diabetes Care , vol.19 , pp. 580-586
    • Creutzfeld, W.O.1    Kleine, N.2    Willms, B.3    Orskov, C.4    Holst, J.J.5    Nauck, M.A.6
  • 67
    • 0026542396 scopus 로고
    • Insulinotropic action of glucagon-like peptide-I-(7-37) in diabetic and non-diabetic subjects
    • NATHAN DM, SCHREIBER E, FOGEL H, MOJSOV S, HABENER JF: Insulinotropic action of glucagon-like peptide-I-(7-37) in diabetic and non-diabetic subjects. Diabetes Care (1992) 15:270-276.
    • (1992) Diabetes Care , vol.15 , pp. 270-276
    • Nathan, D.M.1    Schreiber, E.2    Fogel, H.3    Mojsov, S.4    Habener, J.F.5
  • 68
    • 0029799525 scopus 로고    scopus 로고
    • Glucagon-like peptide I enhances the insulinotropic effect of glibenclamide in NIDDM patients and in the perfused rat pancreas
    • GUTNIAK MK, JUNTTI-BERGGREN L, HELLSTROM PM, GUENIFI A, HOLST JJ, EFENDIC S: Glucagon-like peptide I enhances the insulinotropic effect of glibenclamide in NIDDM patients and in the perfused rat pancreas. Diabetes Care (1996) 19:857-863.
    • (1996) Diabetes Care , vol.19 , pp. 857-863
    • Gutniak, M.K.1    Juntti-Berggren, L.2    Hellstrom, P.M.3    Guenifi, A.4    Holst, J.J.5    Efendic, S.6
  • 69
    • 0029033945 scopus 로고
    • Glucagon-like peptide I reduces postprandial glycemic excursions in IDDM
    • DUPRE J, BEHME MT, HRAMIAK IM et al.: Glucagon-like peptide I reduces postprandial glycemic excursions in IDDM. Diabetes (1995) 44:626-630.
    • (1995) Diabetes , vol.44 , pp. 626-630
    • Dupre, J.1    Behme, M.T.2    Hramiak, I.M.3
  • 70
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • DEACON CF, JOHNSEN AH, HOLST JJ: Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J. Clin. Endocrinol. Metab. (1995) 80:952-957.
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 71
    • 0027157849 scopus 로고
    • Biological effects and metabolic rates of glucagon-like peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable
    • ORSKOV C, WETTERGREN A, HOLST JJ: Biological effects and metabolic rates of glucagon-like peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable. Diabetes (1993) 42:658-661.
    • (1993) Diabetes , vol.42 , pp. 658-661
    • Orskov, C.1    Wettergren, A.2    Holst, J.J.3
  • 72
    • 0035432607 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment
    • LARSEN J, HYLLEBERG B, NG K, DAMSBO P: Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment. Diabetes Care (2001) 24:1416-1421.
    • (2001) Diabetes Care , vol.24 , pp. 1416-1421
    • Larsen, J.1    Hylleberg, B.2    Ng, K.3    Damsbo, P.4
  • 73
    • 0034857141 scopus 로고    scopus 로고
    • Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes
    • DRUCKER DJ: Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Curr. Pharm. Des. (2001) 7:1399-1412.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1399-1412
    • Drucker, D.J.1
  • 74
    • 0031033531 scopus 로고    scopus 로고
    • Near normalization of diurnal glucose concentrations by continuous administration of glucagon-like peptide 1 (GLP-1) in subjects with NIDDM
    • RACHMAN J, BARROW BA, LEVY JC, TURNER RC: Near normalization of diurnal glucose concentrations by continuous administration of glucagon-like peptide 1 (GLP-1) in subjects with NIDDM. Diabetologia (1997) 40:205-211.
    • (1997) Diabetologia , vol.40 , pp. 205-211
    • Rachman, J.1    Barrow, B.A.2    Levy, J.C.3    Turner, R.C.4
  • 75
    • 0032976939 scopus 로고    scopus 로고
    • Continuous subcutaneous infusion of glucagon-like peptide 1 lowers plasma glucose and reduces appetite in Type 2 diabetic patients
    • TOFT-NIELSEN MB, MADSBAD S, HOLST JJ: Continuous subcutaneous infusion of glucagon-like peptide 1 lowers plasma glucose and reduces appetite in Type 2 diabetic patients. Diabetes Care (1999) 22:1137-1143.
    • (1999) Diabetes Care , vol.22 , pp. 1137-1143
    • Toft-Nielsen, M.B.1    Madsbad, S.2    Holst, J.J.3
  • 76
    • 0031664857 scopus 로고    scopus 로고
    • Subcutaneous glucagon-like peptide-1 improves postprandial glycaemic control over a 3-week period in patients with early Type 2 diabetes
    • TODD JF, EDWARDS CM, GHATEI MA, MATHER HM, BLOOM SR. Subcutaneous glucagon-like peptide-1 improves postprandial glycaemic control over a 3-week period in patients with early Type 2 diabetes. Clin. Sci. (Colch.) (1998) 95:325-329.
    • (1998) Clin. Sci. (Colch.) , vol.95 , pp. 325-329
    • Todd, J.F.1    Edwards, C.M.2    Ghatei, M.A.3    Mather, H.M.4    Bloom, S.R.5
  • 77
    • 0027184119 scopus 로고
    • Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting β-cells
    • GOKE R, FEHMANN H-C, LINN T et al.: Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting β-cells. J. Biol. Chem. (1993) 268:19650-19655.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19650-19655
    • Goke, R.1    Fehmann, H.-C.2    Linn, T.3
  • 78
    • 0036965113 scopus 로고    scopus 로고
    • The insulinotropic effect of acute exendin-4 administered to humans: Comparison of nondiabetic state to Type 2 diabetes
    • EGAN JM, CLOCQUET AR, ELAHI D: The insulinotropic effect of acute exendin-4 administered to humans: comparison of nondiabetic state to Type 2 diabetes. J. Clin. Endocrinol. Metab. (2002) 87:1282-1290.
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 1282-1290
    • Egan, J.M.1    Clocquet, A.R.2    Elahi, D.3
  • 79
    • 0036189831 scopus 로고    scopus 로고
    • The pharmacokinetics, pharmacodynamics, safety and tolerability of NN2211, a new long-acting GLP-1 derivative, in healthy men
    • AGERSO H, JENSEN LB, ELBROND B, ROLAN P, ZDRAVKOVIC M: The pharmacokinetics, pharmacodynamics, safety and tolerability of NN2211, a new long-acting GLP-1 derivative, in healthy men. Diabetologia (2002) 45:195-202.
    • (2002) Diabetologia , vol.45 , pp. 195-202
    • Agerso, H.1    Jensen, L.B.2    Elbrond, B.3    Rolan, P.4    Zdravkovic, M.5
  • 80
    • 0036066641 scopus 로고    scopus 로고
    • Bedtime administration of NN2211, a long-acting GLP-1 derivative, substantially reduces fasting and postprandial glycemia in Type 2 diabetes
    • JUHL CB, HOLLINGDAL M, STURIS J: Bedtime administration of NN2211, a long-acting GLP-1 derivative, substantially reduces fasting and postprandial glycemia in Type 2 diabetes. Diabetes (2002) 51:424-429.
    • (2002) Diabetes , vol.51 , pp. 424-429
    • Juhl, C.B.1    Hollingdal, M.2    Sturis, J.3
  • 81
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • MENTLEIN R: Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul. Pept. (1999) 85:9-24.
    • (1999) Regul. Pept. , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 82
    • 0035723325 scopus 로고    scopus 로고
    • CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes
    • GORRELL MD, GYSBERS V, MCCAUGHAN GW. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand. J. Immunol. (2001) 54:249-264.
    • (2001) Scand. J. Immunol. , vol.54 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    Mccaughan, G.W.3
  • 83
    • 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. (Tokyo) (1998) 124:428-433.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 428-433
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Kikuya, Y.3    Fujimoto, Y.4
  • 84
    • 0033852128 scopus 로고    scopus 로고
    • Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides
    • DURINX C, LAMBEIR AM, BOSMANS E 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) 267:5608-5613.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5608-5613
    • Durinx, C.1    Lambeir, A.M.2    Bosmans, E.3
  • 85
    • 0027236545 scopus 로고
    • Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases
    • DAVID F, BERNARD AM, PIERRES M, MARGUET D: Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases.J. Biol. Chem (1993) 268:17247-17252.
    • (1993) J. Biol. Chem , vol.268 , pp. 17247-17252
    • David, F.1    Bernard, A.M.2    Pierres, M.3    Marguet, D.4
  • 86
    • 0027982677 scopus 로고
    • Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene
    • 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) 40:331-338.
    • (1994) Immunogenetics , vol.40 , pp. 331-338
    • Abbott, C.A.1    Baker, E.2    Sutherland, G.R.3    Mccaughan, G.W.4
  • 87
    • 0024588694 scopus 로고
    • Expression of dipeptidyl peptidase IV in rat tissues is mainly regulated at the mRNA levels
    • 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) 182:256-266.
    • (1989) Exp. Cell Res. , vol.182 , pp. 256-266
    • Hong, W.J.1    Petell, J.K.2    Swank, D.3    Sanford, J.4    Hixson, D.C.5    Doyle, D.6
  • 88
    • 0027523145 scopus 로고
    • Distribution of adenosine deaminase binding protein in normal and malignant tissues of the gastrointestinal tract studied by monoclonal antibodies
    • SAKAMOTO J, WATANABE T, TERAMUKAI S et al.: Distribution of adenosine deaminase binding protein in normal and malignant tissues of the gastrointestinal tract studied by monoclonal antibodies. J. Surg. Oncol. (1993) 52:124-134.
    • (1993) J. Surg. Oncol. , vol.52 , pp. 124-134
    • Sakamoto, J.1    Watanabe, T.2    Teramukai, S.3
  • 89
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T-cell immune response
    • MORIMOTO C, SCHLOSSMAN SF: 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
  • 90
    • 0033853381 scopus 로고    scopus 로고
    • A guardian angel: The involvement of dipeptidyl peptidase IV in psychoneuroendocrine function, nutrition and immune defence
    • HILDEBRANDT M, REUTTER W, ARCK P, ROSE M, KLAPP BF: A guardian angel: the involvement of dipeptidyl peptidase IV in psychoneuroendocrine function, nutrition and immune defence. Clin. Sci. (Lond) (2000) 99:93-104.
    • (2000) Clin. Sci. (Lond) , vol.99 , pp. 93-104
    • Hildebrandt, M.1    Reutter, W.2    Arck, P.3    Rose, M.4    Klapp, B.F.5
  • 92
    • 0033517154 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase IV in context. The diflerent roles of a multifunctional ectoenzyme in malignant transformation
    • IWATA S, MORIMOTO C: CD26/dipeptidyl peptidase IV in context. The diflerent roles of a multifunctional ectoenzyme in malignant transformation. J. Exp. Med. (1999) 190:301-306.
    • (1999) J. Exp. Med. , vol.190 , pp. 301-306
    • Iwata, S.1    Morimoto, C.2
  • 93
    • 0036790842 scopus 로고    scopus 로고
    • CD26: An expanding role in immune regulation and cancer
    • DANG NH, MORIMOTO C: CD26: an expanding role in immune regulation and cancer. Histol. Histopathol. (2002) 17:1213-1226.
    • (2002) Histol. Histopathol. , vol.17 , pp. 1213-1226
    • Dang, N.H.1    Morimoto, C.2
  • 94
    • 0035834010 scopus 로고    scopus 로고
    • CD26-mediated signaling for T cell activation occurs in lipid rafts through its association with CD45RO
    • ISHII T, OHNUMA K, MURAKAMI A et al.: CD26-mediated signaling for T cell activation occurs in lipid rafts through its association with CD45RO. Proc. Natl. Acad Sci. USA (2001) 98:12138-12143.
    • (2001) Proc. Natl. Acad Sci. USA , vol.98 , pp. 12138-12143
    • Ishii, T.1    Ohnuma, K.2    Murakami, A.3
  • 95
    • 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
  • 96
  • 97
    • 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 RP, SCHLOSSMAN SF, 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
  • 98
    • 0034682458 scopus 로고    scopus 로고
    • Internalization of CD26 by mannose 6-phosphate/insulin-like growth Factor II receptor contributes to T cell activation
    • IKUSHIMA H, MUNAKATA Y, ISHII T et al.: Internalization of CD26 by mannose 6-phosphate/insulin-like growth Factor II receptor contributes to T cell activation. Proc. Natl. Acad. Sci. USA (2000) 97:8439-8444.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8439-8444
    • Ikushima, H.1    Munakata, Y.2    Ishii, T.3
  • 99
    • 0036346299 scopus 로고    scopus 로고
    • Soluble CD26/dipeptidyl peptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin-like growth Factor II receptor
    • IKUSHIMA H, MUNAKATA Y, IWATA S et al.: Soluble CD26/dipeptidyl peptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin-like growth Factor II receptor. Cell Immunol. (2002) 215:106-110.
    • (2002) Cell Immunol. , vol.215 , pp. 106-110
    • Ikushima, H.1    Munakata, Y.2    Iwata, S.3
  • 100
    • 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
  • 101
    • 18744386083 scopus 로고    scopus 로고
    • G1/S cell cycle arrest provoked in human T cells by antibody to CD26
    • OHNUMA K, ISHII T, IWATA S et al.: G1/S cell cycle arrest provoked in human T cells by antibody to CD26. Immunology (2002) 107:325-333.
    • (2002) Immunology , vol.107 , pp. 325-333
    • Ohnuma, K.1    Ishii, T.2    Iwata, S.3
  • 102
    • 0028148853 scopus 로고
    • In vitro immune responsiveness of rats lacking active dipeptidylpeptidase IV
    • COBURN MC, HIXSON DC, REICHNER JS: In vitro immune responsiveness of rats lacking active dipeptidylpeptidase IV. Cell Immunol. (1994) 158:269-280.
    • (1994) Cell Immunol. , vol.158 , pp. 269-280
    • Coburn, M.C.1    Hixson, D.C.2    Reichner, J.S.3
  • 103
    • 0034612348 scopus 로고    scopus 로고
    • Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26
    • MARGUET D, BAGGIO, L, KOBAYASHI T et al.: Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Proc. Natl. Acad. Sci. USA (2000) 97:6874-6879.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6874-6879
    • Marguet, D.1    Baggio, L.2    Kobayashi, T.3
  • 104
    • 0033166243 scopus 로고    scopus 로고
    • Dipeptidyl peptidase activity of CD26 in serum and urine as a marker of cholestasis: Experimental and clinical evidence
    • PERNER F, GYURIS T, RAKOCZY G et al.: Dipeptidyl peptidase activity of CD26 in serum and urine as a marker of cholestasis: experimental and clinical evidence. J. Lab. Clin. Med. (1999) 134:56-67.
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 56-67
    • Perner, F.1    Gyuris, T.2    Rakoczy, G.3
  • 105
    • 0034948257 scopus 로고    scopus 로고
    • Serum dipeptidyl peptidase IV (DPP IV, CD26) activity in chronic hepatitis C
    • FIRNEISZ G, LAKATOS PL, SZALAY F: Serum dipeptidyl peptidase IV (DPP IV, CD26) activity in chronic hepatitis C. Scand. J. Gastroenterol. (2001) 36:877-880.
    • (2001) Scand. J. Gastroenterol. , vol.36 , pp. 877-880
    • Firneisz, G.1    Lakatos, P.L.2    Szalay, F.3
  • 106
    • 0024245494 scopus 로고
    • Activity of dipeptidyl peptidase IV and post-proline cleaving enzyme in sera from osteoporotic patients
    • GOTOH H, HAGIHARA M, NAGATSU T, IWATA H, MIURA T: Activity of dipeptidyl peptidase IV and post-proline cleaving enzyme in sera from osteoporotic patients. Clin. Chem. (1988) 34:2499-2501.
    • (1988) Clin. Chem. , vol.34 , pp. 2499-2501
    • Gotoh, H.1    Hagihara, M.2    Nagatsu, T.3    Iwata, H.4    Miura, T.5
  • 107
    • 0034470226 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26): Role in T cell activation and autoimmune disease
    • REINHOLD D, HEMMER B, GRAN B et al.: Dipeptidyl peptidase IV (CD26): role in T cell activation and autoimmune disease. Adv. Exp. Med. Biol. (2000) 477:155-160.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 155-160
    • Reinhold, D.1    Hemmer, B.2    Gran, B.3
  • 108
    • 0027294596 scopus 로고
    • Decreased expression of the memory marker CD26 on both CD4+ and CD8+ T lymphocytes of HIV-infected subjects
    • VANHAM G, KESTENS L, DE MEESTER I et al.: Decreased expression of the memory marker CD26 on both CD4+ and CD8+ T lymphocytes of HIV-infected subjects. J. Acquir. Immune Defic. Syndr. (1993) 6:749-757.
    • (1993) J. Acquir. Immune Defic. Syndr. , vol.6 , pp. 749-757
    • Vanham, G.1    Kestens, L.2    De Meester, I.3
  • 109
    • 0033046381 scopus 로고    scopus 로고
    • Decreased dipeptidyl peptidase IV enzyme activity of plasma soluble CD26 and its inverse correlation with HIV-1 RNA in HIV-1 infected individuals
    • HOSONO O, HOMMA T, KOBAYASHI H et al.: Decreased dipeptidyl peptidase IV enzyme activity of plasma soluble CD26 and its inverse correlation with HIV-1 RNA in HIV-1 infected individuals. Clin. Immunol. (1999) 91:283-295.
    • (1999) Clin. Immunol. , vol.91 , pp. 283-295
    • Hosono, O.1    Homma, T.2    Kobayashi, H.3
  • 110
    • 0034780946 scopus 로고    scopus 로고
    • An evaluation of serum soluble CD30 levels and serum CD26 (DPPIV) enzyme activity as markers of Type 2 and Type 1 cytokines in HIV patients receiving highly active antiretroviral therapy
    • KEANE NM, PRICE P. LEE S, STONE SF, FRENCH MA. An evaluation of serum soluble CD30 levels and serum CD26 (DPPIV) enzyme activity as markers of Type 2 and Type 1 cytokines in HIV patients receiving highly active antiretroviral therapy. Clin. Exp. Immunol. (2001) 126:111-116.
    • (2001) Clin. Exp. Immunol. , vol.126 , pp. 111-116
    • Keane, N.M.1    Price, P.2    Lee, S.3    Stone, S.F.4    French, M.A.5
  • 111
    • 84945023347 scopus 로고
    • Influence of pregnancy on dipeptidyl peptidase IV activity (CD 26 leukocyte differentiation antigen) of circulating lymphocytes
    • MENTLEIN R, STAVES R, RIXMATZEN H, TINNEBERG HR: Influence of pregnancy on dipeptidyl peptidase IV activity (CD 26 leukocyte differentiation antigen) of circulating lymphocytes. Eur. J. Clin. Chem. Clin. Biochem. (1991) 29:477-480.
    • (1991) Eur. J. Clin. Chem. Clin. Biochem. , vol.29 , pp. 477-480
    • Mentlein, R.1    Staves, R.2    Rixmatzen, H.3    Tinneberg, H.R.4
  • 113
    • 0030999425 scopus 로고    scopus 로고
    • Lower serum dipeptidyl peptidase IV activity in treatment resistant major depression: Relationships with immune- inflammatory markers
    • MAES M, DE MEESTER I, VERKERK R et al.: Lower serum dipeptidyl peptidase IV activity in treatment resistant major depression: relationships with immune- inflammatory markers. Psychoneuroendocrinology (1997) 22:65-78.
    • (1997) Psychoneuroendocrinology , vol.22 , pp. 65-78
    • Maes, M.1    De Meester, I.2    Verkerk, R.3
  • 114
    • 0032843197 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and adenosine deaminase activity. Decrease in depression
    • ELGUN S, KESKINEGE A, KUMBASAR H: Dipeptidyl peptidase IV and adenosine deaminase activity. Decrease in depression. Psychoneuroendocrinology (1999) 24:823-832.
    • (1999) Psychoneuroendocrinology , vol.24 , pp. 823-832
    • Elgun, S.1    Keskinege, A.2    Kumbasar, H.3
  • 115
    • 0034473192 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPP IV, CD26) in patients with mental eating disorders
    • HILDEBRANDT M, ROSE M, MAYR C et al.: Dipeptidyl peptidase IV (DPP IV, CD26) in patients with mental eating disorders. Adv. Exp. Med. Biol. (2000) 477:197-204.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 197-204
    • Hildebrandt, M.1    Rose, M.2    Mayr, C.3
  • 116
    • 0026662359 scopus 로고
    • Dipeptidyl peptidase IV in patients with systemic lupus erythematosus
    • STANCIKOVA M, LOJDA Z, LUKAC J, RUZICKOVA M: Dipeptidyl peptidase IV in patients with systemic lupus erythematosus. Clin. Exp. Rheumatol. (1992) 10:381-385.
    • (1992) Clin. Exp. Rheumatol. , vol.10 , pp. 381-385
    • Stancikova, M.1    Lojda, Z.2    Lukac, J.3    Ruzickova, M.4
  • 117
    • 0034767689 scopus 로고    scopus 로고
    • Serum interleukin-12, interleukin-15, soluble CD26, and adenosine deaminase in patients with rheumatoid arthritis
    • CORDERO OJ, SALGADO FJ, MERAVARELA A, NOGUEIRA M: Serum interleukin-12, interleukin-15, soluble CD26, and adenosine deaminase in patients with rheumatoid arthritis. Rheumatol. Int. (2001) 21:69-74.
    • (2001) Rheumatol. Int. , vol.21 , pp. 69-74
    • Cordero, O.J.1    Salgado, F.J.2    Meravarela, A.3    Nogueira, M.4
  • 120
    • 0028823181 scopus 로고
    • CD26 (dipeptidyl peptidase IV/DPP IV) as a novel molecular marker for differentiated thyroid carcinoma
    • 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) 64:326-331.
    • (1995) Int. J. Cancer , vol.64 , pp. 326-331
    • Tanaka, T.1    Umeki, K.2    Yamamoto, I.3    Sakamoto, F.4    Noguchi, S.5    Ohtaki, S.6
  • 121
    • 0029872324 scopus 로고    scopus 로고
    • Differential expression of dipeptidyl peptidase IV (CD26) and thyroid peroxidase in neoplastic thyroid tissues
    • UMEKI K, TANAKA T, YAMAMOTO I et al.: Differential expression of dipeptidyl peptidase IV (CD26) and thyroid peroxidase in neoplastic thyroid tissues. Endocr. J. (1996) 43:53-60.
    • (1996) Endocr. J. , vol.43 , pp. 53-60
    • Umeki, K.1    Tanaka, T.2    Yamamoto, I.3
  • 122
    • 0034000946 scopus 로고    scopus 로고
    • Dipeptidylpeptidase IV activities are elevated in prostate cancers and adjacent benign hyperplastic glands
    • WILSON MJ, RUHLAND AR, QUAST BJ, REDDY PK, EWING SL, SINHA AA: Dipeptidylpeptidase IV activities are elevated in prostate cancers and adjacent benign hyperplastic glands. J. Androl. (2000) 21:220-226.
    • (2000) J. Androl. , vol.21 , pp. 220-226
    • Wilson, M.J.1    Ruhland, A.R.2    Quast, B.J.3    Reddy, P.K.4    Ewing, S.L.5    Sinha, A.A.6
  • 124
    • 0030267113 scopus 로고    scopus 로고
    • Reduced expression of dipeptidyl peptidase (DPP) IV in peripheral blood T lymphocytes of oral cancer patients
    • UEMATSU T, URADE M, YAMAOKA M, YOSHIOKA W: Reduced expression of dipeptidyl peptidase (DPP) IV in peripheral blood T lymphocytes of oral cancer patients. J. Oral Pathol. Med. (1996) 25:507-512.
    • (1996) J. Oral Pathol. Med. , vol.25 , pp. 507-512
    • Uematsu, T.1    Urade, M.2    Yamaoka, M.3    Yoshioka, W.4
  • 125
    • 0035839639 scopus 로고    scopus 로고
    • Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family
    • LAMBEIR AM, PROOST P, DURINX C et al.: Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J. Biol. Chem. (2001) 276:29839-29845.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29839-29845
    • Lambeir, A.M.1    Proost, P.2    Durinx, C.3
  • 126
    • 0035798196 scopus 로고    scopus 로고
    • Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion
    • LAMBEIR AM, DURINX C, PROOST P, VAN DAMME J, SCHARPE S, DE MEESTER I: Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett. (2001) 507:327-330.
    • (2001) FEBS Lett. , vol.507 , pp. 327-330
    • Lambeir, A.M.1    Durinx, C.2    Proost, P.3    Van Damme, J.4    Scharpe, S.5    De Meester, I.6
  • 127
    • 0034473089 scopus 로고    scopus 로고
    • Natural substrates of dipeptidyl peptidase IV
    • DE MEESTER I, DURINX C, BAL G et al.: Natural substrates of dipeptidyl peptidase IV. Adv. Exp. Med. Biol. (2000) 477:67-87.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 67-87
    • Demeester, I.1    Durinx, C.2    Bal, G.3
  • 128
    • 0035847312 scopus 로고    scopus 로고
    • Metabolism of glucagon by dipeptidyl peptidase IV (CD26)
    • POSPISILIK JA, HINKE SA, PEDERSON RA et al.: Metabolism of glucagon by dipeptidyl peptidase IV (CD26). Regul. Pept. (2001) 6:133-141.
    • (2001) Regul. Pept. , vol.6 , pp. 133-141
    • Pospisilik, J.A.1    Hinke, S.A.2    Pederson, R.A.3
  • 129
    • 0034635440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs
    • HINKE SA, POSPISILIK JA, DEMUTH HU et al.: Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs. J. Biol. Chem. (2000) 275:3827-3834.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3827-3834
    • Hinke, S.A.1    Pospisilik, J.A.2    Demuth, H.U.3
  • 131
    • 0033303516 scopus 로고    scopus 로고
    • Glucagon-like pepride-1-(736)amide is transformed to glucagon-like pepride-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries Supplying the L cells of the porcine intestine
    • HANSEN L, DEACON CF, ORSKOV C, HOLST JJ: Glucagon-like pepride-1-(736)amide is transformed to glucagon-like pepride-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries Supplying the L cells of the porcine intestine. Endocrinology (1999) 140:5356-5363.
    • (1999) Endocrinology , vol.140 , pp. 5356-5363
    • Hansen, L.1    Deacon, C.F.2    Orskov, C.3    Holst, J.J.4
  • 132
    • 0032969356 scopus 로고    scopus 로고
    • Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor Ile-thiazolidide
    • PAULY RP, DEMUTH HU, ROSCHE F et al.: Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor Ile-thiazolidide. Metabolism (1999) 48:385-389.
    • (1999) Metabolism , vol.48 , pp. 385-389
    • Pauly, R.P.1    Demuth, H.U.2    Rosche, F.3
  • 133
    • 0000135759 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats
    • BALKAN B, KWASNIK L, MISERENDINO R, HOLST JJ, LI X: Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7-36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia (1999) 42:1324-1331.
    • (1999) Diabetologia , vol.42 , pp. 1324-1331
    • Balkan, B.1    Kwasnik, L.2    Miserendino, R.3    Holst, J.J.4    Li, X.5
  • 134
    • 0036188070 scopus 로고    scopus 로고
    • Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs
    • DEACON CF, WAMBERG S, BIE P, HUGHES TE, HOLST JJ: Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs. J. Endocrinol. (2002) 172:355-362.
    • (2002) J. Endocrinol. , vol.172 , pp. 355-362
    • Deacon, C.F.1    Wamberg, S.2    Bie, P.3    Hughes, T.E.4    Holst, J.J.5
  • 135
    • 0036107064 scopus 로고    scopus 로고
    • Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice
    • REIMER MK, HOIST JJ, AHREN B et al.: Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice. Eur. J. Endocrinol. (2002) 146:717-727.
    • (2002) Eur. J. Endocrinol. , vol.146 , pp. 717-727
    • Reimer, M.K.1    Hoist, J.J.2    Ahren, B.3
  • 136
    • 0034811909 scopus 로고    scopus 로고
    • Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient Fischer rats
    • NAGAKURA T, YASUDA N, YAMAZAKI K et al.: Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient Fischer rats. Biochem. Biophys. Res. Commun. (2001) 284:501-506.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 501-506
    • Nagakura, T.1    Yasuda, N.2    Yamazaki, K.3
  • 137
    • 0030607672 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-(9-36) amide is a major metabolite of glucagon-like peptide-1-(736)amide after in vivo administration to dogs and it acts as an antagonist on the pancreatic receptor
    • KNUDSEN LB, PRIDAL L: Glucagon-like peptide-1-(9-36) amide is a major metabolite of glucagon-like peptide-1-(736)amide after in vivo administration to dogs and it acts as an antagonist on the pancreatic receptor. Eur. J. Pharmacol. (1996) 318:429-435.
    • (1996) Eur. J. Pharmacol. , vol.318 , pp. 429-435
    • Knudsen, L.B.1    Pridal, L.2
  • 138
    • 0035477462 scopus 로고    scopus 로고
    • 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
    • AYTAC U, CLARET FX, HO L et al.: 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) 61:7204-7210.
    • (2001) Cancer Res. , vol.61 , pp. 7204-7210
    • Aytac, U.1    Claret, F.X.2    Ho, L.3
  • 139
    • 0033517124 scopus 로고    scopus 로고
    • A role for dipeptidyl peptidase IV in suppressing the malignant phenotype of melanocytic cells
    • 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) 190:311-322.
    • (1999) J. Exp. Med. , vol.190 , pp. 311-322
    • Wesley, U.V.1    Albino, A.P.2    Tiwari, S.3    Houghton, A.N.4
  • 140
    • 0034956605 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPPIV) inhibits cellular invasion of melanoma cells
    • PETHIYAGODA CL, WELCH DR, FLEMING TP: Dipeptidyl peptidase IV (DPPIV) inhibits cellular invasion of melanoma cells. Clin. Exp. Metastasis (2000) 18:391-400.
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 391-400
    • Pethiyagoda, C.L.1    Welch, D.R.2    Fleming, T.P.3
  • 141
    • 0037093198 scopus 로고    scopus 로고
    • Prolonged survival and decreased invasive activity attributable to dipeptidyl peptidase IV overexpression in ovarian carcinoma
    • 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.
    • (2002) Cancer Res. , vol.62 , pp. 2753-2757
    • Kajiyama, H.1    Kikkawa, F.2    Suzuki, T.3    Shibata, K.4    Ino, K.5    Mizutani, S.6
  • 142
    • 0036739969 scopus 로고    scopus 로고
    • Involvement of Dipeptidyl Peptidase IV in Extravillous Trophoblast Invasion and Differentiation
    • SATO Y, FUJIWARA H, HIGUCHI T et al.: Involvement of Dipeptidyl Peptidase IV in Extravillous Trophoblast Invasion and Diffcrendation.J. Clin. Endocrinol. Metab. (2002) 87:4287-4296.
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 4287-4296
    • Sato, Y.1    Fujiwara, H.2    Higuchi, T.3
  • 143
    • 0037047342 scopus 로고    scopus 로고
    • Regulation of fibroblast migration on collagenous matrix by a cell surface peptidase complex
    • GHERSI G, DONG H, GOLDSTEIN LA et al.: Regulation of fibroblast migration on collagenous matrix by a cell surface peptidase complex. J. Biol. Chem. (2002) 277(32):29231-29241.
    • (2002) J. Biol. Chem. , vol.277 , Issue.32 , pp. 29231-29241
    • Ghersi, G.1    Dong, H.2    Goldstein, L.A.3
  • 144
    • 0035253496 scopus 로고    scopus 로고
    • Targeting dipeptidyl peptidase IV (CD26) suppresses autoimmune encephalomyelitis and upregulates TGF-beta 1 secretion in vivo
    • STEINBRECHER A, REINHOLD D, QUIGLEY L et al.: Targeting dipeptidyl peptidase IV (CD26) suppresses autoimmune encephalomyelitis and upregulates TGF-beta 1 secretion in vivo. J. Immunol. (2001) 166:2041-2048.
    • (2001) J. Immunol. , vol.166 , pp. 2041-2048
    • Steinbrecher, A.1    Reinhold, D.2    Quigley, L.3
  • 145
    • 0036227801 scopus 로고    scopus 로고
    • Involvement of dipeptidyl peptidase TV in immune complex-mediated glomerulonephritis
    • SHINOSAKI T, KOBAYASHI T, KIMURA K, KURIHARA H: Involvement of dipeptidyl peptidase TV in immune complex-mediated glomerulonephritis. Lab. Invest. (2002) 82:505-513.
    • (2002) Lab. Invest. , vol.82 , pp. 505-513
    • Shinosaki, T.1    Kobayashi, T.2    Kimura, K.3    Kurihara, H.4
  • 146
    • 0036634815 scopus 로고    scopus 로고
    • Loss of dipeptidylpeptidase IV activity in chronic rhinosinusitis contributes to the neurogenic inflammation induced by substance P in the nasal mucosa
    • GROUZMANN E, MONOD M, LANDIS B et al.: Loss of dipeptidylpeptidase IV activity in chronic rhinosinusitis contributes to the neurogenic inflammation induced by substance P in the nasal mucosa. FASEB J. (2002) 16:1132-1134.
    • (2002) FASEB J. , vol.16 , pp. 1132-1134
    • Grouzmann, E.1    Monod, M.2    Landis, B.3
  • 147
    • 0035905372 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV-like molecules: Homologous proteins or homologous activities?
    • 1550
    • SEDO A, MALIK R. Dipeptidyl peptidase IV-like molecules: homologous proteins or homologous activities? Biochim. Biophys. Acta (2001) 1550:107-116.
    • (2001) Biochim. Biophys. Acta , pp. 107-116
    • Sedo, A.1    Malik, R.2
  • 148
    • 0031690479 scopus 로고    scopus 로고
    • Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for Type 2 diabetes
    • HOLST JJ, DEACON CF: Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for Type 2 diabetes. Diabetes (1998) 47:1663-1670.
    • (1998) Diabetes , vol.47 , pp. 1663-1670
    • Holst, J.J.1    Deacon, C.F.2
  • 149
    • 0036290037 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition as an approach to the treatment and prevention of Type 2 diabetes: A historical perspective
    • DEACON CF, HOLST JJ: Dipeptidyl peptidase IV inhibition as an approach to the treatment and prevention of Type 2 diabetes: a historical perspective. Biochem. Biophys. Res. Commun. (2002) 294:1-4.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 1-4
    • Deacon, C.F.1    Holst, J.J.2
  • 150
    • 0036391928 scopus 로고    scopus 로고
    • Rebuttal to Deacon and Holst: 'Metformin effects on dipeptidyl peptidase IV degradation of glucagon-like peptide-1' versus 'Dipeptidyl peptidase inhibition as an approach to the treatment and prevention of Type 2 diabetes: A historical perspective
    • DEMUTH HU, HINKE SA, PEDERSON RA, MCINTOSH CH: Rebuttal to Deacon and Holst: 'Metformin effects on dipeptidyl peptidase IV degradation of glucagon-like peptide-1' versus 'Dipeptidyl peptidase inhibition as an approach to the treatment and prevention of Type 2 diabetes: a historical perspective. Biochem. Biophys. Res. Commun. (2002) 296:229-232.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 229-232
    • Demuth, H.U.1    Hinke, S.A.2    Pederson, R.A.3    Mcintosh, C.H.4
  • 151
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig
    • DEACON CF, HUGHES TE, HOLST JJ: Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes (1998) 47:764-769.
    • (1998) Diabetes , vol.47 , pp. 764-769
    • Deacon, C.F.1    Hughes, T.E.2    Holst, J.J.3
  • 152
    • 0031870418 scopus 로고    scopus 로고
    • Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide
    • PEDERSON RA, WHITE HA, SCHLENZIG D, PAULY RP, MCINTOSH CH, DEMUTH HU: Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes (1998) 47:1253-1258.
    • (1998) Diabetes , vol.47 , pp. 1253-1258
    • Pederson, R.A.1    White, H.A.2    Schlenzig, D.3    Pauly, R.P.4    Mcintosh, C.H.5    Demuth, H.U.6
  • 153
    • 0034666562 scopus 로고    scopus 로고
    • Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice
    • AHREN B, HOLST JJ, MARTENSSON H, BALKAN B: Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice. Eur. J. Pharmacol (2000) 404:239-245.
    • (2000) Eur. J. Pharmacol. , vol.404 , pp. 239-245
    • Ahren, B.1    Holst, J.J.2    Martensson, H.3    Balkan, B.4
  • 154
    • 0035403058 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition reduces the degradation and clearance of GIP and potentiates its insulinotropic and antihyperglycemic effects in anesthetized pigs
    • DEACON CF, DANIELSEN P, KLARSKOV L, OLESEN M, HOIST JJ: Dipeptidyl peptidase IV inhibition reduces the degradation and clearance of GIP and potentiates its insulinotropic and antihyperglycemic effects in anesthetized pigs. Diabetes (2001) 50:1588-1597.
    • (2001) Diabetes , vol.50 , pp. 1588-1597
    • Deacon, C.F.1    Danielsen, P.2    Klarskov, L.3    Olesen, M.4    Hoist, J.J.5
  • 155
    • 0036228243 scopus 로고    scopus 로고
    • Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and beta-cell glucose responsiveness in VDF (fa/fa) Zucker rats
    • POSPISILIK JA, STAFFORD SG, DEMUTH HU et al.: Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and beta-cell glucose responsiveness in VDF (fa/fa) Zucker rats. Diabetes (2002) 51:943-950.
    • (2002) Diabetes , vol.51 , pp. 943-950
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.U.3
  • 156
    • 0036724721 scopus 로고    scopus 로고
    • Long-term treatment with dipeptidyl peptidase iv inhibitor improves hepatic and peripheral insulin sensitivity in the VDF Zucker rat: A euglycemic-hyperinsulinemic clamp study
    • POSPISILIK JA, STAFFORD SG, DEMUTH HU, MCINTOSH CH, PEDERSON RA: Long-term treatment with dipeptidyl peptidase iv inhibitor improves hepatic and peripheral insulin sensitivity in the VDF Zucker rat: a euglycemic-hyperinsulinemic clamp study. Diabetes (2002) 51:2677-2683.
    • (2002) Diabetes , vol.51 , pp. 2677-2683
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.U.3    Mcintosh, C.H.4    Pederson, R.A.5
  • 157
    • 0036312876 scopus 로고    scopus 로고
    • Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male zucker diabetic fatty rats
    • SUDRE B, BROQUA P, WHITE RB et al.: Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male zucker diabetic fatty rats. Diabetes (2002) 51:1461-1469.
    • (2002) Diabetes , vol.51 , pp. 1461-1469
    • Sudre, B.1    Broqua, P.2    White, R.B.3
  • 158
    • 0036583164 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in Type 2 diabetes
    • AHREN B, SIMONSSON E, LARSSON H et al.: Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in Type 2 diabetes. Diabetes Care (2002) 25:869-875.
    • (2002) Diabetes Care , vol.25 , pp. 869-875
    • Ahren, B.1    Simonsson, E.2    Larsson, H.3


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