메뉴 건너뛰기




Volumn 61, Issue 31, 2013, Pages 7500-7506

Inhibition of dipeptidyl peptidase (DPP)-IV and α-glucosidase activities by pepsin-treated whey proteins

Author keywords

glucosidase inhibitor; dipeptidyl peptidase (DPP) IV inhibitor; peptide; type 2 diabetes; whey protein

Indexed keywords

BENEFICIAL EFFECTS; DIPEPTIDYL PEPTIDASE; GLUCOSIDASE ACTIVITY; GLUCOSIDASE INHIBITORS; INHIBITORY ACTIVITY; TYPE-2 DIABETES; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

EID: 84881259510     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf401000s     Document Type: Article
Times cited : (184)

References (46)
  • 1
    • 65549151663 scopus 로고    scopus 로고
    • Regulation of insulin action by diet and exercise
    • Schmidt, S. L.; Hickey, M. S. Regulation of insulin action by diet and exercise J. Equine Vet. Sci. 2009, 29, 274-284
    • (2009) J. Equine Vet. Sci. , vol.29 , pp. 274-284
    • Schmidt, S.L.1    Hickey, M.S.2
  • 2
    • 84881260316 scopus 로고    scopus 로고
    • International Diabetes Federation. The global burden; (accessed Dec 24, 2012).
    • International Diabetes Federation. The global burden; http://www.idf.org/diabetesatlas/5e/the-global-burden, 2011, (accessed Dec 24, 2012).
    • (2011)
  • 3
    • 84866268783 scopus 로고    scopus 로고
    • Management of hyperglycemia in type 2 diabetes: A patient-centered approach. Position statement of the American Diabetes Association (ADA) and the European Association for the Study of Diabetes (EASD)
    • Inzucchi, S. E.; Bergenstal, R. M.; Buse, J. B.; Diamant, M.; Ferrannini, E.; Nauck, M.; Peters, A. L.; Tsapas, A.; Wender, R.; Matthews, D. R. Management of hyperglycemia in type 2 diabetes: a patient-centered approach. Position statement of the American Diabetes Association (ADA) and the European Association for the Study of Diabetes (EASD) Diabetes Care 2012, 35, 1364-1379
    • (2012) Diabetes Care , vol.35 , pp. 1364-1379
    • Inzucchi, S.E.1    Bergenstal, R.M.2    Buse, J.B.3    Diamant, M.4    Ferrannini, E.5    Nauck, M.6    Peters, A.L.7    Tsapas, A.8    Wender, R.9    Matthews, D.R.10
  • 5
    • 79960262492 scopus 로고    scopus 로고
    • Management of type 2 diabetes: New and future development
    • Tahrani, A. A.; Bailey, C. J.; Del Prato, S.; Barnett, A. H. Management of type 2 diabetes: new and future development Lancet 2011, 378, 182-197
    • (2011) Lancet , vol.378 , pp. 182-197
    • Tahrani, A.A.1    Bailey, C.J.2    Del Prato, S.3    Barnett, A.H.4
  • 6
    • 78649686908 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: A comparative review
    • Deacon, C. F. Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review Diabetes Obes. Metab. 2011, 13, 7-18
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 7-18
    • Deacon, C.F.1
  • 7
    • 42449084168 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitors: Pharmacological profile and clinical use
    • White, J. R. Dipeptidyl peptidase-IV inhibitors: pharmacological profile and clinical use Clin. Diabetes 2008, 26, 53-57
    • (2008) Clin. Diabetes , vol.26 , pp. 53-57
    • White, J.R.1
  • 8
    • 79955897721 scopus 로고    scopus 로고
    • Diabetes and cardiovascular disease: The potential benefit of incretin-based therapies
    • Addison, D.; Aguilar, D. Diabetes and cardiovascular disease: the potential benefit of incretin-based therapies Curr. Atheroscler. Rep. 2011, 13, 115-122
    • (2011) Curr. Atheroscler. Rep. , vol.13 , pp. 115-122
    • Addison, D.1    Aguilar, D.2
  • 9
    • 14044264798 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus
    • Holst, J. J.; Deacon, C. F. Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus Curr. Opin. Pharmacol. 2004, 4, 589-596
    • (2004) Curr. Opin. Pharmacol. , vol.4 , pp. 589-596
    • Holst, J.J.1    Deacon, C.F.2
  • 10
    • 12744269699 scopus 로고    scopus 로고
    • Therapeutic assessment of glucagon-like peptide-1 agonists compared with dipeptidyl peptidase IV inhibitors as potential antidiabetic drugs
    • Mentlein, R. Therapeutic assessment of glucagon-like peptide-1 agonists compared with dipeptidyl peptidase IV inhibitors as potential antidiabetic drugs Expert Opin. Investig. Drugs 2005, 14, 57-64
    • (2005) Expert Opin. Investig. Drugs , vol.14 , pp. 57-64
    • Mentlein, R.1
  • 11
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma, R.; Löffler, B.; Stihle, M.; Huber, W.; Ruf, A.; Henning, M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV Structure 2003, 11, 947-959
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Löffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Henning, M.6
  • 12
    • 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, I. M. E.; Li-Chan, E. C. Y. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach J. Funct. Foods 2012, 4, 403-422
    • (2012) J. Funct. Foods , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 14
    • 84856555742 scopus 로고    scopus 로고
    • Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors
    • Li-Chan, E. C. Y.; Huang, S.-L.; Jao, C.-L.; Ho, K.-P.; Hsu, K.-C. Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors J. Agric. Food Chem. 2012, 60, 973-978
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 973-978
    • Li-Chan, E.C.Y.1    Huang, S.-L.2    Jao, C.-L.3    Ho, K.-P.4    Hsu, K.-C.5
  • 15
    • 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.; Hsu, K.-C. Dipeptidyl peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates Peptides 2012, 35, 114-121
    • (2012) Peptides , vol.35 , pp. 114-121
    • Huang, S.-L.1    Jao, C.-L.2    Ho, K.-P.3    Hsu, K.-C.4
  • 18
    • 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.. 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 2010, 151, 3095-3104
    • (2010) Endocrinology , vol.151 , pp. 3095-3104
    • Mochida, T.1    Hira, T.2    Hara, H.3
  • 19
    • 79952799368 scopus 로고    scopus 로고
    • Whey proteins as source of dipeptidyl peptidase IV (dipeptidyl peptidase-4) inhibitors
    • Tulipano, G.; Sibilia, V.; Caroli, A. M.; Cocchi, D. Whey proteins as source of dipeptidyl peptidase IV (dipeptidyl peptidase-4) inhibitors Peptides 2011, 32, 835-838
    • (2011) Peptides , vol.32 , pp. 835-838
    • Tulipano, G.1    Sibilia, V.2    Caroli, A.M.3    Cocchi, D.4
  • 20
    • 84861898887 scopus 로고    scopus 로고
    • Comparison of goat and sheep β-lactoglobulin to bovine β-lactoglobulin as potential source of dipeptidyl peptidase IV (DPP-4) inhibitors
    • Tulipano, G.; Cocchi, D.; Caroli, A. M. Comparison of goat and sheep β-lactoglobulin to bovine β-lactoglobulin as potential source of dipeptidyl peptidase IV (DPP-4) inhibitors Int. Dairy J. 2012, 24, 97-101
    • (2012) Int. Dairy J. , vol.24 , pp. 97-101
    • Tulipano, G.1    Cocchi, D.2    Caroli, A.M.3
  • 21
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin
    • Uchida, M.; Ohshiba, Y.; Mogami, O. Novel dipeptidyl peptidase-4- inhibiting peptide derived from β-lactoglobulin J. Pharmacol. Sci. 2011, 117, 63-66
    • (2011) J. Pharmacol. Sci. , vol.117 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 22
    • 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.; Serizawa, A.; Nakajima, H. 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. 2012, 22, 24-30
    • (2012) Int. Dairy J. , vol.22 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3    Serizawa, A.4    Nakajima, H.5
  • 23
    • 84861332110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates
    • Lacroix, I. M. E.; Li-Chan, E. C. Y. Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates Int. Dairy J. 2012, 25, 97-102
    • (2012) Int. Dairy J. , vol.25 , pp. 97-102
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 24
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates
    • Nongonierma, A. B.; FitzGerald, R. J. Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates Peptides 2013, 39, 157-163
    • (2013) Peptides , vol.39 , pp. 157-163
    • Nongonierma, A.B.1    Fitzgerald, R.J.2
  • 26
    • 16344384538 scopus 로고    scopus 로고
    • Different polyphenolic components of soft fruits inhibit α-amylase and α-glucosidase
    • McDougall, G. J.; Shpiro, F.; Dobson, P.; Smith, P.; Blake, A.; Stewart, D. Different polyphenolic components of soft fruits inhibit α-amylase and α-glucosidase J. Agric. Food Chem. 2005, 53, 2760-2766
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2760-2766
    • McDougall, G.J.1    Shpiro, F.2    Dobson, P.3    Smith, P.4    Blake, A.5    Stewart, D.6
  • 27
    • 47349103327 scopus 로고    scopus 로고
    • Functionality of bioactive compounds in Brazilian strawberry (Fragaria × ananassa Duch.) cultivars: Evaluation of hyperglycemia and hypertension potential using in vitro models
    • da Silva Pinto, M.; Kwon, Y.-I.; Apostolidis, E.; Lajolo, F. M.; Genovese, M. I.; Shetty, K. Functionality of bioactive compounds in Brazilian strawberry (Fragaria × ananassa Duch.) cultivars: evaluation of hyperglycemia and hypertension potential using in vitro models J. Agric. Food Chem. 2008, 56, 4386-4392
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 4386-4392
    • Da Silva Pinto, M.1    Kwon, Y.-I.2    Apostolidis, E.3    Lajolo, F.M.4    Genovese, M.I.5    Shetty, K.6
  • 28
    • 23744507092 scopus 로고    scopus 로고
    • Anti-amylase, anti-glucosidase and anti-angiotensin I-converting enzyme potential of selected foods
    • McCue, P.; Kwon, Y.-I.; Shetty, K. Anti-amylase, anti-glucosidase and anti-angiotensin I-converting enzyme potential of selected foods J. Food Biochem. 2005, 29, 278-294
    • (2005) J. Food Biochem. , vol.29 , pp. 278-294
    • McCue, P.1    Kwon, Y.-I.2    Shetty, K.3
  • 29
    • 84858244509 scopus 로고    scopus 로고
    • Antidiabetic effects of natural plant extracts via inhibition of carbohydrate hydrolysis enzymes with emphasis on pancreatic alpha amylase
    • Etxeberria, U.; de la Garza, A. L.; Campión, J.; Martínez, J. A.; Milagro, F. I. Antidiabetic effects of natural plant extracts via inhibition of carbohydrate hydrolysis enzymes with emphasis on pancreatic alpha amylase Expert Opin. Ther. Targets 2012, 16, 269-297
    • (2012) Expert Opin. Ther. Targets , vol.16 , pp. 269-297
    • Etxeberria, U.1    De La Garza, A.L.2    Campión, J.3    Martínez, J.A.4    Milagro, F.I.5
  • 31
    • 0034330742 scopus 로고    scopus 로고
    • Inhibition of alpha-glucosidase and amylase by luteolin, a flavonoid
    • Kim, J.-S.; Kwon, C.-S.; Son, K. H. Inhibition of alpha-glucosidase and amylase by luteolin, a flavonoid Biosci., Biotechnol., Biochem. 2000, 64, 2458-2461
    • (2000) Biosci., Biotechnol., Biochem. , vol.64 , pp. 2458-2461
    • Kim, J.-S.1    Kwon, C.-S.2    Son, K.H.3
  • 32
    • 78049425026 scopus 로고    scopus 로고
    • Inhibition of α-amylase activity by condensed tannins
    • Gonçalves, R.; Mateus, N.; de Freitas, V. Inhibition of α-amylase activity by condensed tannins Food Chem. 2011, 125, 665-672
    • (2011) Food Chem. , vol.125 , pp. 665-672
    • Gonçalves, R.1    Mateus, N.2    De Freitas, V.3
  • 34
    • 80051793911 scopus 로고    scopus 로고
    • Novel peptides derived from egg white protein inhibiting alpha-glucosidase
    • Yu, Z.; Yin, Y.; Zhao, W.; Yu, Y.; Liu, B.; Liu, J.; Chen, F. Novel peptides derived from egg white protein inhibiting alpha-glucosidase Food Chem. 2011, 129, 1376-1382
    • (2011) Food Chem. , vol.129 , pp. 1376-1382
    • Yu, Z.1    Yin, Y.2    Zhao, W.3    Yu, Y.4    Liu, B.5    Liu, J.6    Chen, F.7
  • 35
    • 84870441206 scopus 로고    scopus 로고
    • Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and type 2 diabetes
    • Jakubowicz, D.; Froy, O. Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and type 2 diabetes J. Nutr. Biochem. 2013, 24, 1-5
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 1-5
    • Jakubowicz, D.1    Froy, O.2
  • 36
    • 80055023970 scopus 로고    scopus 로고
    • Effects of whey protein supplements on metabolism: Evidence from human intervention studies
    • Graf, S.; Egert, S.; Heer, M. Effects of whey protein supplements on metabolism: evidence from human intervention studies Curr. Opin. Clin. Nutr. Metab. Care 2011, 14, 569-580
    • (2011) Curr. Opin. Clin. Nutr. Metab. Care , vol.14 , pp. 569-580
    • Graf, S.1    Egert, S.2    Heer, M.3
  • 37
    • 80053104218 scopus 로고    scopus 로고
    • A high-throughput assay for quantification of starch hydrolysate inhibition based on turbidity measurement
    • Liu, T.; Song, L.; Wang, H.; Huang, D. A high-throughput assay for quantification of starch hydrolysate inhibition based on turbidity measurement J. Agric. Food Chem. 2011, 59, 9756-9762
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 9756-9762
    • Liu, T.1    Song, L.2    Wang, H.3    Huang, D.4
  • 38
    • 0000186865 scopus 로고
    • Some fundamental aspects of food protein hydrolysis
    • Elsevier Applied Science Publisher: New York
    • Adler-Nissen, J. Some fundamental aspects of food protein hydrolysis. In Enzymic Hydrolysis of Food Proteins; Elsevier Applied Science Publisher: New York, 1986; pp 9-24.
    • (1986) Enzymic Hydrolysis of Food Proteins , pp. 9-24
    • Adler-Nissen, J.1
  • 39
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion
    • Reddy, M.; Kella, N. K. D.; Kinsella, J. E. Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion J. Agric. Food Chem. 1988, 36, 737-741
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 737-741
    • Reddy, M.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 40
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: Opioid and ace-inhibitory peptides
    • Pihlanto-Leppälä, A. Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides Trends Food Sci. Technol. 2001, 11, 347-356
    • (2001) Trends Food Sci. Technol. , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 41
    • 0033008866 scopus 로고    scopus 로고
    • Inhibitory effect of α-glucosidase inhibitors varies according to its origin
    • Oki, T.; Matsui, T.; Osajima, Y. Inhibitory effect of α-glucosidase inhibitors varies according to its origin J. Agric. Food Chem. 1999, 47, 550-553
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 550-553
    • Oki, T.1    Matsui, T.2    Osajima, Y.3
  • 42
    • 79959770729 scopus 로고    scopus 로고
    • Effects of onion (Allium cepa L.) extract administration on intestinal α-glucosidase activities and spikes in postprandial blood glucose levels in SD rats model
    • Kim, S.-H.; Jo, S.-H.; Kwon, Y.-I.; Hwang, J.-K. Effects of onion (Allium cepa L.) extract administration on intestinal α-glucosidase activities and spikes in postprandial blood glucose levels in SD rats model Int. J. Mol. Sci. 2011, 12, 3757-3769
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 3757-3769
    • Kim, S.-H.1    Jo, S.-H.2    Kwon, Y.-I.3    Hwang, J.-K.4
  • 43
    • 42749087181 scopus 로고    scopus 로고
    • Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of α-glucosidase inhibitors
    • Bharatham, K.; Bharatham, N.; Park, K. H.; Lee, K. W. Binding mode analyses and pharmacophore model development for sulfonamide chalcone derivatives, a new class of α-glucosidase inhibitors J. Mol. Graph. Model 2008, 26, 1202-1212
    • (2008) J. Mol. Graph. Model , vol.26 , pp. 1202-1212
    • Bharatham, K.1    Bharatham, N.2    Park, K.H.3    Lee, K.W.4
  • 44
    • 83955163773 scopus 로고    scopus 로고
    • Anti-diabetic activities of phenolic compounds in muscadine against alpha-glucosidase and pancreatic lipase
    • You, Q.; Chen, F.; Wang, X.; Jiang, Y.; Lin, S. Anti-diabetic activities of phenolic compounds in muscadine against alpha-glucosidase and pancreatic lipase Food Sci. Technol. 2012, 46, 164-168
    • (2012) Food Sci. Technol. , vol.46 , pp. 164-168
    • You, Q.1    Chen, F.2    Wang, X.3    Jiang, Y.4    Lin, S.5
  • 45
    • 0034861322 scopus 로고    scopus 로고
    • α-Glucosidase inhibitory of natural acylated anthocyannins. 1. Survey of natural pigments with potent inhibitory activity
    • Matsui, T.; Ueda, T.; Oki, T.; Sugita, K.; Terahara, N.; Matsumoto, K. α-Glucosidase inhibitory of natural acylated anthocyannins. 1. Survey of natural pigments with potent inhibitory activity J. Agric. Food Chem. 2001, 49, 1948-1951
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1948-1951
    • Matsui, T.1    Ueda, T.2    Oki, T.3    Sugita, K.4    Terahara, N.5    Matsumoto, K.6
  • 46
    • 0033103875 scopus 로고    scopus 로고
    • Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate
    • Matsui, T.; Oki, T.; Osajima, Y. Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate Z. Naturforsch. 1999, 54C, 259-263
    • (1999) Z. Naturforsch. , vol.54 , pp. 259
    • Matsui, T.1    Oki, T.2    Osajima, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.