A casein hydrolysate increases GLP-1 secretion and reduces food intake

O’Halloran, Fiona; Bruen, Christine M.; McGrath, Brian A.; Schellekens, Harriët; Murray, Brian A.; Cryan, John F.; Kelly, Alan L.; McSweeney, P.L.H.; Giblin, Linda

doi:10.1016/j.foodchem.2018.01.107

Cited by 28 publications

(15 citation statements)

References 34 publications

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“…Furthermore, the effect of casein using the STC-1 cell line also showed a different tendency in the release of GLP-1 in other research [155]. Results of O' Halloran et al are in agreement with the increased GLP-1 secretion when compared to digested casein [156]. In contrast, Gillespie et al reported that β-casein hydrolysate digested with chymotrypsin or trypsin (exception of pepsin) did not stimulate GLP-1 release [155].…”

Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 84%

“…Recently, M. Santos-Hernández published a paper regarding the fact that egg white proteins only had a modest effect in inducing GLP-1 production, while peptides (except free amino acids) released a significant amount [33]. The molecular weight fractions derived from enzymatically digested proteins are related to this activity, showing that small fragments (smaller than 3 kDa in size) of casein hydrolysate increased GLP-1 secretion in STC-1 cells [156]. Small peptides may be responsible for GLP-1 secretion bioactivity but the lengths of peptides for the stimulation of maximal GLP-1 production are continuously being discovered [153,156,169].…”

Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 99%

“…The molecular weight fractions derived from enzymatically digested proteins are related to this activity, showing that small fragments (smaller than 3 kDa in size) of casein hydrolysate increased GLP-1 secretion in STC-1 cells [156]. Small peptides may be responsible for GLP-1 secretion bioactivity but the lengths of peptides for the stimulation of maximal GLP-1 production are continuously being discovered [153,156,169]. M. Santos-Hernández also indicated that only two egg white peptides (PEL (3 amino acids) and RVASMASEKM (10 amino acids)) significantly released GLP-1 [33].…”

Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 99%

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Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.

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Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 84%

Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 99%

Section: The Specific In Vitro Models Of Glp-1 Secretion Studiesmentioning

confidence: 99%

See 1 more Smart Citation

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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“…Dipeptide RF is found encrypted in several peptide sequences released by the action of chymosin on sodium caseinate [106]. RF is able to induce the CCK release from STC-1 cells in vitro and revealed to be effective also in vivo in mice.…”

Section: Evidence Supporting a Role Of Bioactive Peptidesmentioning

confidence: 99%

“…A chymosin hydrolysate of sodium caseinate with secretagogue activity in vitro, was shown to reduce food intake after intraperitoneal (ip) administration in rodents [106]. However, it did not significantly change food intake, post prandial levels of GLP-1 and insulin in vivo compared to unhydrolysed sodium caseinate after oral administration in both animals and human subjects [8,101], suggesting that the active fractions generated by the preliminary digestion were not resistant to gastrointestinal proteases.…”

Section: Evidence Supporting a Role Of Bioactive Peptidesmentioning

confidence: 99%

Role of Bioactive Peptide Sequences in the Potential Impact of Dairy Protein Intake on Metabolic Health

Tulipano

2020

IJMS

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For years, there has been an increasing move towards elucidating the complexities of how food can interplay with the signalling networks underlying energy homeostasis and glycaemic control. Dairy foods can be regarded as the greatest source of proteins and peptides with various health benefits and are a well-recognized source of bioactive compounds. A number of dairy protein-derived peptide sequences with the ability to modulate functions related to the control of food intake, body weight gain and glucose homeostasis have been isolated and characterized. Their being active in vivo may be questionable mainly due to expected low bioavailability after ingestion, and hence their real contribution to the metabolic impact of dairy protein intake needs to be discussed. Some reports suggest that the differential effects of dairy proteins—in particular whey proteins—on mechanisms underlying energy balance and glucose-homeostasis may be attributed to their unique amino acid composition and hence the release of free amino acid mixtures enriched in essential amino acids (i.e., branched-chain-amino acids) upon digestion. Actually, the research reports reviewed in this article suggest that, among a number of dairy protein-derived peptides isolated and characterized as bioactive compounds in vitro, some peptides can be active in vivo post-oral administration through a local action in the gut, or, alternatively, a systemic action on specific molecular targets after entering the systemic circulation. Moreover, these studies highlight the importance of the enteroendocrine system in the cross talk between food proteins and the neuroendocrine network regulating energy balance.

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Flavone Hispidulin Stimulates Glucagon‐Like Peptide‐1 Secretion and Ameliorates Hyperglycemia in Streptozotocin‐Induced Diabetic Mice

Wang

Alkhalidy

et al. 2020

Molecular Nutrition Food Res

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Scope Loss of functional β‐cell mass is central for the deterioration of glycemic control in diabetes. The incretin hormone glucagon‐like peptide‐1 (GLP‐1) plays a critical role in maintaining glycemic homeostasis via potentiating glucose‐stimulated insulin secretion and promoting β‐cell mass. Agents that can directly promote GLP‐1 secretion, thereby increasing insulin secretion and preserving β‐cell mass, hold great potential for the treatment of T2D. Methods and results GluTag L‐cells, INS832/13 cells, and mouse ileum crypts and islets are cultured for examining the effects of flavone hispidulin on GLP‐1 and insulin secretion. Mouse livers and isolated hepatocytes are used for gluconeogenesis. Streptozotocin‐induced diabetic mice are treated with hispidulin (20 mg kg−1 day−1, oral gavage) for 6 weeks to evaluate its anti‐diabetic potential. Hispidulin stimulates GLP‐1 secretion from the L‐cell line, ileum crypts, and in vivo. This hispidulin action is mediated via activation of cyclic adenosine monophosphate/protein kinase A signaling. Hispidulin significantly improves glycemic control in diabetic mice, concomitant with improved insulin release, and β‐cell survival. Additionally, hispidulin decreases hepatic pyruvate carboxylase expression in diabetic mice and suppresses gluconeogenesis in hepatocytes. Furthermore, hispidulin stimulates insulin secretion from β‐cells. Conclusion These findings suggest that Hispidulin may be a novel dual‐action anti‐diabetic compound via stimulating GLP‐1 secretion and suppressing hepatic glucose production.

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A casein hydrolysate increases GLP-1 secretion and reduces food intake

Cited by 28 publications

References 34 publications

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Role of Bioactive Peptide Sequences in the Potential Impact of Dairy Protein Intake on Metabolic Health

Flavone Hispidulin Stimulates Glucagon‐Like Peptide‐1 Secretion and Ameliorates Hyperglycemia in Streptozotocin‐Induced Diabetic Mice

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