Dipeptidyl peptidase iv inhibitory activity of protein hydrolyzates from Amaranthus hypochondriacus L. Grain and their influence on postprandial glycemia in streptozotocin-induced diabetic mice

African Journal of Traditional, Complementary and Alternative Medicines

Volumn 12, Issue 1, 2015, Pages 90-98

  Jorge, Soriano Santos ^a   Raúl, Reyes Bautista ^a   Isabel, Guerrero Legarreta ^a   Edith, Ponce Alquicira ^a   Bernardo, Escalona Buendía Héctor ^a   César, Almanza Pérez Julio ^a   Gerardo, Díaz Godínez ^b   Rubén, Román Ramos ^a  

^a DEPARTAMENTO DE QUÍMICA   (Mexico)

^b CENTRO TLAXCALA DE BIOLOGÍA DE LA CONDUCTA   (Mexico)

Author keywords

Amaranth protein hydrolyzate; Diabetes; DPP IV inhibitory activity

Indexed keywords

ALBUMIN 1; AMARANTHUS HYPOCHONDRIACUS EXTRACT; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; DIPROTIN A; GLOBULIN; GLUCOSE; GLUTENIN; INSULIN; PLANT EXTRACT; SEED STORAGE PROTEIN; SITAGLIPTIN; UNCLASSIFIED DRUG;

AMARANTHUS; AMARANTHUS HYPOCHONDRIACUS; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIDIABETIC ACTIVITY; ARTICLE; CHRONIC DRUG ADMINISTRATION; CONTROLLED STUDY; DIABETES CONTROL; DRUG IDENTIFICATION; DRUG ISOLATION; ENZYME INHIBITION; GEL FILTRATION; GLUCOSE BLOOD LEVEL; GRAIN; IC50; IMPAIRED GLUCOSE TOLERANCE; IN VITRO STUDY; INSULIN BLOOD LEVEL; MALE; MOUSE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; PHARMACOLOGICAL PARAMETERS; POSTPRANDIAL STATE; PROTEIN HYDROLYSIS; PROTEIN ISOLATION; SINGLE DRUG DOSE; STREPTOZOTOCIN-INDUCED DIABETES MELLITUS;

EID: 84923931504     PISSN: 01896016     EISSN: 01896016     Source Type: Journal    
DOI: 10.4314/ajtcam.v12i1.13     Document Type: Article

References (38)

1. AOAC (2000). Official methods of analysis. Association of Official Analytical Chemists.
2. A.P. Barba de la Rosa, A. Barba Montoya, Pedro Martínez-Cuevas, B. Hernández-Ledesma, M.F. León-Galván, A. De León-Rodríguez, C. González (2010). Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide. 23: 106–111.
3. Bjelke, J. D., Christensen, J., Nielsen, P. F., Branner et al. (2006). Dipeptidyl peptidases 8 and 9: Specificity and molecular characterization compared with dipeptidyl peptidase IV. Biochem J. 396: 391-399.
4. Caselato-Sousa, V. M. and Amaya-Farfán, J. (2012). State of knowledge on amaranth grain: A comprehensive review. J Food Sci. 77: R93-R104.
5. Condés, M. C., Scilingo, A. A. and Añón, M. C. (2009). Characterization of amaranth proteins modified by tripsin proteolysis: Structural and functional changes. LWT - Food SciTechnol. 42: 963–70.
6. Drab, S. R. (2010). Incretin-based therapy for type-2 diabetes mellitus: current status and future prospects. Pharmacotherapy. 30: 609-624.
7. Drucker, D. J. (2006). The biology of incretin hormones. Cell Metabol. 3:153-165.
8. Fritz, M, Vecchi, B., Rinaldi, G. and Añón, M. C. (2011). Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity. Food Chem. 126: 878–884.
9. Tadashi Hatanaka, Yosikazu Inoue, Jiro Arima, Yuya Kumagai, Hirokazu Usuki, Kayoko Kawakami, Masayo Kimura, Takafumi Mukaihara (2012). Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chem. 134: 797-802.
10. Huang, S. L., Jao, C. L., Ho, K. P. and Hsu, K. C. (2012). Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides. 35: 114-121.
11. Kim, H. K., Kim, M. J., Cho, H. Y., Kim E. K. and Shin, D. H. (2006). Antioxidative and anti-diabetic effects of amaranth (Amaranthus hypochondriacus) in streptozotocin-induced diabetic rats. Cell Biochem Funct. 24: 195-199.
12. Kojima, K., Ham, T. and Kato, T. (1980). Rapid chromatogrpahic purification of dipeptidyl peptidase IV in human submaxillary gland. J Chromatogr A. 189: 233-240.
13. Konishi, Y., Horikawa, K., Oku, Y., Azumaya, J. and Nakatani, N. (1991). Extraction of two albumin fractions from amaranth grains: comparison of some physicochemical properties and the putative localization in the grains. J Agr Biol Chem. 55: 1745-1750.
14. Korhonen, H. and Philanto, A., (2003). Food-derived bioactive peptides –opportunities for designing future foods. Curr Pharm Design. 9: 1297-1308.
15. Lacroix, I. M. E. and Li-Chan, E. C. Y. (2012a). Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int Dairy J. 25: 97–102.
16. Lacroix, I. M. E. and Li-Chan, E. C. Y. (2012b). Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J Funct Foods. 4: 403-422.
17. Luna-Suárez, S., Medina-Godoy, S., Cruz-Hernández, A. and Paredes-López, O. (2010). Modification of the amaranth 11S globulin storage protein to produce an inhibitory peptide of the angiotensin I converting enzyme, and its expression in Escherichia coli. J Biotechnol. 148: 240–247.
18. Matteucci, E. and Giampietro, O. (2011). Dipeptidyl peptidase-4 inhibition: Linking chemical properties to clinical safety. Curr Med Chem. 18: 4753-4760.
19. Nauck, M. A. (2011). Incretin-based therapies for type 2 diabetes mellitus: Properties, functions, and clinical implications. Am J Med. 124: 53-518.
20. NOM-062-ZOO-1999. Especificaciones y técnicas para la producción, cuidado y uso de los animales de laboratorio.
21. Orsini, D.M.C., Tironi, V. A and Añón, M. C. (2011). Antioxidant activity of amaranth protein or their hydrolysates under simulated gastrointestinal digestion. LWT – Food Sci Technol. 44: 1752–1760.
22. Rahfeld, J., Schierhorn, M., Hartrodt, B., Neubert, K. and Heins, J. (1991). Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV. Biochim Biophys Acta. 1076: 314-316.
23. Rastogi, A. and Shukla, S. (2013). Amaranth: A new millennium crop of nutraceutical values. Crit Rev Food Sci. 53: 109-125.
24. Richter, B., Banderia-Echtler, E., Bergerhoff, K. and Lerch, C. (2008). Emerging role of dipeptidyl peptidase-4 inhibitors in the management of type 2 diabetes. Vasc Health Risk Manag. 4: 753-768.
25. Silva-Sánchez, C., Barba de la Rosa, A. P., León-Galván, M. F., De Lumen, B. O., De León-Rodríguez, A. and González de Mejía, E. (2008). Bioactive Peptides in Amaranth (Amaranthushypochondriacus) Seed. J Agr Food Chem. 56: 1233-1240.
26. Tiengo, A. M. and Netto, E. M. (2009). Characterization and ACE-inhibitory activity of amaranth proteins. J Food Sci. 74: H121-H126.
27. Tironi, V. A. and Añón, M. C. (2010). Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis. Food Res Int. 43: 315–322.
28. Tovar-Pérez, E. G., Guerrero-Legarreta, I., Farrés-González, A. and Soriano-Santos, J. (2009). Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain. Food Chem. 116: 437–444.
29. Uchida, M., Ohshiba, Y. and Mogami, O. (2011). Novel dipeptidyl peptiase-4-inhibiting peptide derived from β-lactoglobulin. J Pharmacol Sci. 117: 63-66.
30. Umezawa, H, Aoyagi, T., Ogawa, K, Naganawa, H., Hamada, M. and Takeuchi, T. (1984). Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria. J Antibiot. 37: 422-425.
31. Vecchi, B. and Añón, M. C. (2009). ACE inhibitory tetrapeptides from Amaranthus hypochondriacus 11S globulin. Phytochemistry. 70: 864–870.
32. Aída J. Velarde-Salcedo, Alberto Barrera-Pacheco, Samuel Lara-González, Gabriela M. Montero-Morán, Agustín Díaz-Gois, Elvira González de Mejia, Ana P. Barba de la Rosa. (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.
33. Ventura-Sobrevilla J, Boone-Villa VD, Aguilar CN, Román-Ramos R, Vega-Avila E, Campos-Sepúlveda E, Alarcón-Aguilar F. (2011). Effect of varying dose and administration of streptozotocin on blood sugar in male CD1 mice. P W Pharmacol Soc. 54: 5-9.
34. Ventureira, J. L., Bolontrade, A. J., Speroni, F., David-Briand, E., Scilingo, A. A., Ropers, M. H., Boury, F., Añón, M. C. and Anton, M. (2012). Interfacial and emulsifying properties of amaranth (Amaranthus hypochondriacus) protein isolates under different conditions of pH. LWT – Food Sci Technol. 45: 1–7.
35. Wiedeman, P. E. (2007). DPPIV inhibition: Promising therapy for the treatment of type 2 diabetes. Progr Med Chem. 45: 63-109.
36. Wiedeman, P. E. and Trevillayn, J. M. (2003). Dipeptidyl peptidase IV inhibitors for the treatment for impared glucose tolerance and type 2 diabetes. Curr Opin Investig Drugs. 4: 412-420.
37. Wild, S., Roglic, G., Green, A., Sicree, R. and King, H. (2004). Global prevalence of diabetes estimates from the year 2000 and projections for 2030. Diabetes Care. 27: 1047-1053.
38. Yan, T. R., Ho, S. C. and Hou, C. L. (1992). Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR. Biosci Biotechnol Biochem. 56: 704–707.