Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases

Fernández-Musoles, Ricardo; Salom, Juan B.; Castelló-Ruiz, María; Contreras, María del Mar; Recio, Isidra; Manzanares, Paloma

doi:10.1016/j.idairyj.2013.05.009

Cited by 51 publications

(60 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is because hydrophobic DBPs must interact with the apical lipid surface via hydrophobic interactions prior to internalization (Shimizu et al ., ). To study the role of transcytosis in transport of DBPs, transcytosis is often inhibited using wortmannin, an inhibitor of phosphoinositide 3‐kinase (Quirós et al ., ; Fernández‐Musoles et al ., ; Vij et al ., ; Wang & Li, ).…”

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

“…The human GIT has many paracellular diffusion pores, also called TJs consisting of zonula occludens‐1, occludin and claudin proteins. Table shows that a variety of DBPs are transported by the energy‐independent paracellular route via TJs (Quirós et al ., ), such as His‐Leu‐Pro‐Leu‐Pro (HLPLP; Quirós et al ., ), Lys‐Val‐Leu‐Pro‐Val‐Pro (KVLPVP; Sun et al ., ), LKP (Gleeson et al ., , ; Xu et al ., ), Arg‐Leu‐Ser‐Phe‐Asn‐Pro (RLSFNP; Guo et al ., ), Arg‐Trp‐Gln (RWQ), Trp‐Gln (WQ; Fernández‐Musoles et al ., ), Ser‐Arg‐Tyr‐Pro‐Ser‐Tyr (SRYPSY), Tyr‐Pro‐Phe‐Pro‐Gly (YPFPG), Tyr‐Pro‐Phe‐Pro‐Gly‐Pro‐Ile (YPFPGPI; Sienkiewicz‐Szłapka et al ., ), Val‐Leu‐Pro‐Val‐Pro (VLPVP; Lei et al ., ) and VPP (Satake et al ., ). However, β‐casein‐f(193–209) cannot be transported via diffusion due to its long length and hydrophobicity (Regazzo et al ., ).…”

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

“…Moreover, dipeptides Gly-Sar and Gly-Pro are PepT1 substrates, therefore, they could competitively bind PepT1 pocket and thus could interfere other peptides' transport by PepT1. All these compounds inhibit the peptide-binding activity of PepT1 and are often used to explore the role of PepT1 in DBP transport (Table 3; Quir os et al, 2008; Regazzo et al, 2010;Fern andez-Musoles et al, 2013;Vij et al, 2016).…”

Section: Pept1-mediated Routementioning

confidence: 99%

See 2 more Smart Citations

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Yan

Zhang

et al. 2018

Int J of Food Sci Tech

View full text Add to dashboard Cite

Summary Dairy protein‐derived bioactive peptides (DBPs) have potential benefits for human health. However, their transport mechanisms and bioavailability from intestinal lumen to bloodstream are not well understood. This review summarises current understanding of their transport mechanisms across the intestinal membrane (peptide transport 1, paracellular route, transcytosis and passive transcellular diffusion) and the bioavailability of DBPs in animal and human studies. Some DBPs can escape the degradation of peptidase and reach the bloodstream at concentrations of micromolar range, and keep intact for several minutes to hours. The presences of brush‐border peptidases at the site of absorption and other peptidases in the blood, along with the peptide properties, such as molecular size and weight, stability to proteases, hydrophobicity and charge, determine their bioavailability. Developing novel analytical tools for accurate measurement and study of the transport, metabolism, and bioavailability of DBPs in vivo are expected.

show abstract

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

Section: Transport Mechanism Of Dbps Across the Intestinal Brush‐bordmentioning

confidence: 99%

Section: Pept1-mediated Routementioning

confidence: 99%

See 1 more Smart Citation

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Yan

Zhang

et al. 2018

Int J of Food Sci Tech

View full text Add to dashboard Cite

show abstract

“…Therefore, it is possible for RLSFNP to transport through paracellular tight junctions. Recently, paracellular transport was reported to be a common route for several intact ACE‐inhibitory peptides with different peptide sequence lengths, such as antihypertensive lactoferricin BRWQ and WQ and intact HLPLP . We assumed that ACE‐inhibitory peptides could remain intact after passing through a tight junction via a paracellular route, but if they were taken into a Caco‐2 cell they might be hydrolyzed by intracellular peptidase.…”

Section: Resultsmentioning

confidence: 99%

Transepithelial transport of milk‐derived angiotensin I‐converting enzyme inhibitory peptide with the RLSFNP sequence

et al. 2017

View full text Add to dashboard Cite

show abstract

“…TJs in Caco-2 cell line monolayers have a diameter of approximately 2.1 nm and thus they cannot transport peptide larger than their pore size (Linnankoski et al, 2010;Shimizu, Tsunogai, & Arai, 1997). Paracellular route via TJ is also common in the absorption of di-and tripeptides (Fernandez-Musoles et al, 2013). Besides, some peptides are transported by both active and passive routes (Xu, Fan, Yu, Hong, & Wu, 2017).…”

Section: The Bioavailability Of Ipp and Vppmentioning

confidence: 99%

Preparation, Bioavailability, and Mechanism of Emerging Activities of Ile‐Pro‐Pro and Val‐Pro‐Pro

Zheng

et al. 2019

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

Ile‐Pro‐Pro and Val‐Pro‐Pro are two most well‐known food‐derived bioactive peptides, initially identified as inhibitors of angiotensin I‐converting enzyme (ACE) from a sample of sour milk. These two peptides were identified in fermented and enzymatic hydrolyzed cow and non‐cow (that is, goat, sheep, buffalo, yak, camel, mare, and donkey) milk, as well as sourdough prepared from wheat, rye, and malt. Similar to other bioactive peptides, bioavailability of these peptides is low (about 0.1%), reaching picomolar concentration in human plasma; they showed blood pressure lowering activity in animals and in human, via improved endothelial function, activation of ACE2, and anti‐inflammatory property. Emerging bioactivities of these two peptides toward against metabolic syndrome and bone‐protection received limited attention, but may open up new applications of these peptides as functional food ingredients. Further studies are warranted to determine the best source as well as to identify novel enzymes (particularly from traditional fermented milk products) to improve the efficiency of production, to characterize possible peptide receptors using a combination of omics technology with molecular methods to understand if these two peptides act as signal‐like molecules, to improve their bioavailability, and to explore new applications based on emerging bioactivities.

show abstract

Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases

Cited by 51 publications

References 39 publications

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Current understanding of transport and bioavailability of bioactive peptides derived from dairy proteins: a review

Transepithelial transport of milk‐derived angiotensin I‐converting enzyme inhibitory peptide with the RLSFNP sequence

Preparation, Bioavailability, and Mechanism of Emerging Activities of Ile‐Pro‐Pro and Val‐Pro‐Pro

Contact Info

Product

Resources

About