Journal Home > Volume 11 , Issue 6
Food Science and Human Wellness 2022, 11(6): 1441-1454 https://doi.org/10.1016/j.fshw.2022.06.001
Review Article | Open Access | Issue | Published: 18 July 2022

A review on mechanisms of action of bioactive peptides against glucose intolerance and insulin resistance

Show Author's Information Forough Jahandideha,b,  Jianping Wua,b( )
Department of Agricultural, Food and Nutritional Science, Faculty of Agricultural, Life and Environmental Sciences, University of Alberta, Edmonton, AB, T6G 2P5, Canada
Cardiovascular Research Centre, Faculty of Medicine & Dentistry, University of Alberta, Edmonton, AB, T6G 2S2, Canada

Peer review under responsibility of KeAi Communications Co., Ltd.

Keywords:
Insulin resistance, Metabolic syndrome, Bioactive peptides, Glucose homeostasis, Adipose tissue
Cite this article:
Jahandideh F, Wu J. A review on mechanisms of action of bioactive peptides against glucose intolerance and insulin resistance. Food Science and Human Wellness, 2022, 11(6): 1441-1454. https://doi.org/10.1016/j.fshw.2022.06.001
Download citation
EndNote(RIS)
BibTeX

499

Views

50

Downloads

Citations

12

Crossref

9

WoS

10

Scopus

0

CSCD

Abstract Full text About this article

Insulin resistance leads to impaired glucose metabolism by disrupting both insulin secretion and sensitivity. Insulin resistance plays a key role in the pathophysiology of type 2 diabetes and metabolic syndrome. Reviews on the mechanisms of action of bioactive peptides on glucose homeostasis and insulin resistance are scarce. The recent discoveries of pathways and target cells in the management of glucose and energy metabolism have opened up new opportunities for identification of novel bioactive peptides on enhancing adipocyte differentiation and insulin signaling, glucose uptake, cholecystokinin receptor expression and activation, as well as insulin mimetics and incretin stimulants. Examples of food-derived bioactive peptides with glucoregulatory properties include Trp-Glu-Lys-Ala-Phe-Lys-Asp-Glu-Asp (WEKAFKDED), Gln-Ala-Met-Pro-Phe-Arg-Val-Thr-Glu-Gln-Glu (QAMPFRVTEQE), Glu-Arg-Tyr-Pro-Ile-Leu (ERKPIL), Val-Phe-Lys-Gly-Leu (VFKGL), Phe-Leu-Val (FLV), Val-Pro-Pro (VPP), Ile-Arg-Trp (IRW), Ala-Lys-Ser-Pro-Leu-Phe (AKSPLF), Ala-Thr-Gln-Pro-Leu-Phe (ATNPLF), Phe-Glu-Glu-Leu-Gln (FEELN), Leu-Ser-Val-Ser-Val-Leu (LSVSVL), Val-Arg-Ileu-Arg-Leu-Leu-Gln-Arg-Phe-Asn-Lys-Arg-Ser (VRIRLLQRFNKRS), and Ala-Gly-Phe-Ala-Gly-Asp-Asp-Ala-Pro-Arg (AGFAGDDAPR). However, as yet, clinical evidence on the efficacy of such bioactive peptides is rare but is inevitable to establish their applications against glucose intolerance and insulin resistance.


menu
Abstract
Full text
Outline
About this article

A review on mechanisms of action of bioactive peptides against glucose intolerance and insulin resistance

Show Author's information Forough Jahandideha,b, Jianping Wua,b( )
Department of Agricultural, Food and Nutritional Science, Faculty of Agricultural, Life and Environmental Sciences, University of Alberta, Edmonton, AB, T6G 2P5, Canada
Cardiovascular Research Centre, Faculty of Medicine & Dentistry, University of Alberta, Edmonton, AB, T6G 2S2, Canada

Peer review under responsibility of KeAi Communications Co., Ltd.

Abstract

Insulin resistance leads to impaired glucose metabolism by disrupting both insulin secretion and sensitivity. Insulin resistance plays a key role in the pathophysiology of type 2 diabetes and metabolic syndrome. Reviews on the mechanisms of action of bioactive peptides on glucose homeostasis and insulin resistance are scarce. The recent discoveries of pathways and target cells in the management of glucose and energy metabolism have opened up new opportunities for identification of novel bioactive peptides on enhancing adipocyte differentiation and insulin signaling, glucose uptake, cholecystokinin receptor expression and activation, as well as insulin mimetics and incretin stimulants. Examples of food-derived bioactive peptides with glucoregulatory properties include Trp-Glu-Lys-Ala-Phe-Lys-Asp-Glu-Asp (WEKAFKDED), Gln-Ala-Met-Pro-Phe-Arg-Val-Thr-Glu-Gln-Glu (QAMPFRVTEQE), Glu-Arg-Tyr-Pro-Ile-Leu (ERKPIL), Val-Phe-Lys-Gly-Leu (VFKGL), Phe-Leu-Val (FLV), Val-Pro-Pro (VPP), Ile-Arg-Trp (IRW), Ala-Lys-Ser-Pro-Leu-Phe (AKSPLF), Ala-Thr-Gln-Pro-Leu-Phe (ATNPLF), Phe-Glu-Glu-Leu-Gln (FEELN), Leu-Ser-Val-Ser-Val-Leu (LSVSVL), Val-Arg-Ileu-Arg-Leu-Leu-Gln-Arg-Phe-Asn-Lys-Arg-Ser (VRIRLLQRFNKRS), and Ala-Gly-Phe-Ala-Gly-Asp-Asp-Ala-Pro-Arg (AGFAGDDAPR). However, as yet, clinical evidence on the efficacy of such bioactive peptides is rare but is inevitable to establish their applications against glucose intolerance and insulin resistance.

Keywords: Insulin resistance, Metabolic syndrome, Bioactive peptides, Glucose homeostasis, Adipose tissue

References(173)

[1]

L. Mayans, Metabolic syndrome: insulin resistance and prediabetes, FP essentials 435 (2015) 11-16.
Google Scholar
[2]

K.G.M.M. Alberti, R.H. Eckel, S.M. Grundy, et al., Harmonizing the metabolic syndrome a joint interim statement of the international diabetes federation task force on epidemiology and prevention; National Heart, Lung, and Blood Institute; American Heart Association; World Heart Federation; International Atherosclerosis Society; and International Association for the Study of Obesity, Circulation 120 (2009) 1640-1645. http://dx.doi.org/10.1161/CIRCULATIONAHA.109.192644.
DOI Google Scholar
[3]

S.M. Grundy, Metabolic syndrome pandemic, Arterioscl. Throm. Vas. 28 (2008) 629-636. http://dx.doi.org/10.1161/ATVBAHA.107.151092.
DOI Google Scholar
[4]

E. Kassi, P. Pervanidou, G. Kaltsas, et al., Metabolic syndrome: definitions and controversies, BMC Medicine 9 (2011) 48. http://dx.doi.org/10.1186/1741-7015-9-48.
DOI Google Scholar
[5]

N. Mikhail, The metabolic syndrome: insulin resistance, Curr. hypertens. Rep. 11 (2009) 156-158. http://dx.doi.org/10.1007/s11906-009-0027-4.
DOI Google Scholar
[6]

R.H. Eckel, S.M. Grundy, P.Z. Zimmet, The metabolic syndrome, Lancet 365 (2005) 1415-1428. http://dx.doi.org/10.1016/S0140-6736(05)66378-7.
DOI Google Scholar
[7]

K. Erdmann, B.W.Y. Cheung, H. Schroder, The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease, J. Nutr. Biochem. 19 (2008) 643-654. http://dx.doi.org/10.1016/j.jnutbio.2007.11.010.
DOI Google Scholar
[8]

C.C. Udenigwe, R.E. Aluko, Food protein-derived bioactive peptides: production, processing, and potential health benefits, J. Food Sci. 77 (2012) R11-R24. http://dx.doi.org/10.1111/j.1750-3841.2011.02455.x.
DOI Google Scholar
[9]

S. Chakrabarti, F. Jahandideh, J.P. Wu, Food-derived bioactive peptides on inflammation and oxidative stress, Biomed. Res. Int. 2014 (2014) 608979. http://dx.doi.org/10.1155/2014/608979.
DOI Google Scholar
[10]

S. Guha, K. Majumder, Structural-features of food-derived bioactive peptides with anti-inflammatory activity: a brief review, J. Food Biochem. 43(1) (2019) e12531. http://dx.doi.org/10.1111/jfbc.12531.
DOI Google Scholar
[11]

K. Majumder, J.P. Wu, Molecular targets of antihypertensive peptides: understanding the mechanisms of action based on the pathophysiology of hypertension, Int. J. Mol. Sci. 16 (2015) 256-283. http://dx.doi.org/10.3390/ijms16010256.
DOI Google Scholar
[12]

S. Nagaoka, Structure-function properties of hypolipidemic peptides, J. Food Biochem. 43(1) (2019) e12539. http://dx.doi.org/10.1111/jfbc.12539.
DOI Google Scholar
[13]

J. Tkaczewska, M. Bukowski, P. Mak, Identification of antioxidant peptides in enzymatic hydrolysates of carp (Cyprinus carpio) skin gelatin, Molecules 24(1) (2018) 97. http://dx.doi.org/10.3390/molecules24010097.
DOI Google Scholar
[14]

X.R. Yang, Y.T. Qiu, Y.Q. Zhao, et al., Purification and characterization of antioxidant peptides derived from protein hydrolysate of the marine bivalve mollusk Tergillarca granosa, Mar. Drugs 17 (2019).
DOI Google Scholar
[15]

Q. Zhang, X. Tong, Y. Li, et al., Purification and characterization of antioxidant peptides from alcalase-hydrolyzed soybean (Glycine max L.) hydrolysate and their cytoprotective effects in human intestinal Caco-2 cells, J. Agric. Food Chem. 67 (2019) 5772-5781. http://dx.doi.org/10.1021/acs.jafc.9b01235.
DOI Google Scholar
[16]

H. Agrawal, R. Joshi, M. Gupta, Purification, identification and characterization of two novel antioxidant peptides from finger millet (Eleusine coracana) protein hydrolysate, Food Res. Int. 120 (2019) 697-707. http://dx.doi.org/10.1016/j.foodres.2018.11.028.
DOI Google Scholar
[17]

J. Yang, L. Hu, T. Cai, et al., Purification and identification of two novel antioxidant peptides from perilla (Perilla frutescens L. Britton) seed protein hydrolysates, PLoS ONE 13 (2018) e0200021.
DOI Google Scholar
[18]

Q. Liang, M. Chalamaiah, X. Ren, et al., Identification of new anti-inflammatory peptides from zein hydrolysate after simulated gastrointestinal digestion and transport in Caco-2 cells, J. Agric. Food Chem. 66 (2018) 1114-1120. http://dx.doi.org/10.1021/acs.jafc.7b04562.
DOI Google Scholar
[19]

L. Zhao, X. Wang, X.L. Zhang, et al., Purification and identification of anti-inflammatory peptides derived from simulated gastrointestinal digests of velvet antler protein (Cervus elaphus Linnaeus), J. Food Drug Anal. 24 (2016) 376-384. http://dx.doi.org/10.1016/j.jfda.2015.10.003.
DOI Google Scholar
[20]

Y. Chen, H. Zhang, L. Mats, et al., Anti-inflammatory effect and cellular uptake mechanism of peptides from common bean (Phaseolus vulga L.) milk and yogurts in Caco-2 mono- and Caco-2/EA.hy926 co-culture models, J. Agric. Food Chem. 67 (2019) 8370-8381. http://dx.doi.org/10.1021/acs.jafc.9b03079.
DOI Google Scholar
[21]

J. Kan, M. Hood, C. Burns, et al., A novel combination of wheat peptides and fucoidan attenuates ethanol-induced gastric mucosal damage through anti-oxidant, anti-inflammatory, and pro-survival mechanisms, Nutrients 9(9) (2017) 978. http://dx.doi.org/10.3390/nu9090978.
DOI Google Scholar
[22]

M. Zhang, Y. Zhao, Y. Yao, et al., Isolation and identification of peptides from simulated gastrointestinal digestion of preserved egg white and their anti-inflammatory activity in TNF-alpha-induced Caco-2 cells, J. Nutr. Biochem. 63 (2019) 44-53. http://dx.doi.org/10.1016/j.jnutbio.2018.09.019.
DOI Google Scholar
[23]

N. Quintal-Bojorquez, M.R. Segura-campos, Bioactive peptides as therapeutic adjuvants for cancer, Nutr. Cancer 4 (2020) 1-13.
Google Scholar
[24]

X. Li, L. Xia, X. Ouyang, et al., Bioactive peptides sensitize cells to anticancer effects of oxaliplatin in human colorectal cancer xenografts in nude mice, Protein Pept. Lett. 26 (2019) 512-522. http://dx.doi.org/10.2174/0929866526666190405124955.
DOI Google Scholar
[25]

Y.H. Shih, F.A. Chen, L.F. Wang, et al., Discovery and study of novel antihypertensive peptides derived from Cassia obtusifolia seeds, J. Agric. Food Chem. 67 (2019) 7810-7820. http://dx.doi.org/10.1021/acs.jafc.9b01922.
DOI Google Scholar
[26]

Y.Q. Zhao, L. Zhang, J. Tao, et al., Eight antihypertensive peptides from the protein hydrolysate of Antarctic krill (Euphausia superba): isolation, identification, and activity evaluation on human umbilical vein endothelial cells (HUVECs), Food Res. Int. 121 (2019) 197-204. http://dx.doi.org/10.1016/j.foodres.2019.03.035.
DOI Google Scholar
[27]

Q. Xu, H. Fan, W. Yu, et al., Transport study of egg-derived antihypertensive peptides (LKP and IQW) using Caco-2 and HT29 coculture monolayers, J. Agric. Food Chem. 65 (2017) 7406-7414. http://dx.doi.org/10.1021/acs.jafc.7b02176.
DOI Google Scholar
[28]

U.G. Yathisha. I. Bhat, I. Karunasagar, et al., Antihypertensive activity of fish protein hydrolysates and its peptides, Crit. Rev. Food Sci. 59 (2019) 2363-2374. http://dx.doi.org/10.1080/10408398.2018.1452182.
DOI Google Scholar
[29]

D. Qian, B. Qiu, N. Zhou, et al., Hypotensive activity of transgenic rice seed accumulating multiple antihypertensive peptides, J. Agric. Food Chem. 68 (2020) 7162-7168. http://dx.doi.org/10.1021/acs.jafc.0c01958.
DOI Google Scholar
[30]

F. Jahandideh, K. Majumder, S. Chakrabarti, et al., Beneficial effects of simulated gastro-intestinal digests of fried egg and its fractions on blood pressure, plasma lipids and oxidative stress in spontaneously hypertensive rats, PLoS ONE 9 (2014).
DOI Google Scholar
[31]

F. Jahandideh, S. Chakrabarti, K. Majumder, et al., Egg white protein hydrolysate reduces blood pressure, improves vascular relaxation and modifies aortic angiotensin II receptors expression in spontaneously hypertensive rats, J. Funct. Foods 27 (2016) 667-673. http://dx.doi.org/10.1016/j.jff.2016.10.019.
DOI Google Scholar
[32]

E. Elkhtab, M. El-Alfy, M. Shenana, et al., New potentially antihypertensive peptides liberated in milk during fermentation with selected lactic acid bacteria and kombucha cultures, J. Dairy Sci. 100 (2017) 9508-9520. http://dx.doi.org/10.1515/jcim-2017-0071.
DOI Google Scholar
[33]

O. Abdelhedi, H. Khemakhem, R. Nasri, et al., Assessment of cholesterol, glycemia control and short- and long-term antihypertensive effects of smooth hound viscera peptides in high-salt and fructose diet-fed wistar rats, Mar. Drugs 17 (2019).
DOI Google Scholar
[34]

R. Ben Slama-Ben Salem, N. Ktari, I. Bkhairia, et al., In vitro and in vivo anti-diabetic and anti-hyperlipidemic effects of protein hydrolysates from Octopus vulgaris in alloxanic rats, Food Res. Int. 106 (2018) 952-963. http://dx.doi.org/10.1016/j.foodres.2018.01.068.
DOI Google Scholar
[35]

M.R. Zanutto-Elgui, J.C.S. Vieira, D.Z.D. Prado, et al., Production of milk peptides with antimicrobial and antioxidant properties through fungal proteases, Food Chem. 278 (2019) 823-831. http://dx.doi.org/10.1016/j.foodchem.2018.11.119.
DOI Google Scholar
[36]

I. Dinika, D.K. Verma, R. Bali, et al., Potential of cheese whey bioactive proteins and peptides in the development of antimicrobial edible film composite: a review of recent trends, Trends Food Sci. Technol. 103 (2020) 57-67. http://dx.doi.org/10.1016/j.tifs.2020.06.017.
DOI Google Scholar
[37]

M. Pandey, S. Kapila, R. Kapila, et al., Evaluation of the osteoprotective potential of whey derived-antioxidative (YVEEL) and angiotensin-converting enzyme inhibitory (YLLF) bioactive peptides in ovariectomised rats, Food Funct. 9(9) (2018) 4791-4801. http://dx.doi.org/10.1039/c8fo00620b.
DOI Google Scholar
[38]

S. Chakrabarti, J. Ren, J. Wu, Phosvitin derived phospho-peptides show better osteogenic potential than intact phosvitin in MC3T3-E1 osteoblastic cells, Nutrients 12 (2020) 2998. http://dx.doi.org/10.3390/nu12102998.
DOI Google Scholar
[39]

Y.X. Chen, J.C. Chen, J. Chen, et al., Recent advances in seafood bioactive peptides and their potential for managing osteoporosis, Crit. Rev. Food Sci. (2020) 1-17. http://dx.doi.org/10.1080/10408398.2020.1836606.
DOI Google Scholar
[40]

S. Reddi, V.P. Shanmugam, K.S. Tanedjeu, et al., Effect of buffalo casein-derived novel bioactive peptides on osteoblast differentiation, Eur. J. Nutr. 57 (2018) 593-605. http://dx.doi.org/10.1007/s00394-016-1346-2.
DOI Google Scholar
[41]

J. Yan, J. Zhao,, R. Yang, et al., Bioactive peptides with antidiabetic properties: a review, Int. J. Food Sci. Technol. 54 (2019) 1909-1919. http://dx.doi.org/10.1111/ijfs.14090.
DOI Google Scholar
[42]

Y.Y. Ngoh, T.S. Lim, C.Y. Gan, Screening and identification of five peptides from pinto bean with inhibitory activities against alpha-amylase using phage display technique, Enzyme Microb. Technol. 89 (2016) 76-84. http://dx.doi.org/10.1016/j.enzmictec.2016.04.001.
DOI Google Scholar
[43]

Y.Y. Ngoh, C.Y. Gan, Identification of Pinto bean peptides with inhibitory effects on alpha-amylase and angiotensin converting enzyme (ACE) activities using an integrated bioinformatics-assisted approach, Food Chem. 267 (2018) 124-131. http://dx.doi.org/10.1016/j.foodchem.2017.04.166.
DOI Google Scholar
[44]

H.L. Siow, T.S. Lim, C.Y. Gan, Development of a workflow for screening and identification of alpha-amylase inhibitory peptides from food source using an integrated bioinformatics-phage display approach: case study - cumin seed, Food Chem. 214 (2017) 67-76. http://dx.doi.org/10.1016/j.foodchem.2016.07.069.
DOI Google Scholar
[45]

N.A. Evaristus, W.N. Wan Abdullah, C.Y. Gan, Extraction and identification of alpha-amylase inhibitor peptides from Nephelium lappacheum and Nephelium mutabile seed protein using gastro-digestive enzymes, Peptides 102 (2018) 61-67.
DOI Google Scholar
[46]

S.A. Ross, E.A. Gulve, M. Wang, Chemistry and biochemistry of type 2 diabetes, Chem. Rev. 104 (2004) 1255-1282. http://dx.doi.org/10.1002/chin.200421298.
DOI Google Scholar
[47]

F. Chaudhry, S. Naureen, R. Huma, et al., In search of new alpha-glucosidase inhibitors: imidazolylpyrazole derivatives, Bioorg. Chem. 71 (2017) 102-109. http://dx.doi.org/10.1016/j.bioorg.2017.01.017.
DOI Google Scholar
[48]

D. Kinariwala, G. Panchal, A. Sakure, et al., Exploring the potentiality of Lactobacillus cultures on the production of milk-derived bioactive peptides with antidiabetic activity, Int. J. Pept. Res. Ther. 26 (2020) 1613-1627.
DOI Google Scholar
[49]

I.M.E. Lacroix, E.C.Y. Li-Chan, Inhibition of dipeptidyl peptidase (DPP)-IV and alpha-glucosidase activities by pepsin-treated whey proteins, J. Agr. Food Chem. 61 (2013) 7500-7506. http://dx.doi.org/10.1021/jf401000s.
DOI Google Scholar
[50]

B. Konrad, D. Anna, S. Marek, et al., The evaluation of dipeptidyl peptidase (DPP)-IV, alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activities of whey proteins hydrolyzed with serine protease isolated from Asian pumpkin (Cucurbita ficifolia), Int. J. Pept. Res. Ther. 20 (2014) 483-491.
DOI Google Scholar
[51]

R. Wang, H. Zhao, X. Pan, et al., Preparation of bioactive peptides with antidiabetic, antihypertensive, and antioxidant activities and identification of alpha-glucosidase inhibitory peptides from soy protein, Food Sci. Nutr. 7 (2019) 1848-1856. http://dx.doi.org/10.1002/fsn3.1038.
DOI Google Scholar
[52]

M. Gonzalez-Montoya, B. Hernandez-Ledesma, R. Mora-Escobedo, et al., Bioactive peptides from germinated soybean with anti-diabetic potential by inhibition of dipeptidyl peptidase-IV, alpha-amylase, and alpha-glucosidase enzymes, Int. J. Mol. Sci. 19 (10) (2018) 2883. http://dx.doi.org/10.3390/ijms19102883.
DOI Google Scholar
[53]

C. Uraipong, J. Zhao, In vitro digestion of rice bran proteins produces peptides with potent inhibitory effects on alpha-glucosidase and angiotensin I converting enzyme, J. Sci. Food Agric. 98 (2018) 758-766. http://dx.doi.org/10.1002/jsfa.8523.
DOI Google Scholar
[54]

J.U. Obaroakpo, L. Liu, S. Zhang, et al., α-Glucosidase and ACE dual inhibitory protein hydrolysates and peptide fractions of sprouted quinoa yoghurt beverages inoculated with Lactobacillus casei, Food Chem. 299 (2019) 124985. http://dx.doi.org/10.1016/j.foodchem.2019.124985.
DOI Google Scholar
[55]

A. Connolly, C.O. Piggott, R.J. FitzGerald, In vitro alpha-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers' spent grain protein hydrolysates, Food Res. Int. 56 (2014) 100-107. http://dx.doi.org/10.1016/j.foodres.2013.12.021.
DOI Google Scholar
[56]

T. Oki, T. Matsui, Y. Osajima, Inhibitory effect of alpha-glucosidase inhibitors varies according to its origin, J. Agric. Food Chem. 47 (1999) 550-553. http://dx.doi.org/10.1021/jf980788t.
DOI Google Scholar
[57]

P.V. Roder, B. Wu, Y. Liu, et al., Pancreatic regulation of glucose homeostasis, Exp. Mol. Med. 48 (2016) e219. http://dx.doi.org/10.1038/emm.2016.6.
DOI Google Scholar
[58]

A.R. Saltiel, C.R. Kahn, Insulin signalling and the regulation of glucose and lipid metabolism, Nature 414 (2001) 799-806. http://dx.doi.org/10.1038/414799a.
DOI Google Scholar
[59]

Y.H. Wang, J. Viscarra, S.J. Kim, et al., Transcriptional regulation of hepatic lipogenesis, Nat. Rev. Mol. Cell Bio. 16 (2015) 678-689. http://dx.doi.org/10.1038/nrm4074.
DOI Google Scholar
[60]

B.E. Grayson, R.J. Seeley, D.A. Sandoval, Wired on sugar: the role of the CNS in the regulation of glucose homeostasis, Nat. Rev. Neurosci. 14 (2013) 24-37. http://dx.doi.org/10.1038/nrn3409.
DOI Google Scholar
[61]
R. Bilous, R. Donnelly, Chapter 5: Normal physiology of insulin secretion and action, in Handbook of Diabetes. 2010, John Wiley & Sons, Ltd.
[62]

R. Meshkani, K. Adeli, Hepatic insulin resistance, metabolic syndrome and cardiovascular disease, Cli. Biochem. 42 (2009) 1331-1346. http://dx.doi.org/10.1016/j.clinbiochem.2009.05.018.
DOI Google Scholar
[63]

J. Jeppesen, T.W. Hansen, S. Rasmussen, et al., Metabolic syndrome, low-density lipoprotein cholesterol, and risk of cardiovascular disease: a population-based study, Atherosclerosis 189 (2006) 369-374. http://dx.doi.org/10.1016/j.atherosclerosis.2005.12.010.
DOI Google Scholar
[64]

R. Schmid, E. Schultefrohlinde, V. Schusdziarra, et al., Contribution of postprandial amino-acid levels to stimulation of insulin, glucagon, and pancreatic-polypeptide in humans, Pancreas 7 (1992) 698-704. http://dx.doi.org/10.1097/00006676-199211000-00011.
DOI Google Scholar
[65]

J.C. Floyd, S.S. Fajans, J.W. Conn, et al., Stimulation of insulin secretion by amino acids, J. Clin. Invest. 45 (1966) 1487-1502. http://dx.doi.org/10.1172/JCI105456.
DOI Google Scholar
[66]

V. Lang, F. Bellisle, C. Alamowitch, et al., Varying the protein source in mixed meal modifies glucose, insulin and glucagon kinetics in healthy men, has weak effects on subjective satiety and fails to affect food intake, Eur. J. Clin. Nutr. 53 (1999) 959-965. http://dx.doi.org/10.1038/sj.ejcn.1600881.
DOI Google Scholar
[67]

J.A.L. Calbet, D.A. MacLean, Plasma glucagon and insulin responses depend on the rate of appearance of amino acids after ingestion of different protein solutions in humans, J. Nutr. 132 (2002) 2174-2182.
DOI Google Scholar
[68]

R.L. Adams, K.S. Broughton, Insulinotropic effects of whey: mechanisms of action, recent clinical trials, and clinical applications, Ann. Nutr. Metab. 69 (2016) 56-63. http://dx.doi.org/10.1159/000448665.
DOI Google Scholar
[69]

M. Nilsson, M. Stenberg, A.H. Frid, et al., Glycemia and insulinemia in healthy subjects after lactoseequivalent meals of milk and other food proteins: the role of plasma amino acids and incretins, Am. J. Clin. Nutr. 80(5) (2004) 1246-1253. http://dx.doi.org/10.1093/ajcn/80.5.1246.
DOI Google Scholar
[70]

M. Nilsson, J.J. Holst, I.M.E. Bjorck, Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks, Am. J. Clin. Nutr. 85 (2007) 996-1004. http://dx.doi.org/10.1186/1476-511X-6-9.
DOI Google Scholar
[71]

C. Gaudel, A.B. Nongonierma, S. Maher, et al., A whey protein hydrolysate promotes insulinotropic activity in a clonal pancreatic beta-cell line and enhances glycemic function in ob/ob mice, J. Nutr. 143 (2013) 1109-1114. http://dx.doi.org/10.3945/jn.113.174912.
DOI Google Scholar
[72]

V. Parthsarathy, C.M. McLaughlin, P.A. Harnedy, et al., Boarfish (Capros aper) protein hydrolysate has potent insulinotropic and GLP-1 secretory activity in vitro and acute glucose lowering effects in mice, Int. J. Food Sci. Tech. 54 (2019) 271-281. http://dx.doi.org/10.1111/ijfs.13975.
DOI Google Scholar
[73]

P.A. Harnedy-Rothwell, C.M. McLaughlin, M.B. O'Keeffe, et al., Identification and characterisation of peptides from a boarfish (Capros aper) protein hydrolysate displaying in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory and insulinotropic activity, Food Res. Int. 131 (2020) 108989. http://dx.doi.org/10.1016/j.foodres.2020.108989.
DOI Google Scholar
[74]

K.D. Copps, M.F. White, Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2, Diabetologia 55 (2012) 2565-2582. http://dx.doi.org/10.1007/s00125-012-2644-8.
DOI Google Scholar
[75]

B. Mlinar, J. Marc, A. Janez, et al., Molecular mechanisms of insulin resistance and associated diseases, Clin. Chim. Acta 375 (2007) 20-35. http://dx.doi.org/10.1016/j.cca.2006.07.005.
DOI Google Scholar
[76]

L. Laviola, S. Perrini, A. Cignarelli, et al., Insulin signaling in human visceral and subcutaneous adipose tissue in vivo, Diabetes 55 (2006) 952-961. http://dx.doi.org/10.2337/diabetes.55.04.06.db05-1414.
DOI Google Scholar
[77]

J. Boucher, A. Kleinridders, C.R. Kahn, Insulin receptor signaling in normal and insulin-resistant states, Csh. Perspect Biol. 6 (2014).
DOI Google Scholar
[78]

F.S. Facchini, N. Hua, F. Abbasi, et al., Insulin resistance as a predictor of age-related diseases, J. Clin. Endocr. Metab. 86 (2001) 3574-3578. http://dx.doi.org/10.1210/jcem.86.8.7763.
DOI Google Scholar
[79]

H.E. Resnick, K. Jones, G. Ruotolo, et al., Insulin resistance, the metabolic syndrome, and risk of incident cardiovascular disease in nondiabetic american indians - the strong heart study, Diabetes Care 26 (2003) 861-867. http://dx.doi.org/10.2337/diacare.26.3.861.
DOI Google Scholar
[80]

F. Angelico, M. Del Ben, R. Conti, et al., Insulin resistance, the metabolic syndrome, and nonalcoholic fatty liver disease, J. Clin. Endocr. Metab. 90 (2005) 1578-1582.
DOI Google Scholar
[81]

F. Jahandideh, J. Wu, Perspectives on the potential benefits of antihypertensive peptides towards metabolic syndrome, Int. J. Mol. Sci. 21(6) (2020) 2192. http://dx.doi.org/10.3390/ijms21062192.
DOI Google Scholar
[82]

C. Lavigne, F. Tremblay, G. Asselin, et al., Prevention of skeletal muscle insulin resistance by dietary cod protein in high fat-fed rats, Am. J. Physiol-Endoc. M. 281 (2001) E62-E71. http://dx.doi.org/10.1152/ajpendo.2001.281.1.E62.
DOI Google Scholar
[83]

Z. Madani, K. Louchami, A. Sener, et al., Dietary sardine protein lowers insulin resistance, leptin and TNF-alpha and beneficially affects adipose tissue oxidative stress in rats with fructose-induced metabolic syndrome, Int. J. Mol. Med. 29 (2012) 311-318.
Google Scholar
[84]

G. Pilon, J. Ruzzin, L.E. Rioux, et al., Differential effects of various fish proteins in altering body weight, adiposity, inflammatory status, and insulin sensitivity in high-fat-fed rats, Metab. Clin. Exp. 60 (2011) 1122-1130. http://dx.doi.org/10.1016/j.metabol.2010.12.005.
DOI Google Scholar
[85]

S.C. de Campos Zani, J. Wu, C.B. Chan, Egg and soy-derived peptides and hydrolysates: a review of their physiological actions against diabetes and obesity, Nutrients 10(5) (2018) 549. http://dx.doi.org/10.3390/nu10050549.
DOI Google Scholar
[86]

F. Jahandideh, S. Chakrabarti, S.T. Davidge, et al., Egg white hydrolysate shows insulin mimetic and sensitizing effects in 3T3-F442A pre-adipocytes, PLoS ONE 12 (2017) e0185653. http://dx.doi.org/10.1371/journal.pone.0185653.
DOI Google Scholar
[87]

M. Son, J. Wu, Egg white hydrolysate and peptide reverse insulin resistance associated with tumor necrosis factor-alpha (TNF-alpha) stimulated mitogen-activated protein kinase (MAPK) pathway in skeletal muscle cells, Eur. J. Nutr. 58 (2019) 1961-1969.
DOI Google Scholar
[88]

F. Jahandideh, S.C.C. Zani, M. Son, et al., Egg white hydrolysate enhances insulin sensitivity in high-fat diet-induced insulin-resistant rats via Akt activation, Brit. J. Nutr. 122 (2019) 14-24. http://dx.doi.org/10.1017/s0007114519000837.
DOI Google Scholar
[89]

S. Chakrabarti, F. Jahandideh, S.T. Davidge, et al., Milk-derived tripeptides IPP (Ile-Pro-Pro) and VPP (Val-Pro-Pro) enhance insulin sensitivity and prevent insulin resistance in 3T3-F442A preadipocytes, J. Agric. Food Chem. 66 (2018) 10179-10187. http://dx.doi.org/10.1021/acs.jafc.8b02051.
DOI Google Scholar
[90]

S. Nishitani, T. Matsumura, S. Fujitani, et al., Leucine promotes glucose uptake in skeletal muscles of rats, Biochem. Biophys. Res. Commun. 299 (2002) 693-696.
DOI Google Scholar
[91]

M. Doi, I. Yamaoka, M. Nakayama, et al., Isoleucine, a blood glucose-lowering amino acid, increases glucose uptake in rat skeletal muscle in the absence of increases in AMP-activated protein kinase activity, J. Nut. 135 (2005) 2103-2108. http://dx.doi.org/10.1093/jn/135.9.2103.
DOI Google Scholar
[92]

P.N. Morato, P.C.B. Lollo, C.S. Moura, et al., Whey protein hydrolysate increases translocation of GLUT-4 to the plasma membrane independent of insulin in Wistar rats, PLoS ONE 8 (2013).
DOI Google Scholar
[93]

K.A. Coughlan, R.J. Valentine, N.B. Ruderman, et al., AMPK activation: a therapeutic target for type 2 diabetes?, Diabet. Metab. Synd. Ob. 7 (2014) 241-253.
DOI Google Scholar
[94]

N. Jessen, L.J. Goodyear, Contraction signaling to glucose transport in skeletal muscle, J. Appl. Physiol. 99 (2005) 330-337. http://dx.doi.org/10.1152/japplphysiol.00175.2005.
DOI Google Scholar
[95]

N. Fujii, N. Jessen, L.J. Goodyear, AMP-activated protein kinase and the regulation of glucose transport, Am. J. Physiol-Endoc. M. 291 (2006) E867-E877. http://dx.doi.org/10.1152/ajpendo.00207.2006.
DOI Google Scholar
[96]

K.I. Stanford, L.J. Goodyear, Exercise and type 2 diabetes: molecular mechanisms regulating glucose uptake in skeletal muscle, Adv. Physiol. Educ. 38 (2014) 308-314. http://dx.doi.org/10.1152/advan.00080.2014.
DOI Google Scholar
[97]

M.J. Sanders, P.O. Grondin, B.D. Hegarty, et al., Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade, Biochem. J. 403 (2007) 139-148.
DOI Google Scholar
[98]

B.B. Zhang, G. Zhou, C. Li, AMPK: an emerging drug target for diabetes and the metabolic syndrome, Cell Metab. 9 (2009) 407-416. http://dx.doi.org/10.1016/j.cmet.2009.03.012.
DOI Google Scholar
[99]

H.A. Koistinen, D. Galuska, A.V. Chibalin, et al., 5-Amino-imidazole carboxamide riboside increases glucose transport and cell-surface GLUT4 content in skeletal muscle from subjects with type 2 diabetes, Diabetes 52(5) (2003) 1066-1072. http://dx.doi.org/10.2337/diabetes.52.5.1066.
DOI Google Scholar
[100]

G. Zhou, R. Myers, Y. Li, et al., Role of AMP-activated protein kinase in mechanism of metformin action, J. Clin. Invest. 108 (2001) 1167-1174. http://dx.doi.org/10.1172/JCI13505.
DOI Google Scholar
[101]

B. Viollet, B. Guigas, N. Sanz Garcia, et al., Cellular and molecular mechanisms of metformin: an overview, Clin. Sci. (Lond) 122 (2012) 253-270. http://dx.doi.org/10.1042/CS20110386.
DOI Google Scholar
[102]

C. Roblet, A. Doyen, J. Amiot, et al., Enhancement of glucose uptake in muscular cell by soybean charged peptides isolated by electrodialysis with ultrafiltration membranes (EDUF): activation of the AMPK pathway, Food Chem. 147 (2014) 124-130.
DOI Google Scholar
[103]

C. Lammi, C. Zanoni, A. Arnoldi, Three peptides from soy glycinin modulate glucose metabolism in human hepatic HepG2 cells, Int. J. Mol. Sci. 16 (2015) 27362-27370. http://dx.doi.org/10.3390/ijms161126029.
DOI Google Scholar
[104]

K.G. Murphy, S.R. Bloom, Gut hormones and the regulation of energy homeostasis, Nature 444 (2006) 854-859. http://dx.doi.org/10.1038/nature05484.
DOI Google Scholar
[105]

N. Irwin, P.R. Flatt, Enteroendocrine hormone mimetics for the treatment of obesity and diabetes, Curr. Opin. Pharmacol. 13 (2013) 989-995. http://dx.doi.org/10.1016/j.coph.2013.09.009.
DOI Google Scholar
[106]

J. Caron, B. Cudennec, D. Domenger, et al., Simulated GI digestion of dietary protein: release of new bioactive peptides involved in gut hormone secretion, Food Res. Int. 89 (2016) 382-390. http://dx.doi.org/10.1016/j.foodres.2016.08.033.
DOI Google Scholar
[107]

J. Austin, D. Marks, Hormonal regulators of appetite, Int. J. Ped. Endocrinol. 2009 (2009) 141753. http://dx.doi.org/10.1155/2009/141753.
DOI Google Scholar
[108]

B. Cudennec, R. Ravallec, Biological active peptides from marine sources related to gut hormones, Curr. Protein Pept. Sci. 14 (2013) 231-234.
DOI Google Scholar
[109]

I.I. Cancre, R. Ravallec, A. Van Wormhoudt, et al., Secretagogues and growth factors in fish and crustacean protein hydrolysates, Mar. Biotechnol. 1 (1999) 489-0494. http://dx.doi.org/10.1007/PL00011805.
DOI Google Scholar
[110]

R. Ravallec-Ple, A.Van Wormhoudt, Secretagogue activities in cod (Gadus morhua) and shrimp (Penaeus aztecus) extracts and alcalase hydrolysates determined in AR4-2J pancreatic tumour cells, Comp. Biochem. Phys. B 134 (2003) 669-679.
DOI Google Scholar
[111]

R. Slizyte, R. Mozuraityte, O. Martinez-Alvarez, et al., Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadus morhua) backbones, Process Biochem. 44 (2009) 668-677. http://dx.doi.org/10.1016/j.procbio.2009.02.010.
DOI Google Scholar
[112]

M. Foltz, P. Ansems, J. Schwarz, et al., Protein hydrolysates induce CCK release from enteroendocrine cells and act as partial agonists of the CCK1 receptor, J. Agr. Food Chem. 56 (2008) 837-843. http://dx.doi.org/10.1021/jf072611h.
DOI Google Scholar
[113]

N. Irwin, P. Frizelle, I.A. Montgomery, et al., Beneficial effects of the novel cholecystokinin agonist (pGlu-Gln)-CCK-8 in mouse models of obesity/diabetes, Diabetologia 55 (2012) 2747-2758. http://dx.doi.org/10.1007/s00125-012-2654-6.
DOI Google Scholar
[114]

R. Pais, F.M. Gribble, F. Reimann, Signalling pathways involved in the detection of peptones by murine small intestinal enteroendocrine L-cells, Peptides 77 (2016) 9-15. http://dx.doi.org/10.1016/j.peptides.2015.07.019.
DOI Google Scholar
[115]

D.J. Drucker, M.A. Nauck, The incretin system: glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes, Lancet 368 (2006) 1696-1705. http://dx.doi.org/10.1016/S0140-6736(06)69705-5.
DOI Google Scholar
[116]

C.M.B. Edwards, Glucagon-like peptide-1 agonists in the treatment of type 2 diabetes, Brit. J. Hosp. Med. 74 (2013) 198-201. http://dx.doi.org/10.12968/hmed.2013.74.4.198.
DOI Google Scholar
[117]
WHO, Obesity: preventing and managing the global epidemic. Report of a WHO consultation (WHO Technical Report Series 894). 2000. 252.
[118]

M. Veldhorst, A. Smeets, S. Soenen, et al., Protein-induced satiety: effects and mechanisms of different proteins, Physiol. Behav. 94 (2008) 300-307. http://dx.doi.org/10.1016/j.physbeh.2008.01.003.
DOI Google Scholar
[119]

S.M. Mellinkoff, M. Frankland, D. Boyle, et al., Relationship between serum amino acid concentration and fluctuations in appetite, J. Appl. Physiol. 8 (1956) 535-538. http://dx.doi.org/10.1152/jappl.1956.8.5.535.
DOI Google Scholar
[120]

J.A. Gilbert, D.R. Joanisse, J.P. Chaput, et al., Milk supplementation facilitates appetite control in obese women during weight loss: a randomised, single-blind, placebo-controlled trial, Brit. J. Nutr. 105 (2011) 133-143. http://dx.doi.org/10.1017/S0007114510003119.
DOI Google Scholar
[121]

B. Hernandez-Ledesma, M.J. Garcia-Nebot, S. Fernandez-Tome, et al., Dairy protein hydrolysates: peptides for health benefits, Int. Dairy. J. 38 (2014) 82-100. http://dx.doi.org/10.1016/j.idairyj.2013.11.004.
DOI Google Scholar
[122]

W.L. Hall, D.J. Millward, S.J. Long, et al., Casein and whey exert different effects on plasma amino acid profiles, gastrointestinal hormone secretion and appetite, Brit. J. Nutr. 89 (2003) 239-248. http://dx.doi.org/10.1079/BJN2002760.
DOI Google Scholar
[123]

T. Akhavan, B.L. Luhovyy, P.H. Brown, et al., Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults, Am. J. Clin. Nutr. 91 (2010) 966-975. http://dx.doi.org/10.3945/ajcn.2009.28406.
DOI Google Scholar
[124]

M.K.N.B. Sufian, T. Hira, K. Miyashita, et al., Pork peptone stimulates cholecystokinin secretion from enteroendocrine cells and suppresses appetite in rats, Biosci. Biotech. Bioch. 70 (2006) 1869-1874.
DOI Google Scholar
[125]

B. Cudennec, R. Ravallec-Ple, E. Courois, et al., Peptides from fish and crustacean by-products hydrolysates stimulate cholecystokinin release in STC-1 cells, Food Chem. 111 (2008) 970-975. http://dx.doi.org/10.1016/j.foodchem.2008.05.016.
DOI Google Scholar
[126]

B. Cudennec, M. Fouchereau-Peron, F. Ferry, et al., In vitro and in vivo evidence for a satiating effect of fish protein hydrolysate obtained from blue whiting (Micromesistius poutassou) muscle, J. Funct. Foods 4 (2012) 271-277.
DOI Google Scholar
[127]

J.R. Greenfield, I.S. Farooqi, J.M. Keogh, et al., Oral glutamine increases circulating glucagon-like peptide 1, glucagon, and insulin concentrations in lean, obese, and type 2 diabetic subjects, Am. J. Clin. Nutr. 89 (2009) 106-113. http://dx.doi.org/10.3945/ajcn.2008.26362.
DOI Google Scholar
[128]

D. Samocha-Bonet, O. Wong, E.L. Synnott, et al., Glutamine reduces postprandial glycemia and augments the glucagon-like peptide-1 response in type 2 diabetes patients, J. Nutr. 141 (2011) 1233-1238. http://dx.doi.org/10.3945/jn.111.139824.
DOI Google Scholar
[129]

M. Kato, T. Nakanishi, T. Tani, et al., Low-molecular fraction of wheat protein hydrolysate stimulates glucagon-like peptide-1 secretion in an enteroendocrine L cell line and improves glucose tolerance in rats, Nutr. Res. 37 (2017) 37-45. http://dx.doi.org/10.1016/j.nutres.2016.12.002.
DOI Google Scholar
[130]

R.A. Reimer, Meat hydrolysate and essential amino acid-induced glucagon-like peptide-1 secretion, in the human NCI-H716 enteroendocrine cell line, is regulated by extracellular signal-regulated kinase1/2 and p38 mitogen-activated protein kinases, J. Endocrinol. 191 (2006) 159-170. http://dx.doi.org/10.1677/joe.1.06557.
DOI Google Scholar
[131]

E. Diakogiannaki, R. Pais, G. Tolhurst, et al., Oligopeptides stimulate glucagon-like peptide-1 secretion in mice through proton-coupled uptake and the calcium-sensing receptor, Diabetologia 56 (2013) 2688-2696. http://dx.doi.org/10.1007/s00125-013-3037-3.
DOI Google Scholar
[132]

B.D. Green, P.R. Flatt, C.J. Bailey, Dipeptidyl peptidase IV (DPP IV) inhibitors: a newly emerging drug class for the treatment of type 2 diabetes, Diabetes Vasc. Dis. Re. 3 (2006) 159-165. http://dx.doi.org/10.3132/dvdr.2006.024.
DOI Google Scholar
[133]

A. Capuano, L. Sportiello, M.I. Maiorino, et al., Dipeptidyl peptidase-4 inhibitors in type 2 diabetes therapy--focus on alogliptin, Drug Des. Dev. Ther. 7 (2013) 989-1001. http://dx.doi.org/10.2147/DDDT.S37647.
DOI Google Scholar
[134]

S.L. Huang, C.L. Jao, K.P. Ho, et al., Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates, Peptides 35 (2012) 114-121. http://dx.doi.org/10.1016/j.peptides.2012.03.006.
DOI Google Scholar
[135]

E.C.Y. Li-Chan, S.L. Hunag, C.L. Jao, et al., Peptides derived from atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors, J. Agr. Food Chem. 60 (2012) 973-978. http://dx.doi.org/10.1021/jf204720q.
DOI Google Scholar
[136]

S. Ketnawa, S. Suwal, J. Huang, et al., Selective separation and characterisation of dual ACE and DPP‐IV inhibitory peptides from rainbow trout (Oncorhynchus mykiss) protein hydrolysates, Int. J. Food Sci. Tech. 54(4) (2019) 1062-1073. http://dx.doi.org/10.1111/ijfs.13939.
DOI Google Scholar
[137]

R. Jin, X. Teng, J. Shang, et al., Identification of novel DPP-IV inhibitory peptides from Atlantic salmon (Salmo salar) skin, Food Res. Int. 133 (2020) 109161. http://dx.doi.org/10.1016/j.foodres.2020.109161.
DOI Google Scholar
[138]

A.J. Velarde-Salcedo, A. Barrera-Pacheco, S. Lara-Gonzalez, et al., In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins, Food Chem. 136 (2013) 758-764. http://dx.doi.org/10.1016/j.foodchem.2012.08.032.
DOI Google Scholar
[139]

C. Lammi, C. Zanoni, A. Arnoldi, et al., Peptides derived from soy and lupin protein as dipeptidyl-peptidase IV inhibitors: in vitro biochemical screening and in silico molecular modeling study, J. Agric. Food Chem. 64 (2016) 9601-9606. http://dx.doi.org/10.1021/acs.jafc.6b04041.
DOI Google Scholar
[140]

C. Lammi, C. Bollati, S. Ferruzza, et al., Soybean- and lupin-derived peptides inhibit DPP-IV activity on in situ human intestinal Caco-2 cells and ex vivo human serum, Nutrients 10(8) (2018) 1082. http://dx.doi.org/10.3390/nu10081082.
DOI Google Scholar
[141]

R. Pugliese, C. Bollati, F. Gelain, et al., A supramolecular approach to develop new soybean and lupin peptide nanogels with enhanced dipeptidyl peptidase IV (DPP-IV) inhibitory activity, J. Agric. Food Chem. 67 (2019) 3615-3623. http://dx.doi.org/10.1021/acs.jafc.8b07264.
DOI Google Scholar
[142]

A.B. Nongonierma, S. Paolella, P. Mudgil, et al., Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates, Food Chem. 244 (2018) 340-348. http://dx.doi.org/10.1016/j.foodchem.2017.10.033.
DOI Google Scholar
[143]

P. Patil, S. Mandal, S.K. Tomar, et al., Food protein-derived bioactive peptides in management of type 2 diabetes, Eur. J. Nutr. 54 (2015) 863-880. http://dx.doi.org/10.1007/s00394-015-0974-2.
DOI Google Scholar
[144]

I.M.E. Lacroix, E.C.Y. Li-Chan, Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation: current knowledge and future research considerations, Trends Food Sci. Technol. 54 (2016) 1-16. http://dx.doi.org/10.1016/j.tifs.2016.05.008.
DOI Google Scholar
[145]

E.H. Jang, J.S. Moon, J.H. Ko, et al., Novel black soy peptides with antiobesity effects: activation of leptin-like signaling and AMP-activated protein kinase, Int. J. Obesity 32 (2008) 1161-1170. http://dx.doi.org/10.1038/ijo.2008.60.
DOI Google Scholar
[146]

H.J. Harwood, The adipocyte as an endocrine organ in the regulation of metabolic homeostasis, Neuropharmacology 63 (2012) 57-75.
DOI Google Scholar
[147]

L.F. Van Gaal, I.L. Mertens, C.E.De Block, Mechanisms linking obesity with cardiovascular disease, Nature 444 (2006) 875-880. http://dx.doi.org/10.1038/nature05487.
DOI Google Scholar
[148]

D.Y. Oh, J.M. Olefsky, G protein-coupled receptors as targets for anti-diabetic therapeutics, Nat. Rev. Drug Discov. 15 (2016) 161-172. http://dx.doi.org/10.1038/nrd.2015.4.
DOI Google Scholar
[149]

E.D. Rosen, O.A. MacDougald, Adipocyte differentiation from the inside out, Nat. Rev. Mol. Cell Bio. 7 (2006) 885-896. http://dx.doi.org/10.1038/nrm2066.
DOI Google Scholar
[150]

T. Kadowaki, K. Hara, T. Yamauchi, et al., Molecular mechanism of insulin resistance and obesity, Exp. Bio. Med. 228 (2003) 1111-1117. http://dx.doi.org/10.1007/s12038-007-0038-8.
DOI Google Scholar
[151]

S.R. Farmer, Transcriptional control of adipocyte formation, Cell Metab. 4 (2006) 263-273. http://dx.doi.org/10.1016/j.cmet.2006.07.001.
DOI Google Scholar
[152]

M. Ahmadian, J.M. Suh, N. Hah, et al., PPAR gamma signaling and metabolism: the good, the bad and the future, Nat. Med. 19 (2013) 557-566. http://dx.doi.org/10.1038/nm.3159.
DOI Google Scholar
[153]

L. Gatticchi, M. Petricciuolo, P. Scarpelli, et al., Tm7sf2 gene promotes adipocyte differentiation of mouse embryonic fibroblasts and improves insulin sensitivity, Biochim. Biophys. Acta. Mol. Cell Res. 1868 (2021) 118897. http://dx.doi.org/10.1016/j.bbamcr.2020.118897.
DOI Google Scholar
[154]

R.M. Evans, G.D. Barish, Y.X. Wang, PPARs and the complex journey to obesity, Nat. Med. 10 (2004) 355-361. http://dx.doi.org/10.1038/nm1025.
DOI Google Scholar
[155]

K.H. Yap, G.S. Yee, M. Candasamy, et al., Catalpol ameliorates insulin sensitivity and mitochondrial respiration in skeletal muscle of type-2 diabetic mice through insulin signaling pathway and AMPK/SIRT1/PGC-1alpha/PPAR-gamma activation, Biomolecules 10 (2020).
DOI Google Scholar
[156]

S. Yasmin, V. Jayaprakash, Thiazolidinediones and PPAR orchestra as antidiabetic agents: from past to present, Eur. J. Med. Chem. 126 (2017) 879-893. http://dx.doi.org/10.1016/j.ejmech.2016.12.020.
DOI Google Scholar
[157]

C.J. de Souza, M. Eckhardt, K. Gagen, et al., Effects of pioglitazone on adipose tissue remodeling within the setting of obesity and insulin resistance, Diabetes 50 (2001) 1863-1871. http://dx.doi.org/10.2337/diabetes.50.8.1863.
DOI Google Scholar
[158]

J.P. Ye, Regulation of PPAR gamma function by TNF-alpha, Biochem. Bioph. Res. Co. 374 (2008) 405-408. http://dx.doi.org/10.1016/j.bbrc.2008.07.068.
DOI Google Scholar
[159]

M. Chandra, S. Miriyala, M. Panchatcharam, PPARgamma and its role in cardiovascular diseases, PPAR Res. 2017 (2017) 6404638. http://dx.doi.org/10.1155/2017/6404638.
DOI Google Scholar
[160]

J. Rieusset, F. Andreelli, D. Auboeuf, et al., Insulin acutely regulates the expression of the peroxisome proliferator-activated receptor-gamma in human adipocytes, Diabetes 48 (1999) 699-705. http://dx.doi.org/10.2337/diabetes.48.4.699.
DOI Google Scholar
[161]

T. Goto, A. Mori, S. Nagaoka, Soluble soy protein peptic hydrolysate stimulates adipocyte differentiation in 3T3-L1 cells, Mol. Nutr. Food Res. 57 (2013) 1435-1445. http://dx.doi.org/10.1002/mnfr.201200573.
DOI Google Scholar
[162]

S.J. Kwak, C.S. Kim, M.S. Choi, et al., The soy peptide Phe-Leu-Val reduces TNF alpha-induced inflammatory response and insulin resistance in adipocytes, J. Med. Food 19 (2016) 678-685. http://dx.doi.org/10.1089/jmf.2016.3685.
DOI Google Scholar
[163]

F. Jahandideh, P. Liu, J. Wu, Purification and identification of adipogenic-differentiating peptides from egg white hydrolysate, Food Chem. 259 (2018) 25-30. http://dx.doi.org/10.1016/j.foodchem.2018.03.099.
DOI Google Scholar
[164]

A.F.G. Cicero, F. Fogacci, A. Colletti, Potential role of bioactive peptides in prevention and treatment of chronic diseases: a narrative review, Brit. J. Pharmacol. 174 (2017) 1378-1394. http://dx.doi.org/10.1111/bph.13608.
DOI Google Scholar
[165]

Z. Yu, Y. Yin, W. Zhao, et al., Anti-diabetic activity peptides from albumin against alpha-glucosidase and alpha-amylase, Food Chem. 135 (2012) 2078-2085.
DOI Google Scholar
[166]

M.A. Ibrahim, M.J. Bester, A.W. Neitz, et al., Rational in silico design of novel α-glucosidase inhibitory peptides and in vitro evaluation of promising candidates, Biomed. Pharmacother. 107 (2018) 234-242. http://dx.doi.org/10.1016/j.biopha.2018.07.163.
DOI Google Scholar
[167]

L. Mojica, E. Gonzalez de Mejia, M.A. Granados-Silvestre, et al., Evaluation of the hypoglycemic potential of a black bean hydrolyzed protein isolate and its pure peptides using in silico, in vitro and in vivo approaches, J. Funct. Foods 31 (2017) 274-286. http://dx.doi.org/10.1016/j.jff.2017.02.006.
DOI Google Scholar
[168]

M. Soga, A. Ohashi, M. Taniguchi, et al., The di-peptide Trp-His activates AMP-activated protein kinase and enhances glucose uptake independently of insulin in L6 myotubes, FEBS Open Bio. 4 (2014) 898-904. http://dx.doi.org/10.1016/j.fob.2014.10.008.
DOI Google Scholar
[169]

T. Nishi, H. Hara, K. Asano, et al., The soybean beta-conglycinin beta 51-63 fragment suppresses appetite by stimulating cholecystokinin release in rats, J. Nutr. 133 (2003) 2537-2542. http://dx.doi.org/10.1046/j.1365-277X.2003.00448.x.
DOI Google Scholar
[170]

Y. Lu, P. Lu, Y. Wang, et al., A novel dipeptidyl peptidase IV inhibitory tea peptide improves pancreatic beta-cell function and reduces alpha-cell proliferation in streptozotocin-induced diabetic mice, Int. J. Mol. Sci. 20 (2019). http://dx.doi.org/10.3390/ijms20020322.
DOI Google Scholar
[171]

Y. Zhang, R. Chen, X. Chen, et al., Dipeptidyl peptidase IV-inhibitory peptides derived from silver carp (Hypophthalmichthys molitrix Val.) proteins, J. Agric. Food Chem. 64 (2016) 831-839. http://dx.doi.org/10.1021/acs.jafc.5b05429.
DOI Google Scholar
[172]

K. Aihara, M. Osaka, M. Yoshida, Oral administration of the milk casein-derived tripeptide Val-Pro-Pro attenuates high-fat diet-induced adipose tissue inflammation in mice, Brit. J. Nutr. 112 (2014) 513-519. http://dx.doi.org/10.1017/S0007114514001147.
DOI Google Scholar
[173]

Y. Sawada, Y. Sakamoto, M. Toh, et al., Milk-derived peptide Val-Pro-Pro (VPP) inhibits obesity-induced adipose inflammation via an angiotensin-converting enzyme (ACE) dependent cascade, Mol. Nutr. Food Res. 59 (2015) 2502-2510.
DOI Google Scholar
Publication history
Copyright
Acknowledgements
Rights and permissions

Publication history

Received: 15 October 2020
Revised: 01 November 2020
Accepted: 09 February 2021
Published: 18 July 2022
Issue date: November 2022

Copyright

© 2022 Beijing Academy of Food Sciences.

Acknowledgements

The laboratory of Jianping Wu is supported by Grants from Natural Sciences and Engineering Research Council (NSERC) of Canada, Alberta Agriculture and Forestry, and Egg Farmers of Canada.

Rights and permissions

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return