Pharmacokinetics of proline-rich tripeptides in the pig

Pijl, Pieter C. van der; Kies, Arie K.; Have, Gabriella A.M. Ten; Duchateau, Guus; Deutz, N.E.P.

doi:10.1016/j.peptides.2008.08.011

Cited by 60 publications

(59 citation statements)

References 30 publications

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“…Foltz et al [160] investigated the transport of Ile-Pro-Pro and ValPro-Pro by using three different absorption models and demonstrated that these tri-peptides are transported in small amounts intact across the barrier of the intestinal epithelium. In another study, the absolute bioavailability of the tri-peptides in pigs was below 0.1%, with an extremely short elimination half-life ranging from 5 to 20 min [161]. In humans, maximal plasma concentration did not exceed picomolar concentration [162].…”

Section: Bioavailabilitymentioning

confidence: 90%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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Section: Bioavailabilitymentioning

confidence: 90%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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“…Half-lives of absorption and elimination for these peptides were about 5 and 15 min respectively [62]. Absorption of intact proteins and peptides was also shown in a study with dogs exposed to intraduodenal infusion of somatostatin.…”

Section: Fate Of Dietary Proteins In the Gastrointestinal Tractmentioning

confidence: 95%

“…Some studies report that the mammalian small intestine can absorb gamma-globulins and other milk proteins [61], while some others reported limited post-absorptive bioavailability of peptides [62]. In humans, the peptides Valine-Proline-Proline (VPP) and Isoleucine-Proline-Proline (IPP) were detected undegraded in the plasma following the consumption of a lactotripeptide-enriched yogurt beverage [63].…”

Section: Fate Of Dietary Proteins In the Gastrointestinal Tractmentioning

confidence: 99%

Dietary Proteins as Determinants of Metabolic and Physiologic Functions of the Gastrointestinal Tract

et al. 2011

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Dietary proteins elicit a wide range of nutritional and biological functions. Beyond their nutritional role as the source of amino acids for protein synthesis, they are instrumental in the regulation of food intake, glucose and lipid metabolism, blood pressure, bone metabolism and immune function. The interaction of dietary proteins and their products of digestion with the regulatory functions of the gastrointestinal (GI) tract plays a dominant role in determining the physiological properties of proteins. The site of interaction is widespread, from the oral cavity to the colon. The characteristics of proteins that influence their interaction with the GI tract in a source-dependent manner include their physico-chemical properties, their amino acid composition and sequence, their bioactive peptides, their digestion kinetics and also the non-protein bioactive components conjugated with them. Within the GI tract, these products affect several regulatory functions by interacting with receptors releasing hormones, affecting stomach emptying and GI transport and absorption, transmitting neural signals to the brain, and modifying the microflora. This review discusses the interaction of dietary proteins during digestion and absorption with the physiological and metabolic functions of the GI tract, and illustrates the importance of this interaction in the regulation of amino acid, glucose, lipid metabolism, and food intake.

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“…Similarly, the use of HPLC-multiple reaction monitoring mass spectrometry (HPLC-MRM-MS) confirmed the presence of the peptides AW, VF, VY, IWR, HLP, LPP, VPP, LPPR and HLPLP in human plasma [132]. However, a recent study [129] investigating the pharmacokinetics of intravenously or intragastrically administered synthetic IPP, LPP and VPP in pigs showed that the absolute bioavailability of intragastrically infused tripeptides was only about 0.1%, and that half-lives of absorption and elimination were maximally about 5 and 15 min, respectively. This study concluded that under these conditions, the bioactive effect of these tripeptides would be rather acute.…”

Section: Digestion and Absorption Of Orally Active Peptidesmentioning

confidence: 97%

ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

Sieber

Bütikofer

Egger

et al. 2009

Dairy Sci. Technol.

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-During the ripening of cheese, a large number of peptides are formed from casein. Some of these peptides have been shown to exert an antihypertensive effect due to their angiotensin-I-converting enzyme (ACE)-inhibitory activity. Recently, several studies have investigated the ACE-inhibiting potential of cheese, and various ACE-inhibiting peptides have been isolated and identified from different cheese varieties. The present review focuses on the occurrence of two tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in cheese. These tripeptides were first described in fermented-milk products and have been demonstrated to exert a blood pressure-lowering effect in humans with mild hypertension. The influence of cheesemaking and ripening on the release of ACE-inhibiting peptides is revealed. Finally, the antihypertensive potential of cheese with high ACE-inhibitory activity is discussed with regard to the bioavailability of the peptides involved.

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Pharmacokinetics of proline-rich tripeptides in the pig

Cited by 60 publications

References 30 publications

Antihypertensive Properties of Plant Protein Derived Peptides

Antihypertensive Properties of Plant Protein Derived Peptides

Dietary Proteins as Determinants of Metabolic and Physiologic Functions of the Gastrointestinal Tract

ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

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