메뉴 건너뛰기




Volumn 73, Issue 1, 2014, Pages 34-46

Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes

Author keywords

Bioactive peptide; Dipeptidyl peptidase IV inhibition; Functional foods; Glucagon like peptide 1; Glucose dependent insulinotropic polypeptide; Hydrolysate; Milk protein; Type 2 diabetes mellitus

Indexed keywords

ANIMALS; BLOOD GLUCOSE; DIABETES MELLITUS, TYPE 2; DIETARY PROTEINS; DIPEPTIDYL PEPTIDASE 4; DIPEPTIDYL-PEPTIDASE IV INHIBITORS; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON-LIKE PEPTIDE 1; HUMANS; HYPOGLYCEMIC AGENTS; MILK PROTEINS; PEPTIDES; PROTEIN HYDROLYSATES;

EID: 84893917196     PISSN: 00296651     EISSN: 14752719     Source Type: Journal    
DOI: 10.1017/S0029665113003601     Document Type: Article
Times cited : (149)

References (87)
  • 1
    • 27144438407 scopus 로고    scopus 로고
    • World Health Organisation. (accessed 12 September 2012)
    • World Health Organisation (2012) Diabetes programme, country and regional data. http://www.who.int/diabetes/ facts/worldfigures/en/ (accessed 12 September 2012).
    • (2012) Diabetes Programme, Country and Regional Data
  • 2
    • 72149109848 scopus 로고    scopus 로고
    • Dietary strategies for patients with type 2 diabetes in the era of multi-approaches; Review and results from the dietary intervention randomized controlled trial (DIRECT)
    • Ben-Avraham S, Harman-Boehm I, Schwarzfuchs D et al. (2009) Dietary strategies for patients with type 2 diabetes in the era of multi-approaches; review and results from the dietary intervention randomized controlled trial (DIRECT). Diabetes Res Clin Pract 86, S41-S48.
    • (2009) Diabetes Res Clin Pract , vol.86
    • Ben-Avraham, S.1    Harman-Boehm, I.2    Schwarzfuchs, D.3
  • 3
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker DJ (2006) The biology of incretin hormones. Cell Metab 3, 153-165.
    • (2006) Cell Metab , vol.3 , pp. 153-165
    • Drucker, D.J.1
  • 4
    • 34249902025 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes
    • Drucker DJ (2007) Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes. Diabetes Care 30, 1335-1343.
    • (2007) Diabetes Care , vol.30 , pp. 1335-1343
    • Drucker, D.J.1
  • 6
    • 77951722213 scopus 로고    scopus 로고
    • DPP-4 inhibitors in type 2 diabetes: Importance of selective enzyme inhibition and implications for clinical use
    • Krushner P & Gorrell M (2010) DPP-4 inhibitors in type 2 diabetes: importance of selective enzyme inhibition and implications for clinical use. J Fam Pract 59, 2.
    • (2010) J Fam Pract , vol.59 , pp. 2
    • Krushner, P.1    Gorrell, M.2
  • 7
    • 63149173251 scopus 로고    scopus 로고
    • Standards of medical care in diabetes-2009
    • American Diabetes Association
    • American Diabetes Association (2009) Standards of medical care in diabetes-2009. Diabetes Care 32, S13-S61.
    • (2009) Diabetes Care , vol.32
  • 8
    • 0742296736 scopus 로고    scopus 로고
    • Milk protein hydrolysates and bioactive peptides
    • 3rd ed.,[PF Fox & PLH Mc Sweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • FitzGerald RJ & Meisel H (2003) Milk protein hydrolysates and bioactive peptides. In Advanced Dairy Chemistry 1:Proteins, 3rd ed., pp. 675-698 [PF Fox & PLH Mc Sweeney, editors]. New York: Kluwer Academic/Plenum Publishers.
    • (2003) Advanced Dairy Chemistry 1: Proteins , pp. 675-698
    • Fitzgerald, R.J.1    Meisel, H.2
  • 9
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray BA & FitzGerald RJ (2007) Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Des 13, 773-791.
    • (2007) Curr Pharm des , vol.13 , pp. 773-791
    • Murray, B.A.1    Fitzgerald, R.J.2
  • 10
    • 23444453867 scopus 로고    scopus 로고
    • Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects
    • Frid AH, Nilsson M, Holst JJ et al. (2005) Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects. Am J Clin Nutr 82, 69-75.
    • (2005) Am J Clin Nutr , vol.82 , pp. 69-75
    • Frid, A.H.1    Nilsson, M.2    Holst, J.J.3
  • 11
    • 23444433404 scopus 로고    scopus 로고
    • Co-ingestion of a protein hydrolysate and amino acid mixture with carbohydrate improves plasma glucose disposal in patients with type 2 diabetes
    • Manders RJF, Wagenmakers AJM, Koopman R et al. (2005) Co-ingestion of a protein hydrolysate and amino acid mixture with carbohydrate improves plasma glucose disposal in patients with type 2 diabetes. Am J Clin Nutr 82, 76-83.
    • (2005) Am J Clin Nutr , vol.82 , pp. 76-83
    • Rjf, M.1    Ajm, W.2    Koopman, R.3
  • 12
    • 84861332110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates
    • Lacroix IME & Li-Chan ECY (2012) Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int Dairy J 25, 97-102.
    • (2012) Int Dairy J , vol.25 , pp. 97-102
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 13
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates
    • Nongonierma AB & FitzGerald RJ (2013a) Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates. Peptides 39, 157-163.
    • (2013) Peptides , vol.39 , pp. 157-163
    • Nongonierma, A.B.1    Fitzgerald, R.J.2
  • 14
    • 0014188893 scopus 로고
    • Plasma insulin responses to oral and intravenous glucose: Studies in normal and diabetic subjects
    • Perley MJ & Kipnis DM (1967) Plasma insulin responses to oral and intravenous glucose: studies in normal and diabetic subjects. J Clin Invest 46, 1954-1962.
    • (1967) J Clin Invest , vol.46 , pp. 1954-1962
    • Perley, M.J.1    Kipnis, D.M.2
  • 15
    • 0022461548 scopus 로고
    • Incretin effects of increasing glucose loads in man calculated from venous insulin and C-peptide responses
    • Nauck M, Homberger E, Siegel EG et al. (1986) Incretin effects of increasing glucose loads in man calculated from venous insulin and C-peptide responses. J Clin Endocr Metab 63, 492-498.
    • (1986) J Clin Endocr Metab , vol.63 , pp. 492-498
    • Nauck, M.1    Homberger, E.2    Siegel, E.G.3
  • 16
    • 58149090676 scopus 로고    scopus 로고
    • The role of incretins in glucose homeostasis and diabetes treatment
    • Kim W & Egan JM (2008) The role of incretins in glucose homeostasis and diabetes treatment. Pharmacol Rev 60, 470-512.
    • (2008) Pharmacol Rev , vol.60 , pp. 470-512
    • Kim, W.1    Egan, J.M.2
  • 17
    • 0022617246 scopus 로고
    • Reduced incretin effect in type 2 (non-insulin-dependent) diabetes
    • Nauck M, Stöckmann F, Ebert R et al. (1986) Reduced incretin effect in type 2 (non-insulin-dependent) diabetes. Diabetologia 29, 46-52.
    • (1986) Diabetologia , vol.29 , pp. 46-52
    • Nauck, M.1    Stöckmann, F.2    Ebert, R.3
  • 18
    • 0001095690 scopus 로고    scopus 로고
    • Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients
    • Vilsbøll T, Krarup T, Deacon CF et al. (2001) Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients. Diabetes 50, 609-613.
    • (2001) Diabetes , vol.50 , pp. 609-613
    • Vilsbøll, T.1    Krarup, T.2    Deacon, C.F.3
  • 19
    • 0027419106 scopus 로고
    • Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations
    • Nauck MA, Bartels E, Orskov C et al. (1993) Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations. J Clin Endocr Metab 76, 912-917.
    • (1993) J Clin Endocr Metab , vol.76 , pp. 912-917
    • Nauck, M.A.1    Bartels, E.2    Orskov, C.3
  • 20
    • 0037234531 scopus 로고    scopus 로고
    • Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes
    • Drucker D (2003) Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes. Expert Opin Inv Drug 12, 87-100.
    • (2003) Expert Opin Inv Drug , vol.12 , pp. 87-100
    • Drucker, D.1
  • 21
    • 56449093424 scopus 로고    scopus 로고
    • Glucose sensing in L cells: A primary cell study
    • Reimann F, Habib AM, Tolhurst G et al. (2008) Glucose sensing in L cells: a primary cell study. Cell Metab 8, 532-539.
    • (2008) Cell Metab , vol.8 , pp. 532-539
    • Reimann, F.1    Habib, A.M.2    Tolhurst, G.3
  • 22
    • 0037321280 scopus 로고    scopus 로고
    • Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite
    • Hall WL, Millward DJ, Long SJ et al. (2003) Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite. Br J Nutr 89, 239-248.
    • (2003) Br J Nutr , vol.89 , pp. 239-248
    • Hall, W.L.1    Millward, D.J.2    Long, S.J.3
  • 23
    • 84893933737 scopus 로고    scopus 로고
    • A comparison of the insulinotropic and enterogastric response to ingestion of an equivalent quantity of maltodextran and whey protein
    • Power O, Conway C, McCormack W et al. (2011) A comparison of the insulinotropic and enterogastric response to ingestion of an equivalent quantity of maltodextran and whey protein. Proc Nutr Soc 70, E357.
    • (2011) Proc Nutr Soc , vol.70
    • Power, O.1    Conway, C.2    McCormack, W.3
  • 24
    • 70349755662 scopus 로고    scopus 로고
    • GLP-1 secretion is enhanced directly in the ileum but indirectly in the duodenum by a newly identified potent stimulator, zein hydrolysate, in rats
    • Hira T, Mochida T, Miyashita K et al. (2009) GLP-1 secretion is enhanced directly in the ileum but indirectly in the duodenum by a newly identified potent stimulator, zein hydrolysate, in rats. Am J Physiol Gastrointest Liver Physiol 297, G663-G671.
    • (2009) Am J Physiol Gastrointest Liver Physiol , vol.297
    • Hira, T.1    Mochida, T.2    Miyashita, K.3
  • 25
    • 84874040640 scopus 로고    scopus 로고
    • The GPRC6A receptor is involved in amino acid-induced glucagon-like peptide-1 secretion from GLUTag cells
    • Oya M, Kitaguchi T, Pais R et al. (2012) The GPRC6A receptor is involved in amino acid-induced glucagon-like peptide-1 secretion from GLUTag cells. J Biol Chem 288, 4513-4521.
    • (2012) J Biol Chem , vol.288 , pp. 4513-4521
    • Oya, M.1    Kitaguchi, T.2    Pais, R.3
  • 26
    • 5644240984 scopus 로고    scopus 로고
    • Glutamine potently stimulates glucagon-like peptide-1 secretion from GLUTag cells
    • Reimann F, Williams L, Silva Xavier G et al. (2004) Glutamine potently stimulates glucagon-like peptide-1 secretion from GLUTag cells. Diabetologia 47, 1592-1601.
    • (2004) Diabetologia , vol.47 , pp. 1592-1601
    • Reimann, F.1    Williams, L.2    Silva Xavier, G.3
  • 27
    • 79961244091 scopus 로고    scopus 로고
    • Incretin hormone and insulin responses to oral versus intravenous lipid administration in humans
    • Lindgren O, Carr RD, Deacon CF et al. (2011) Incretin hormone and insulin responses to oral versus intravenous lipid administration in humans. J Clin Endocr Metab 96, 2519-2524.
    • (2011) J Clin Endocr Metab , vol.96 , pp. 2519-2524
    • Lindgren, O.1    Carr, R.D.2    Deacon, C.F.3
  • 28
    • 0030031146 scopus 로고    scopus 로고
    • Gastric emptying and release of incretin hormones after glucose ingestion in humans
    • Schirra J, Katschinski M, Weidmann C et al. (1996) Gastric emptying and release of incretin hormones after glucose ingestion in humans. J Clin Invest 97, 92-103.
    • (1996) J Clin Invest , vol.97 , pp. 92-103
    • Schirra, J.1    Katschinski, M.2    Weidmann, C.3
  • 29
    • 0027215348 scopus 로고
    • Dipeptidyl-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 (1993) Dipeptidyl-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 214, 829-835.
    • (1993) Eur J Biochem , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 30
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • Holst JJ (2007) The physiology of glucagon-like peptide 1. Physiol Rev 87, 1409-1439.
    • (2007) Physiol Rev , vol.87 , pp. 1409-1439
    • Holst, J.J.1
  • 31
    • 0023638829 scopus 로고
    • Glucagon-like peptide 1 7-36: A physiological incretin in man
    • Kreymann B, Ghatei MA, Williams G et al. (1987) Glucagon-like peptide 1 7-36: a physiological incretin in man. Lancet 330, 1300-1304.
    • (1987) Lancet , vol.330 , pp. 1300-1304
    • Kreymann, B.1    Ghatei, M.A.2    Williams, G.3
  • 32
    • 0027533758 scopus 로고
    • Truncated GLP-1 (proglucagon 78-107-amide) inhibits gastric and pancreatic functions in man
    • Wettergren A, Schjoldager B, Mortensen PE et al. (1993) Truncated GLP-1 (proglucagon 78-107-amide) inhibits gastric and pancreatic functions in man. Digest Dis Sci 38, 665-673.
    • (1993) Digest Dis Sci , vol.38 , pp. 665-673
    • Wettergren, A.1    Schjoldager, B.2    Mortensen, P.E.3
  • 33
    • 0032871230 scopus 로고    scopus 로고
    • GLP-1 slows solid gastric emptying and inhibits insulin, glucagon, and PYY release in humans
    • N'slund E, Bogefors J, Skogar S et al. (1999) GLP-1 slows solid gastric emptying and inhibits insulin, glucagon, and PYY release in humans. Am J Physiol Regul Integr Comp Physiol 277, R910-R916.
    • (1999) Am J Physiol Regul Integr Comp Physiol , vol.277
    • Nslund, E.1    Bogefors, J.2    Skogar, S.3
  • 34
    • 0032005005 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 promotes satiety and suppresses energy intake in humans
    • Flint A, Raben A, Astrup A et al. (1998) Glucagon-like peptide 1 promotes satiety and suppresses energy intake in humans. J Clin Invest 101, 515-520.
    • (1998) J Clin Invest , vol.101 , pp. 515-520
    • Flint, A.1    Raben, A.2    Astrup, A.3
  • 35
    • 77949595748 scopus 로고    scopus 로고
    • Effects of meal size and composition on incretin, α-cell, and β-cell responses
    • Rijkelijkhuizen JM, McQuarrie K, Girman CJ et al. (2010) Effects of meal size and composition on incretin, α-cell, and β-cell responses. Metabolis 59, 502-511.
    • (2010) Metabolis , vol.59 , pp. 502-511
    • Rijkelijkhuizen, J.M.1    McQuarrie, K.2    Girman, C.J.3
  • 36
    • 34247880256 scopus 로고    scopus 로고
    • Activation of lipoprotein lipase by glucose-dependent insulinotropic polypeptide in adipocytes
    • Kim S-J, Nian C & McIntosh CHS (2007) Activation of lipoprotein lipase by glucose-dependent insulinotropic polypeptide in adipocytes. J Biol Chem 282, 8557-8567.
    • (2007) J Biol Chem , vol.282 , pp. 8557-8567
    • Kim, S.-J.1    Nian, C.2    McIntosh, C.H.S.3
  • 37
    • 0038121744 scopus 로고    scopus 로고
    • Both GLP-1 and GIP are insulinotropic at basal and postprandial glucose levels and contribute nearly equally to the incretin effect of a meal in healthy subjects
    • Vilsbøll T, Krarup T, Madsbad S et al. (2003) Both GLP-1 and GIP are insulinotropic at basal and postprandial glucose levels and contribute nearly equally to the incretin effect of a meal in healthy subjects. Regul Pept 114, 115-121.
    • (2003) Regul Pept , vol.114 , pp. 115-121
    • Vilsbøll, T.1    Krarup, T.2    Madsbad, S.3
  • 38
    • 3242730474 scopus 로고    scopus 로고
    • Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans
    • Holst JJ & Gromada J (2004) Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans. Am J Physiol Endo M 287, E199-E206.
    • (2004) Am J Physiol Endo M , vol.287
    • Holst, J.J.1    Gromada, J.2
  • 39
    • 0034612348 scopus 로고    scopus 로고
    • Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26
    • Marguet D, Baggio L, Kobayashi T et al. (2000) Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Proc Natl Acad Sci USA 97, 6874-6879.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6874-6879
    • Marguet, D.1    Baggio, L.2    Kobayashi, T.3
  • 40
    • 0037267892 scopus 로고    scopus 로고
    • Enteroinsular axis of db/db mice and efficacy of dipeptidyl peptidase IV inhibition
    • Nagakura T, Yasuda N, Yamazaki K et al. (2003) Enteroinsular axis of db/db mice and efficacy of dipeptidyl peptidase IV inhibition. Metabolis 52, 81-86.
    • (2003) Metabolis , vol.52 , pp. 81-86
    • Nagakura, T.1    Yasuda, N.2    Yamazaki, K.3
  • 41
    • 0037974604 scopus 로고    scopus 로고
    • Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance
    • Conarello SL, Li Z, Ronan J et al. (2003) Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance. Proc Natl Acad Sci USA 100, 6825-6830.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6825-6830
    • Conarello, S.L.1    Li, Z.2    Ronan, J.3
  • 42
    • 58149177392 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of vildagliptin in healthy chinese volunteers
    • Hu P, Yin Q, Deckert F et al. (2009) Pharmacokinetics and pharmacodynamics of vildagliptin in healthy chinese volunteers. J Clin Pharmacol 49, 39-49.
    • (2009) J Clin Pharmacol , vol.49 , pp. 39-49
    • Hu, P.1    Yin, Q.2    Deckert, F.3
  • 43
    • 2442482515 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase-IV reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes
    • Ahrén B, Landin-Olsson M, Jansson P-A et al. (2004) Inhibition of dipeptidyl peptidase-IV reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes. J Clin Endocr Metab 89, 2078-2084.
    • (2004) J Clin Endocr Metab , vol.89 , pp. 2078-2084
    • Ahrén, B.1    Landin-Olsson, M.2    Jansson, P.-A.3
  • 44
    • 76349097770 scopus 로고    scopus 로고
    • The dipeptidyl peptidase IV family in cancer and cell biology
    • Yu DMT, Yao T-W, Chowdhury S et al. (2010) The dipeptidyl peptidase IV family in cancer and cell biology. FEBS J 277, 1126-1144.
    • (2010) FEBS J , vol.277 , pp. 1126-1144
    • Dmt, Y.1    Yao, T.-W.2    Chowdhury, S.3
  • 45
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • Mentlein R (1999) Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul Pept 85, 9-24.
    • (1999) Regul Pept , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 46
    • 17144404555 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders
    • Gorrell MD (2005) Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clin Sci 108, 277-292.
    • (2005) Clin Sci , vol.108 , pp. 277-292
    • Gorrell, M.D.1
  • 47
    • 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 MG et al. (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci 13, 412-421.
    • (2004) Protein Sci , vol.13 , pp. 412-421
    • Aertgeerts, K.1    Ye, S.2    Tennant, M.G.3
  • 48
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen HB, Branner S, Wiberg FC et al. (2003) Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat Struct Mol Biol 10, 19-25.
    • (2003) Nat Struct Mol Biol , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3
  • 49
    • 79953713734 scopus 로고    scopus 로고
    • Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site
    • Kühn-Wache K, B'r JW, Hoffmann T et al. (2011) Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site. Biol Chem 392, 223-231.
    • (2011) Biol Chem , vol.392 , pp. 223-231
    • Kühn-Wache, K.1    Br, J.W.2    Hoffmann, T.3
  • 50
    • 0037787851 scopus 로고    scopus 로고
    • Dipeptidyl-Peptidase IV from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP IV
    • Lambeir A-M, Durinx C, Scharpé S et al. (2003) Dipeptidyl-Peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Crit Rev Clin Lab Sci 40, 209.
    • (2003) Crit Rev Clin Lab Sci , vol.40 , pp. 209
    • Lambeir, A.-M.1    Durinx, C.2    Scharpé, S.3
  • 51
    • 79960831855 scopus 로고    scopus 로고
    • Mechanisms of action of the dipeptidyl peptidase-4 inhibitor vildagliptin in humans
    • Ahrén B, Schweizer A, Dejager S et al. (2011) Mechanisms of action of the dipeptidyl peptidase-4 inhibitor vildagliptin in humans. Diabetes Obes Metab 13, 775-783.
    • (2011) Diabetes Obes Metab , vol.13 , pp. 775-783
    • Ahrén, B.1    Schweizer, A.2    Dejager, S.3
  • 52
    • 0025976294 scopus 로고
    • Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV'
    • Rahfeld J, Schierborn M, Hartrodt B et al. (1991) Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV' BBA-Protein Struct M 1076, 314-316.
    • (1991) BBA-Protein Struct M , vol.1076 , pp. 314-316
    • Rahfeld, J.1    Schierborn, M.2    Hartrodt, B.3
  • 53
    • 84860295841 scopus 로고    scopus 로고
    • Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran
    • Hatanaka T, Inoue Y, Arima J et al. (2012) Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chem 134, 797-802.
    • (2012) Food Chem , vol.134 , pp. 797-802
    • Hatanaka, T.1    Inoue, Y.2    Arima, J.3
  • 54
    • 64349093749 scopus 로고    scopus 로고
    • Covalent modifiers: An orthogonal approach to drug design
    • Potashman MH & Duggan ME (2009) Covalent modifiers: an orthogonal approach to drug design. J Med Chem 52, 1231-1246.
    • (2009) J Med Chem , vol.52 , pp. 1231-1246
    • Potashman, M.H.1    Duggan, M.E.2
  • 55
    • 84893942940 scopus 로고    scopus 로고
    • The present application relates to the secondary binding site of dipeptidyl peptidase IV, its relationship amongst substrates and to the modulation of substrate specificity of dipeptidyl peptidase IV
    • inventors; OSI Pharmaceuticals, Inc., assignee
    • Hoffmann T, Kuehn-Wache K, Demuth H-U et al. (2002) inventors; OSI Pharmaceuticals, Inc., assignee. The present application relates to the secondary binding site of dipeptidyl peptidase IV, its relationship amongst substrates and to the modulation of substrate specificity of dipeptidyl peptidase IV. United States US 2004/0058876 A1 (Patent).
    • (2002) United States US 2004/0058876 A1 (Patent)
    • Hoffmann, T.1    Kuehn-Wache, K.2    Demuth, H.-U.3
  • 56
    • 84866883091 scopus 로고    scopus 로고
    • Vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.)
    • Velarde-Salcedo AJ, Barrera-Pacheco A, Lara-González S et al. (2013) In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins. Food Chem 136, 758-764.
    • (2013) Proteins. Food Chem , vol.136 , pp. 758-764
    • Velarde-Salcedo, A.J.1    Barrera-Pacheco, A.2    Lara-González, S.3
  • 57
    • 0038531163 scopus 로고    scopus 로고
    • Different modes of dipeptidyl peptidase IV (CD26) inhibition by oligopeptides derived from the N-terminus of HIV-1 Tat indicate at least two inhibitor binding sites
    • Lorey S, Stöckel-Maschek A, Faust J et al. (2003) Different modes of dipeptidyl peptidase IV (CD26) inhibition by oligopeptides derived from the N-terminus of HIV-1 Tat indicate at least two inhibitor binding sites. Eur J Biochem 270, 2147-2156.
    • (2003) Eur J Biochem , vol.270 , pp. 2147-2156
    • Lorey, S.1    Stöckel-Maschek, A.2    Faust, J.3
  • 58
    • 58149132303 scopus 로고    scopus 로고
    • Biofunctional properties of bioactive peptides of milk origin
    • Haque E, Chand R & Kapila S (2009) Biofunctional properties of bioactive peptides of milk origin. Food Revs Int 25, 28-43.
    • (2009) Food Revs Int , vol.25 , pp. 28-43
    • Haque, E.1    Chand, R.2    Kapila, S.3
  • 59
    • 64549156088 scopus 로고    scopus 로고
    • Milk-derived bioactive peptides: From science to applications
    • Korhonen H (2009) Milk-derived bioactive peptides: From science to applications. J Funct Food 1, 177-187.
    • (2009) J Funct Food , vol.1 , pp. 177-187
    • Korhonen, H.1
  • 60
    • 84860318855 scopus 로고    scopus 로고
    • Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach
    • Lacroix IME & Li-Chan ECY (2012) Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J Funct Food 4, 403-422.
    • (2012) J Funct Food , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 61
    • 84856555742 scopus 로고    scopus 로고
    • Peptides derived from atlantic salmon skin gelatin as dipeptidylpeptidase IV inhibitors
    • Li-Chan ECY, Hunag S-L, Jao C-L et al. (2012) Peptides derived from atlantic salmon skin gelatin as dipeptidylpeptidase IV inhibitors. J Agric Food Chem 60, 973-978.
    • (2012) J Agric Food Chem , vol.60 , pp. 973-978
    • Li-Chan, E.C.Y.1    Hunag, S.-L.2    Jao, C.-L.3
  • 62
    • 84859788742 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates
    • Huang S-L, Jao C-L, Ho K-P et al. (2012) Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides 35, 114-121.
    • (2012) Peptides , vol.35 , pp. 114-121
    • Huang, S.-L.1    Jao, C.-L.2    Ho, K.-P.3
  • 63
    • 82655173852 scopus 로고    scopus 로고
    • Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats
    • Uenishi H, Kabuki T, Seto Y et al. (2012) Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. Int Dairy J 22, 24-30.
    • (2012) Int Dairy J , vol.22 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3
  • 64
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4 inhibiting peptide derived from betalactoglobulin
    • Uchida M, Ohshiba Y & Mogami O (2011) Novel dipeptidyl peptidase-4 inhibiting peptide derived from betalactoglobulin. J Pharmacol Sci 117, 63-66.
    • (2011) J Pharmacol Sci , vol.117 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 65
    • 79952799368 scopus 로고    scopus 로고
    • Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors
    • Tulipano G, Sibilia V, Caroli AM et al. (2011) Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 32, 835-838.
    • (2011) Peptides , vol.32 , pp. 835-838
    • Tulipano, G.1    Sibilia, V.2    Caroli, A.M.3
  • 66
    • 84878313919 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin
    • Silveira ST, Mart'nez-Maqueda D, Recio I et al. (2013) Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chem 141, 1072-1077.
    • (2013) Food Chem , vol.141 , pp. 1072-1077
    • Silveira, S.T.1    Martínez-Maqueda, D.2    Recio, I.3
  • 68
    • 40549134122 scopus 로고    scopus 로고
    • Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed
    • Silva-Sánchez C, de la Rosa APB, León-Galván MF et al. (2008) Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed. J Agric Food Chem 56, 1233-1240.
    • (2008) J Agric Food Chem , vol.56 , pp. 1233-1240
    • Silva-Sánchez, C.1    De La Rosa Apb2    León-Galván, M.F.3
  • 70
    • 69749111280 scopus 로고    scopus 로고
    • Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity
    • Foltz M, Van Buren L, KlaffkeWet al. (2009) Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity. J Food Sci 74, H243-H251.
    • (2009) J Food Sci , vol.74
    • Foltz, M.1    Van Buren, L.2    Klaffke, W.3
  • 71
    • 84884602268 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides
    • Nongonierma AB, Mooney C, Shields DC et al. (2013b) Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chem 141, 644-653.
    • (2013) Food Chem , vol.141 , pp. 644-653
    • Nongonierma, A.B.1    Mooney, C.2    Shields, D.C.3
  • 72
    • 0003955901 scopus 로고    scopus 로고
    • Proteins
    • 3rd ed. [P Fox & P McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • Fox P, McSweeney P (2003) Proteins. In Advanced Dairy Chemistry, 3rd ed., pp. 146-238 [P Fox & P McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers.
    • (2003) Advanced Dairy Chemistry , pp. 146-238
    • Fox, P.1    McSweeney, P.2
  • 73
    • 84893912697 scopus 로고    scopus 로고
    • Protein hydrolysates enriched in peptides inhibiting DPP IV and thier use
    • inventor Campina Nederland Holding B.V., assignee
    • Boots J (2006) inventor Campina Nederland Holding B.V., assignee. Protein hydrolysates enriched in peptides inhibiting DPP IV and thier use. WO 2006/068480 200 (Patent).
    • (2006) WO 2006/068480 200 (Patent)
    • Boots, J.1
  • 75
    • 0032240057 scopus 로고    scopus 로고
    • Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion
    • Abubakar A, Saito T, Kitazawa H et al. (1998) Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. J Diary Sci 81, 3131-3138.
    • (1998) J Diary Sci , vol.81 , pp. 3131-3138
    • Abubakar, A.1    Saito, T.2    Kitazawa, H.3
  • 76
    • 80054950510 scopus 로고    scopus 로고
    • Molecular dynamics simulations and drug discovery
    • Durrant J & McCammon JA (2011) Molecular dynamics simulations and drug discovery. BMC Bio 9, 71.
    • (2011) BMC Bio , vol.9 , pp. 71
    • Durrant, J.1    McCammon, J.A.2
  • 77
    • 34250643512 scopus 로고    scopus 로고
    • Docking and virtual screening of ACE inhibitory dipeptides
    • Pripp A (2007) Docking and virtual screening of ACE inhibitory dipeptides. Eur Food Res Technol 225, 589-592.
    • (2007) Eur Food Res Technol , vol.225 , pp. 589-592
    • Pripp, A.1
  • 78
    • 84859791745 scopus 로고    scopus 로고
    • Predictive modelling of angiotensin converting enzyme inhibitory dipeptides
    • Norris R, Casey F, FitzGerald RJ et al. (2012) Predictive modelling of angiotensin converting enzyme inhibitory dipeptides. Food Chem 133, 1349-1354.
    • (2012) Food Chem , vol.133 , pp. 1349-1354
    • Norris, R.1    Casey, F.2    Fitzgerald, R.J.3
  • 79
    • 48149099080 scopus 로고    scopus 로고
    • ASP4000, a novel, selective, dipeptidyl peptidase 4 inhibitor with antihyperglycemic activity
    • Tanaka-Amino K, Matsumoto K, Hatakeyama Y et al. (2008) ASP4000, a novel, selective, dipeptidyl peptidase 4 inhibitor with antihyperglycemic activity. Eur J Pharmacol 590, 444-449.
    • (2008) Eur J Pharmacol , vol.590 , pp. 444-449
    • Tanaka-Amino, K.1    Matsumoto, K.2    Hatakeyama, Y.3
  • 80
    • 77954572544 scopus 로고    scopus 로고
    • The corn protein, zein hydrolysate, administered into the ileum attenuates hyperglycemia via its dual action on glucagon-like peptide-1 secretion and dipeptidyl peptidase-IV activity in rats
    • Mochida T, Hira T & Hara H (2010) The corn protein, zein hydrolysate, administered into the ileum attenuates hyperglycemia via its dual action on glucagon-like peptide-1 secretion and dipeptidyl peptidase-IV activity in rats. Endocrinology 151, 3095-3104.
    • (2010) Endocrinology , vol.151 , pp. 3095-3104
    • Mochida, T.1    Hira, T.2    Hara, H.3
  • 81
    • 0036583164 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes
    • Ahrén B, Simonsson E, Larsson H et al. (2002) Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes. Diabetes Care 25, 869-875.
    • (2002) Diabetes Care , vol.25 , pp. 869-875
    • Ahrén, B.1    Simonsson, E.2    Larsson, H.3
  • 82
    • 9444285818 scopus 로고    scopus 로고
    • Twelve- and 52-week efficacy of the dipeptidyl peptidase IV Inhibitor LAF237 in metformin-treated patients with type 2 diabetes
    • Ahrén B, Gomis R, Standl E et al. (2004) Twelve- and 52-week efficacy of the dipeptidyl peptidase IV Inhibitor LAF237 in metformin-treated patients with type 2 diabetes. Diabetes Care 27, 2874-2880.
    • (2004) Diabetes Care , vol.27 , pp. 2874-2880
    • Ahrén, B.1    Gomis, R.2    Standl, E.3
  • 83
    • 17844374375 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV activity by oral metformin in Type 2 diabetes
    • Lindsay JR, Duffy NA, McKillop AM et al. (2005) Inhibition of dipeptidyl peptidase IV activity by oral metformin in Type 2 diabetes. Diabetic Med 22, 654-657.
    • (2005) Diabetic Med , vol.22 , pp. 654-657
    • Lindsay, J.R.1    Duffy, N.A.2    McKillop, A.M.3
  • 84
    • 34147133191 scopus 로고    scopus 로고
    • Metabolic effects of amino acid mixtures and whey protein in healthy subjects: Studies using glucose-equivalent drinks
    • Nilsson M, Holst JJ & Bjorck IME (2007) Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks. Am J Clin Nutr 85, 996-1004.
    • (2007) Am J Clin Nutr , vol.85 , pp. 996-1004
    • Nilsson, M.1    Holst, J.J.2    Bjorck, I.M.E.3
  • 85
    • 67650730250 scopus 로고    scopus 로고
    • Human insulinotropic response to oral ingestion of native and hydrolysed whey protein
    • Power O, Hallihan A & Jakeman P (2009) Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Amino Acids 37, 333-339.
    • (2009) Amino Acids , vol.37 , pp. 333-339
    • Power, O.1    Hallihan, A.2    Jakeman, P.3
  • 86
    • 0033949496 scopus 로고    scopus 로고
    • Plasma insulin response after ingestion of different amino acid or protein mixtures with carbohydrate
    • van Loon L, Saris W, Verhagen H et al. (2000) Plasma insulin response after ingestion of different amino acid or protein mixtures with carbohydrate. Am J Clin Nutr 72, 96-105.
    • (2000) Am J Clin Nutr , vol.72 , pp. 96-105
    • Van Loon, L.1    Saris, W.2    Verhagen, H.3
  • 87
    • 84877836950 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction
    • Nongonierma AB & FitzGerald RJ (2013c) Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction. Int Dairy J 32, 33-39.
    • (2013) Int Dairy J , vol.32 , pp. 33-39
    • Nongonierma, A.B.1    Fitzgerald, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.