Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes
The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous am...
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Published in | Proceedings of the Nutrition Society Vol. 73; no. 1; pp. 34 - 46 |
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Main Authors | , , , |
Format | Journal Article Conference Proceeding |
Language | English |
Published |
Cambridge, UK
Cambridge University Press
01.02.2014
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Subjects | |
Online Access | Get full text |
ISSN | 0029-6651 1475-2719 1475-2719 |
DOI | 10.1017/S0029665113003601 |
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Abstract | The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure–activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM. |
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AbstractList | The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure-activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM. [PUBLICATION ABSTRACT] The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure-activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM.The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure-activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM. The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure-activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM. |
Author | Power, Orla Jakeman, P. Nongonierma, A. B. FitzGerald, R. J. |
Author_xml | – sequence: 1 givenname: Orla surname: Power fullname: Power, Orla organization: Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland – sequence: 2 givenname: A. B. surname: Nongonierma fullname: Nongonierma, A. B. organization: Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland – sequence: 3 givenname: P. surname: Jakeman fullname: Jakeman, P. organization: Food for Health Ireland, University of Limerick, Castletroy, Limerick, Ireland – sequence: 4 givenname: R. J. surname: FitzGerald fullname: FitzGerald, R. J. email: dick.fitzgerald@ul.ie organization: Department of Life Sciences, University of Limerick, Castletroy, Limerick, Ireland |
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Cites_doi | 10.1016/j.peptides.2012.03.006 10.1016/j.peptides.2012.11.016 10.1016/S0140-6736(87)91194-9 10.1016/S0167-0115(99)00089-0 10.1016/S0168-8227(09)70008-7 10.1016/S0167-0115(03)00111-3 10.1016/j.idairyj.2011.08.002 10.1254/jphs.11089SC 10.1074/jbc.M112.402677 10.1053/meta.2003.50014 10.1016/j.cmet.2006.01.004 10.1016/j.ejphar.2008.05.034 10.1210/jcem-63-2-492 10.2337/diacare.25.5.869 10.1016/j.foodchem.2012.02.183 10.1110/ps.03460604 10.1016/j.jff.2012.01.008 10.1016/j.jff.2009.01.007 10.1210/jc.2011-0266 10.1079/BJN2002760 10.1177/0091270008325152 10.1007/s00217-006-0450-6 10.1021/jf072911z 10.1016/j.foodchem.2012.02.023 10.1080/713609354 10.1111/j.1463-1326.2011.01414.x 10.1093/ajcn/85.4.996 10.1007/978-1-4419-8602-3_20 10.2337/diabetes.50.3.609 10.1021/jm8008597 10.1111/j.1464-5491.2005.01461.x 10.1016/j.foodchem.2013.02.115 10.2337/dc09-S013 10.1080/87559120802458198 10.1172/JCI105685 10.1172/JCI990 10.1046/j.1432-1033.2003.03568.x 10.1124/pr.108.000604 10.1016/j.idairyj.2012.01.003 10.1016/j.idairyj.2013.03.005 10.1073/pnas.0631828100 10.1007/BF02427280 10.1172/JCI118411 10.1186/1741-7007-9-71 10.1210/jc.2003-031907 10.1007/BF01316798 10.1111/j.1742-4658.2009.07526.x 10.1210/en.2009-1510 10.1016/0167-4838(91)90284-7 10.1074/jbc.M609088200 10.1073/pnas.120069197 10.1007/s00726-008-0156-0 10.1111/j.1750-3841.2009.01301.x 10.1093/ajcn/72.1.96 10.1007/s00125-004-1498-0 10.1152/ajpregu.1999.277.3.R910 10.2337/diacare.27.12.2874 10.1016/j.foodchem.2013.03.056 10.1111/j.1432-1033.1993.tb17986.x 10.1016/j.foodchem.2012.08.032 10.2337/dc07-0228 10.3168/jds.S0022-0302(98)75878-3 10.1042/CS20040302 10.1093/ajcn/82.1.76 10.2174/138161207780363068 10.1016/j.metabol.2009.07.039 10.1517/13543784.12.1.87 10.1515/bc.2011.028 10.1016/j.peptides.2011.01.002 10.1017/S0029665111004423 10.1152/ajpgi.90635.2008 10.1021/jf204720q 10.1002/jbt.10058 10.1038/nsb882 10.1152/physrev.00034.2006 10.1016/j.cmet.2008.11.002 10.1093/ajcn/82.1.69 |
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Keywords | Milk protein Glucose-dependent insulinotropic polypeptide Hydrolysate Dipeptidyl peptidase IV inhibition Functional foods Bioactive peptide Glucagon like peptide-1 Type 2 diabetes mellitus Endocrinopathy Type 2 diabetes Enzyme Metabolic diseases Glucagon like peptide 1 Peptidases Gastrointestinal hormone Health food Hydrolases Inhibition Gastric inhibitory peptide |
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References | Nagakura, Yasuda, Yamazaki (40) 2003; 52 Lorey, Stöckel-Maschek, Faust (57) 2003; 270 Norris, Casey, FitzGerald (78) 2012; 133 Lindgren, Carr, Deacon (27) 2011; 96 Holst (30) 2007; 87 Lindsay, Duffy, McKillop (83) 2005; 22 Nilsson, Holst, Bjorck (84) 2007; 85 Holst, Gromada (38) 2004; 287 Kim, Egan (16) 2008; 60 Maritim, Sanders, Watkins (74) 2003; 17 Mentlein, Gallwitz, Schmidt (29) 1993; 214 van Loon, Saris, Verhagen (86) 2000; 72 Wettergren, Schjoldager, Mortensen (32) 1993; 38 (7) 2009; 32 Näslund, Bogefors, Skogar (33) 1999; 277 Tanaka-Amino, Matsumoto, Hatakeyama (79) 2008; 590 Conarello, Li, Ronan (41) 2003; 100 Aertgeerts, Ye, Tennant (47) 2004; 13 Power, Hallihan, Jakeman (85) 2009; 37 Ahrén, Landin-Olsson, Jansson (43) 2004; 89 Manders, Wagenmakers, Koopman (11) 2005; 82 Uenishi, Kabuki, Seto (63) 2012; 22 Schirra, Katschinski, Weidmann (28) 1996; 97 Ben-Avraham, Harman-Boehm, Schwarzfuchs (2) 2009; 86 Lacroix, Li-Chan (60) 2012; 4 Durrant, McCammon (76) 2011; 9 Gorrell (46) 2005; 108 Huang, Jao, Ho (62) 2012; 35 Silveira, Martínez-Maqueda, Recio (66) 2013; 141 Oya, Kitaguchi, Pais (25) 2012; 288 Drucker (20) 2003; 12 Hu, Yin, Deckert (42) 2009; 49 Lambeir, Durinx, Scharpé (50) 2003; 40 Pripp (77) 2007; 225 Krushner, Gorrell (6) 2010; 59 Nauck, Homberger, Siegel (15) 1986; 63 Hall, Millward, Long (22) 2003; 89 Nauck, Bartels, Orskov (19) 1993; 76 Lacroix, Li-Chan (12) 2012; 25 Foltz, Van Buren, Klaffke (70) 2009; 74 Drucker (3) 2006; 3 Potashman, Duggan (54) 2009; 52 Kreymann, Ghatei, Williams (31) 1987; 330 Flint, Raben, Astrup (34) 1998; 101 Kim, Nian, McIntosh (36) 2007; 282 Silva-Sánchez, de la Rosa, León-Galván (68) 2008; 56 Rahfeld, Schierborn, Hartrodt (52) 1991; 1076 Ahrén, Gomis, Standl (82) 2004; 27 Nauck, Stöckmann, Ebert (17) 1986; 29 Vilsbøll, Krarup, Madsbad (37) 2003; 114 Yu, Yao, Chowdhury (44) 2010; 277 Mentlein (45) 1999; 85 Li-Chan, Hunag, Jao (61) 2012; 60 Mochida, Hira, Hara (80) 2010; 151 Haque, Chand, Kapila (58) 2009; 25 Drucker (4) 2007; 30 Hatanaka, Inoue, Arima (53) 2012; 134 Nongonierma, FitzGerald (87) 2013; 32 Reimann, Williams, Silva Xavier (26) 2004; 47 Rasmussen, Branner, Wiberg (48) 2003; 10 Rijkelijkhuizen, McQuarrie, Girman (35) 2010; 59 Reimann, Habib, Tolhurst (21) 2008; 8 Ahrén, Schweizer, Dejager (51) 2011; 13 Marguet, Baggio, Kobayashi (39) 2000; 97 Korhonen (59) 2009; 1 Vilsbøll, Krarup, Deacon (18) 2001; 50 Hira, Mochida, Miyashita (24) 2009; 297 Nongonierma, Mooney, Shields (71) 2013; 141 Uchida, Ohshiba, Mogami (64) 2011; 117 Nongonierma, FitzGerald (13) 2013; 39 Kühn-Wache, Bär, Hoffmann (49) 2011; 392 Murray, FitzGerald (9) 2007; 13 Gupta, Kalra (5) 2011; 15 Perley, Kipnis (14) 1967; 46 Abubakar, Saito, Kitazawa (75) 1998; 81 Frid, Nilsson, Holst (10) 2005; 82 Power, Conway, McCormack (23) 2011; 70 Velarde-Salcedo, Barrera-Pacheco, Lara-González (56) 2013; 136 Ahrén, Simonsson, Larsson (81) 2002; 25 Tulipano, Sibilia, Caroli (65) 2011; 32 Holst (S0029665113003601_ref38) 2004; 287 S0029665113003601_ref23 S0029665113003601_ref66 S0029665113003601_ref22 S0029665113003601_ref25 S0029665113003601_ref68 S0029665113003601_ref24 S0029665113003601_ref27 S0029665113003601_ref26 S0029665113003601_ref29 S0029665113003601_ref28 S0029665113003601_ref61 S0029665113003601_ref60 Fox (S0029665113003601_ref72) 2003 S0029665113003601_ref63 S0029665113003601_ref62 S0029665113003601_ref21 S0029665113003601_ref65 S0029665113003601_ref20 S0029665113003601_ref64 cr-split#-S0029665113003601_ref55.1 cr-split#-S0029665113003601_ref55.2 Gupta (S0029665113003601_ref5) 2011; 15 S0029665113003601_ref78 S0029665113003601_ref34 S0029665113003601_ref33 S0029665113003601_ref77 S0029665113003601_ref36 S0029665113003601_ref79 S0029665113003601_ref35 S0029665113003601_ref37 S0029665113003601_ref39 S0029665113003601_ref70 S0029665113003601_ref7 S0029665113003601_ref4 S0029665113003601_ref71 S0029665113003601_ref30 S0029665113003601_ref3 S0029665113003601_ref74 S0029665113003601_ref73 S0029665113003601_ref2 Krushner (S0029665113003601_ref6) 2010; 59 S0029665113003601_ref1 S0029665113003601_ref76 S0029665113003601_ref32 S0029665113003601_ref31 S0029665113003601_ref75 van Loon (S0029665113003601_ref86) 2000; 72 S0029665113003601_ref9 S0029665113003601_ref8 cr-split#-S0029665113003601_ref67.1 cr-split#-S0029665113003601_ref67.2 Nauck (S0029665113003601_ref19) 1993; 76 S0029665113003601_ref45 S0029665113003601_ref44 S0029665113003601_ref47 S0029665113003601_ref46 S0029665113003601_ref49 S0029665113003601_ref48 S0029665113003601_ref81 S0029665113003601_ref80 S0029665113003601_ref83 S0029665113003601_ref82 S0029665113003601_ref85 S0029665113003601_ref41 S0029665113003601_ref40 S0029665113003601_ref84 S0029665113003601_ref43 S0029665113003601_ref87 S0029665113003601_ref42 cr-split#-S0029665113003601_ref69.1 cr-split#-S0029665113003601_ref69.2 S0029665113003601_ref12 S0029665113003601_ref56 S0029665113003601_ref11 S0029665113003601_ref58 S0029665113003601_ref14 S0029665113003601_ref57 S0029665113003601_ref13 S0029665113003601_ref16 S0029665113003601_ref15 S0029665113003601_ref59 S0029665113003601_ref18 S0029665113003601_ref17 S0029665113003601_ref50 S0029665113003601_ref52 S0029665113003601_ref51 S0029665113003601_ref54 S0029665113003601_ref10 S0029665113003601_ref53 |
References_xml | – volume: 86 start-page: S41 year: 2009 end-page: S48 ident: 2 article-title: 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) publication-title: Diabetes Res Clin Pract – volume: 100 start-page: 6825 year: 2003 end-page: 6830 ident: 41 article-title: Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance publication-title: Proc Natl Acad Sci USA – volume: 32 start-page: S13 year: 2009 end-page: S61 ident: 7 article-title: Standards of medical care in diabetes—2009 publication-title: Diabetes Care – volume: 85 start-page: 9 year: 1999 end-page: 24 ident: 45 article-title: Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides publication-title: Regul Pept – volume: 56 start-page: 1233 year: 2008 end-page: 1240 ident: 68 article-title: Bioactive peptides in amaranth (Amaranthus hypochondriacus) seed publication-title: J Agric Food Chem – volume: 39 start-page: 157 year: 2013 end-page: 163 ident: 13 article-title: Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates publication-title: Peptides – volume: 81 start-page: 3131 year: 1998 end-page: 3138 ident: 75 article-title: Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion publication-title: J Diary Sci – volume: 225 start-page: 589 year: 2007 end-page: 592 ident: 77 article-title: Docking and virtual screening of ACE inhibitory dipeptides publication-title: Eur Food Res Technol – volume: 46 start-page: 1954 year: 1967 end-page: 1962 ident: 14 article-title: Plasma insulin responses to oral and intravenous glucose: studies in normal and diabetic subjects publication-title: J Clin Invest – volume: 29 start-page: 46 year: 1986 end-page: 52 ident: 17 article-title: Reduced incretin effect in type 2 (non-insulin-dependent) diabetes publication-title: Diabetologia – volume: 52 start-page: 81 year: 2003 end-page: 86 ident: 40 article-title: Enteroinsular axis of db/db mice and efficacy of dipeptidyl peptidase IV inhibition publication-title: Metabolis – volume: 40 start-page: 209 year: 2003 ident: 50 article-title: Dipeptidyl-Peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV publication-title: Crit Rev Clin Lab Sci – volume: 117 start-page: 63 year: 2011 end-page: 66 ident: 64 article-title: Novel dipeptidyl peptidase-4 inhibiting peptide derived from beta-lactoglobulin publication-title: J Pharmacol Sci – volume: 59 start-page: 2 year: 2010 ident: 6 article-title: DPP-4 inhibitors in type 2 diabetes: importance of selective enzyme inhibition and implications for clinical use publication-title: J Fam Pract – volume: 282 start-page: 8557 year: 2007 end-page: 8567 ident: 36 article-title: Activation of lipoprotein lipase by glucose-dependent insulinotropic polypeptide in adipocytes publication-title: J Biol Chem – volume: 3 start-page: 153 year: 2006 end-page: 165 ident: 3 article-title: The biology of incretin hormones publication-title: Cell Metab – volume: 15 start-page: 298 year: 2011 end-page: 308 ident: 5 article-title: Choosing a gliptin publication-title: Indian J Endo Metab – volume: 60 start-page: 470 year: 2008 end-page: 512 ident: 16 article-title: The role of incretins in glucose homeostasis and diabetes treatment publication-title: Pharmacol Rev – volume: 37 start-page: 333 year: 2009 end-page: 339 ident: 85 article-title: Human insulinotropic response to oral ingestion of native and hydrolysed whey protein publication-title: Amino Acids – volume: 133 start-page: 1349 year: 2012 end-page: 1354 ident: 78 article-title: Predictive modelling of angiotensin converting enzyme inhibitory dipeptides publication-title: Food Chem – volume: 136 start-page: 758 year: 2013 end-page: 764 ident: 56 article-title: In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins publication-title: Food Chem – volume: 270 start-page: 2147 year: 2003 end-page: 2156 ident: 57 article-title: 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 publication-title: Eur J Biochem – volume: 13 start-page: 773 year: 2007 end-page: 791 ident: 9 article-title: Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production publication-title: Curr Pharm Des – volume: 108 start-page: 277 year: 2005 end-page: 292 ident: 46 article-title: Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders publication-title: Clin Sci – volume: 8 start-page: 532 year: 2008 end-page: 539 ident: 21 article-title: Glucose sensing in L cells: a primary cell study publication-title: Cell Metab – volume: 89 start-page: 239 year: 2003 end-page: 248 ident: 22 article-title: Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite publication-title: Br J Nutr – volume: 13 start-page: 412 year: 2004 end-page: 421 ident: 47 article-title: Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation publication-title: Protein Sci – volume: 76 start-page: 912 year: 1993 end-page: 917 ident: 19 article-title: 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 publication-title: J Clin Endocr Metab – volume: 1076 start-page: 314 year: 1991 end-page: 316 ident: 52 article-title: Are diprotin A (Ile-Pro-Ile) and diprotin B (Val–Pro–Leu) inhibitors or substrates of dipeptidyl peptidase IV? publication-title: BBA-Protein Struct M – volume: 114 start-page: 115 year: 2003 end-page: 121 ident: 37 article-title: 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 publication-title: Regul Pept – volume: 32 start-page: 835 year: 2011 end-page: 838 ident: 65 article-title: Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors publication-title: Peptides – volume: 13 start-page: 775 year: 2011 end-page: 783 ident: 51 article-title: Mechanisms of action of the dipeptidyl peptidase-4 inhibitor vildagliptin in humans publication-title: Diabetes Obes Metab – volume: 101 start-page: 515 year: 1998 end-page: 520 ident: 34 article-title: Glucagon-like peptide 1 promotes satiety and suppresses energy intake in humans publication-title: J Clin Invest – volume: 288 start-page: 4513 year: 2012 end-page: 4521 ident: 25 article-title: The GPRC6A receptor is involved in amino acid-induced glucagon-like peptide-1 secretion from GLUTag cells publication-title: J Biol Chem – volume: 22 start-page: 654 year: 2005 end-page: 657 ident: 83 article-title: Inhibition of dipeptidyl peptidase IV activity by oral metformin in Type 2 diabetes publication-title: Diabetic Med – volume: 50 start-page: 609 year: 2001 end-page: 613 ident: 18 article-title: Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients publication-title: Diabetes – volume: 38 start-page: 665 year: 1993 end-page: 673 ident: 32 article-title: Truncated GLP-1 (proglucagon 78–107-amide) inhibits gastric and pancreatic functions in man publication-title: Digest Dis Sci – volume: 49 start-page: 39 year: 2009 end-page: 49 ident: 42 article-title: Pharmacokinetics and pharmacodynamics of vildagliptin in healthy chinese volunteers publication-title: J Clin Pharmacol – volume: 52 start-page: 1231 year: 2009 end-page: 1246 ident: 54 article-title: Covalent modifiers: an orthogonal approach to drug design publication-title: J Med Chem – volume: 82 start-page: 76 year: 2005 end-page: 83 ident: 11 article-title: Co-ingestion of a protein hydrolysate and amino acid mixture with carbohydrate improves plasma glucose disposal in patients with type 2 diabetes publication-title: Am J Clin Nutr – volume: 17 start-page: 24 year: 2003 end-page: 38 ident: 74 article-title: Diabetes, oxidative stress, and antioxidants: a review publication-title: J Biochem Mol Toxic – volume: 151 start-page: 3095 year: 2010 end-page: 3104 ident: 80 article-title: 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 publication-title: Endocrinology – volume: 30 start-page: 1335 year: 2007 end-page: 1343 ident: 4 article-title: Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes publication-title: Diabetes Care – volume: 97 start-page: 92 year: 1996 end-page: 103 ident: 28 article-title: Gastric emptying and release of incretin hormones after glucose ingestion in humans publication-title: J Clin Invest – volume: 89 start-page: 2078 year: 2004 end-page: 2084 ident: 43 article-title: Inhibition of dipeptidyl peptidase-IV reduces glycemia, sustains insulin levels, and reduces glucagon levels in type 2 diabetes publication-title: J Clin Endocr Metab – volume: 297 start-page: G663 year: 2009 end-page: G671 ident: 24 article-title: GLP-1 secretion is enhanced directly in the ileum but indirectly in the duodenum by a newly identified potent stimulator, zein hydrolysate, in rats publication-title: Am J Physiol Gastrointest Liver Physiol – volume: 287 start-page: E199 year: 2004 end-page: E206 ident: 38 article-title: Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans publication-title: Am J Physiol Endo M – volume: 10 start-page: 19 year: 2003 end-page: 25 ident: 48 article-title: Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog publication-title: Nat Struct Mol Biol – volume: 12 start-page: 87 year: 2003 end-page: 100 ident: 20 article-title: Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes publication-title: Expert Opin Inv Drug – volume: 96 start-page: 2519 year: 2011 end-page: 2524 ident: 27 article-title: Incretin hormone and insulin responses to oral versus intravenous lipid administration in humans publication-title: J Clin Endocr Metab – volume: 59 start-page: 502 year: 2010 end-page: 511 ident: 35 article-title: Effects of meal size and composition on incretin, α-cell, and β-cell responses publication-title: Metabolis – volume: 277 start-page: 1126 year: 2010 end-page: 1144 ident: 44 article-title: The dipeptidyl peptidase IV family in cancer and cell biology publication-title: FEBS J – volume: 25 start-page: 869 year: 2002 end-page: 875 ident: 81 article-title: Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes publication-title: Diabetes Care – volume: 74 start-page: H243 year: 2009 end-page: H251 ident: 70 article-title: Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity publication-title: J Food Sci – volume: 47 start-page: 1592 year: 2004 end-page: 1601 ident: 26 article-title: Glutamine potently stimulates glucagon-like peptide-1 secretion from GLUTag cells publication-title: Diabetologia – volume: 141 start-page: 644 year: 2013 end-page: 653 ident: 71 article-title: Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides publication-title: Food Chem – volume: 25 start-page: 97 year: 2012 end-page: 102 ident: 12 article-title: Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates publication-title: Int Dairy J – volume: 330 start-page: 1300 year: 1987 end-page: 1304 ident: 31 article-title: Glucagon-like peptide 1 7–36: a physiological incretin in man publication-title: Lancet – volume: 277 start-page: R910 year: 1999 end-page: R916 ident: 33 article-title: GLP-1 slows solid gastric emptying and inhibits insulin, glucagon, and PYY release in humans publication-title: Am J Physiol Regul Integr Comp Physiol – volume: 25 start-page: 28 year: 2009 end-page: 43 ident: 58 article-title: Biofunctional properties of bioactive peptides of milk origin publication-title: Food Revs Int – volume: 97 start-page: 6874 year: 2000 end-page: 6879 ident: 39 article-title: Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26 publication-title: Proc Natl Acad Sci USA – volume: 590 start-page: 444 year: 2008 end-page: 449 ident: 79 article-title: ASP4000, a novel, selective, dipeptidyl peptidase 4 inhibitor with antihyperglycemic activity publication-title: Eur J Pharmacol – volume: 82 start-page: 69 year: 2005 end-page: 75 ident: 10 article-title: Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects publication-title: Am J Clin Nutr – volume: 9 start-page: 71 year: 2011 ident: 76 article-title: Molecular dynamics simulations and drug discovery publication-title: BMC Bio – volume: 63 start-page: 492 year: 1986 end-page: 498 ident: 15 article-title: Incretin effects of increasing glucose loads in man calculated from venous insulin and C-peptide responses publication-title: J Clin Endocr Metab – volume: 72 start-page: 96 year: 2000 end-page: 105 ident: 86 article-title: Plasma insulin response after ingestion of different amino acid or protein mixtures with carbohydrate publication-title: Am J Clin Nutr – volume: 392 start-page: 223 year: 2011 end-page: 231 ident: 49 article-title: Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site publication-title: Biol Chem – volume: 134 start-page: 797 year: 2012 end-page: 802 ident: 53 article-title: Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran publication-title: Food Chem – volume: 27 start-page: 2874 year: 2004 end-page: 2880 ident: 82 article-title: Twelve- and 52-week efficacy of the dipeptidyl peptidase IV Inhibitor LAF237 in metformin-treated patients with type 2 diabetes publication-title: Diabetes Care – volume: 22 start-page: 24 year: 2012 end-page: 30 ident: 63 article-title: 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 publication-title: Int Dairy J – volume: 32 start-page: 33 year: 2013 end-page: 39 ident: 87 article-title: Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction publication-title: Int Dairy J – volume: 1 start-page: 177 year: 2009 end-page: 187 ident: 59 article-title: Milk-derived bioactive peptides: From science to applications publication-title: J Funct Food – volume: 87 start-page: 1409 year: 2007 end-page: 1439 ident: 30 article-title: The physiology of glucagon-like peptide 1 publication-title: Physiol Rev – volume: 141 start-page: 1072 year: 2013 end-page: 1077 ident: 66 article-title: Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin publication-title: Food Chem – volume: 60 start-page: 973 year: 2012 end-page: 978 ident: 61 article-title: Peptides derived from atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors publication-title: J Agric Food Chem – volume: 35 start-page: 114 year: 2012 end-page: 121 ident: 62 article-title: Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates publication-title: Peptides – volume: 85 start-page: 996 year: 2007 end-page: 1004 ident: 84 article-title: Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks publication-title: Am J Clin Nutr – volume: 4 start-page: 403 year: 2012 end-page: 422 ident: 60 article-title: Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach publication-title: J Funct Food – volume: 214 start-page: 829 year: 1993 end-page: 835 ident: 29 article-title: 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 publication-title: Eur J Biochem – volume: 70 start-page: E357 year: 2011 ident: 23 article-title: A comparison of the insulinotropic and enterogastric response to ingestion of an equivalent quantity of maltodextran and whey protein publication-title: Proc Nutr Soc – start-page: 146 volume-title: Advanced Dairy Chemistry year: 2003 ident: S0029665113003601_ref72 – ident: S0029665113003601_ref62 doi: 10.1016/j.peptides.2012.03.006 – ident: S0029665113003601_ref13 doi: 10.1016/j.peptides.2012.11.016 – ident: S0029665113003601_ref31 doi: 10.1016/S0140-6736(87)91194-9 – ident: S0029665113003601_ref45 doi: 10.1016/S0167-0115(99)00089-0 – ident: S0029665113003601_ref2 doi: 10.1016/S0168-8227(09)70008-7 – ident: S0029665113003601_ref37 doi: 10.1016/S0167-0115(03)00111-3 – ident: S0029665113003601_ref63 doi: 10.1016/j.idairyj.2011.08.002 – ident: S0029665113003601_ref64 doi: 10.1254/jphs.11089SC – ident: S0029665113003601_ref25 doi: 10.1074/jbc.M112.402677 – ident: #cr-split#-S0029665113003601_ref67.2 – volume: 15 start-page: 298 year: 2011 ident: S0029665113003601_ref5 article-title: Choosing a gliptin publication-title: Indian J Endo Metab – ident: S0029665113003601_ref40 doi: 10.1053/meta.2003.50014 – ident: S0029665113003601_ref3 doi: 10.1016/j.cmet.2006.01.004 – ident: S0029665113003601_ref79 doi: 10.1016/j.ejphar.2008.05.034 – ident: S0029665113003601_ref15 doi: 10.1210/jcem-63-2-492 – ident: S0029665113003601_ref81 doi: 10.2337/diacare.25.5.869 – ident: S0029665113003601_ref73 – ident: S0029665113003601_ref53 doi: 10.1016/j.foodchem.2012.02.183 – ident: S0029665113003601_ref47 doi: 10.1110/ps.03460604 – volume: 287 start-page: E199 year: 2004 ident: S0029665113003601_ref38 article-title: Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans publication-title: Am J Physiol Endo M – ident: S0029665113003601_ref60 doi: 10.1016/j.jff.2012.01.008 – ident: S0029665113003601_ref59 doi: 10.1016/j.jff.2009.01.007 – ident: S0029665113003601_ref27 doi: 10.1210/jc.2011-0266 – ident: S0029665113003601_ref22 doi: 10.1079/BJN2002760 – volume: 59 start-page: 2 year: 2010 ident: S0029665113003601_ref6 article-title: DPP-4 inhibitors in type 2 diabetes: importance of selective enzyme inhibition and implications for clinical use publication-title: J Fam Pract – ident: S0029665113003601_ref42 doi: 10.1177/0091270008325152 – ident: S0029665113003601_ref77 doi: 10.1007/s00217-006-0450-6 – ident: S0029665113003601_ref68 doi: 10.1021/jf072911z – ident: #cr-split#-S0029665113003601_ref69.2 – ident: S0029665113003601_ref78 doi: 10.1016/j.foodchem.2012.02.023 – ident: S0029665113003601_ref50 doi: 10.1080/713609354 – ident: S0029665113003601_ref51 doi: 10.1111/j.1463-1326.2011.01414.x – volume: 76 start-page: 912 year: 1993 ident: S0029665113003601_ref19 article-title: 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 publication-title: J Clin Endocr Metab – ident: S0029665113003601_ref84 doi: 10.1093/ajcn/85.4.996 – ident: S0029665113003601_ref8 doi: 10.1007/978-1-4419-8602-3_20 – ident: S0029665113003601_ref18 doi: 10.2337/diabetes.50.3.609 – ident: S0029665113003601_ref54 doi: 10.1021/jm8008597 – ident: S0029665113003601_ref83 doi: 10.1111/j.1464-5491.2005.01461.x – ident: #cr-split#-S0029665113003601_ref67.1 – ident: S0029665113003601_ref71 doi: 10.1016/j.foodchem.2013.02.115 – ident: S0029665113003601_ref7 doi: 10.2337/dc09-S013 – ident: S0029665113003601_ref58 doi: 10.1080/87559120802458198 – ident: S0029665113003601_ref14 doi: 10.1172/JCI105685 – ident: S0029665113003601_ref34 doi: 10.1172/JCI990 – ident: S0029665113003601_ref57 doi: 10.1046/j.1432-1033.2003.03568.x – ident: S0029665113003601_ref16 doi: 10.1124/pr.108.000604 – ident: S0029665113003601_ref12 doi: 10.1016/j.idairyj.2012.01.003 – ident: S0029665113003601_ref87 doi: 10.1016/j.idairyj.2013.03.005 – ident: S0029665113003601_ref41 doi: 10.1073/pnas.0631828100 – ident: S0029665113003601_ref17 doi: 10.1007/BF02427280 – ident: S0029665113003601_ref28 doi: 10.1172/JCI118411 – ident: S0029665113003601_ref76 doi: 10.1186/1741-7007-9-71 – ident: S0029665113003601_ref43 doi: 10.1210/jc.2003-031907 – ident: #cr-split#-S0029665113003601_ref55.2 – ident: S0029665113003601_ref32 doi: 10.1007/BF01316798 – ident: S0029665113003601_ref44 doi: 10.1111/j.1742-4658.2009.07526.x – ident: S0029665113003601_ref80 doi: 10.1210/en.2009-1510 – ident: S0029665113003601_ref52 doi: 10.1016/0167-4838(91)90284-7 – ident: S0029665113003601_ref36 doi: 10.1074/jbc.M609088200 – ident: S0029665113003601_ref39 doi: 10.1073/pnas.120069197 – ident: S0029665113003601_ref85 doi: 10.1007/s00726-008-0156-0 – ident: S0029665113003601_ref70 doi: 10.1111/j.1750-3841.2009.01301.x – volume: 72 start-page: 96 year: 2000 ident: S0029665113003601_ref86 article-title: Plasma insulin response after ingestion of different amino acid or protein mixtures with carbohydrate publication-title: Am J Clin Nutr doi: 10.1093/ajcn/72.1.96 – ident: S0029665113003601_ref26 doi: 10.1007/s00125-004-1498-0 – ident: S0029665113003601_ref33 doi: 10.1152/ajpregu.1999.277.3.R910 – ident: S0029665113003601_ref82 doi: 10.2337/diacare.27.12.2874 – ident: S0029665113003601_ref66 doi: 10.1016/j.foodchem.2013.03.056 – ident: S0029665113003601_ref29 doi: 10.1111/j.1432-1033.1993.tb17986.x – ident: S0029665113003601_ref56 doi: 10.1016/j.foodchem.2012.08.032 – ident: S0029665113003601_ref4 doi: 10.2337/dc07-0228 – ident: S0029665113003601_ref75 doi: 10.3168/jds.S0022-0302(98)75878-3 – ident: S0029665113003601_ref46 doi: 10.1042/CS20040302 – ident: S0029665113003601_ref11 doi: 10.1093/ajcn/82.1.76 – ident: #cr-split#-S0029665113003601_ref69.1 – ident: S0029665113003601_ref9 doi: 10.2174/138161207780363068 – ident: S0029665113003601_ref35 doi: 10.1016/j.metabol.2009.07.039 – ident: #cr-split#-S0029665113003601_ref55.1 – ident: S0029665113003601_ref20 doi: 10.1517/13543784.12.1.87 – ident: S0029665113003601_ref49 doi: 10.1515/bc.2011.028 – ident: S0029665113003601_ref65 doi: 10.1016/j.peptides.2011.01.002 – ident: S0029665113003601_ref1 – ident: S0029665113003601_ref23 doi: 10.1017/S0029665111004423 – ident: S0029665113003601_ref24 doi: 10.1152/ajpgi.90635.2008 – ident: S0029665113003601_ref61 doi: 10.1021/jf204720q – ident: S0029665113003601_ref74 doi: 10.1002/jbt.10058 – ident: S0029665113003601_ref48 doi: 10.1038/nsb882 – ident: S0029665113003601_ref30 doi: 10.1152/physrev.00034.2006 – ident: S0029665113003601_ref21 doi: 10.1016/j.cmet.2008.11.002 – ident: S0029665113003601_ref10 doi: 10.1093/ajcn/82.1.69 |
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Snippet | The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this... |
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SubjectTerms | Amino acids Animals Biological and medical sciences blood glucose Blood Glucose - metabolism Diabetes Diabetes Mellitus, Type 2 - blood Diabetes Mellitus, Type 2 - diet therapy Diabetes Mellitus, Type 2 - drug therapy Diabetes. Impaired glucose tolerance Dietary Proteins - therapeutic use Dipeptidyl Peptidase 4 - blood dipeptidyl-peptidase IV Dipeptidyl-Peptidase IV Inhibitors - therapeutic use drugs Endocrine pancreas. Apud cells (diseases) Endocrinopathies Enzymes Etiopathogenesis. Screening. Investigations. Target tissue resistance Food gastric inhibitory polypeptide Gastric Inhibitory Polypeptide - blood Glucagon glucagon-like peptide 1 Glucagon-Like Peptide 1 - blood Glucose half life Hormones Humans Hypoglycemic Agents - pharmacology Hypoglycemic Agents - therapeutic use Inhibitors Insulin resistance Irish Section Postgraduate Meeting Medical sciences Milk milk proteins Milk Proteins - therapeutic use Natural & organic foods noninsulin-dependent diabetes mellitus nutritional intervention Peptides Peptides - pharmacology Peptides - therapeutic use Physiology Polypeptides protein hydrolysates Protein Hydrolysates - pharmacology Protein Hydrolysates - therapeutic use Proteins Small intestine structure-activity relationships |
Title | Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes |
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