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Bo Lönnerdal - One of the best experts on this subject based on the ideXlab platform.
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bioactive peptides derived from human Milk Proteins an update
Current Opinion in Clinical Nutrition and Metabolic Care, 2020Co-Authors: Yasuaki Wada, Bo LönnerdalAbstract:Purpose of review Human Milk contains a variety of bioactive Proteins, and some of the bioactivities are exerted only after Proteins are digested in the gastrointestinal tract. This review aims to overview recent studies on bioactive peptides in human Milk and gastric digesta of breast-fed infants. Recent findings Milk protein-derived peptides are endogenously present in human Milk, and some of them have been reported to be bioactive peptides, such as a homologue of caseinophosphopeptide, an antimicrobial peptide, and an immunomodulatory peptide. A larger number of peptides are identified in gastric aspirates from breast-fed infants, and bioactive peptides such as angiotensin I-converting enzyme-inhibitory peptides, an antioxidative peptide, opioid agonist peptides are only found in the digesta of human Milk but not in human Milk per se. Casein is the greatest source of released bioactive peptides. Summary Technological advances have considerably increased our capability to identify and characterize peptides derived from human Milk Proteins. However, their physiological significance and the roles of these bioactive peptides in growth and development of breast-fed infants have not yet been sufficiently elucidated, and further in-vivo experiments and clinical trials are warranted.
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in vivo digestomics of Milk Proteins in human Milk and infant formula using a suckling rat pup model
Peptides, 2017Co-Authors: Yasuaki Wada, Brett S Phinney, Darren Weber, Bo LönnerdalAbstract:Human Milk is the optimal mode of infant feeding for the first several months of life, and infant formulas serve as an alternative when breast-feeding is not possible. Milk Proteins have a balanced amino acid composition and some of them provide beneficial bioactivities in their intact forms. They also encrypt a variety of bioactive peptides, possibly contributing to infant health and growth. However, there is limited knowledge of how Milk Proteins are digested in the gastrointestinal tract and bioactive peptides are released in infants. A peptidomic analysis was conducted to identify peptides released from Milk Proteins in human Milk and infant formula, using a suckling rat pup model. Among the major Milk Proteins targeted, α-lactalbumin and β-casein in human Milk, and β-lactoglobulin and β-casein in infant formula were the main sources of peptides, and these peptides covered large parts of the parental Proteins' sequences. Release of peptides was concentrated to specific regions, such as residues 70-92 of β-casein in human Milk, residues 39-55 of β-lactoglobulin in infant formula, and residues 57-96 and 145-161 of β-CN in infant formula, where resistance to gastrointestinal digestion was suggested. In the context of bioactive peptides, release of fragments containing known bioactive peptides was confirmed, such as β-CN-derived opioid and antihypertensive peptides. It is therefore likely that these fragments are of biological significance in neonatal health and development.
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Bioactive peptides derived from human Milk Proteins - mechanisms of action
Journal of Nutritional Biochemistry, 2014Co-Authors: Yasuaki Wada, Bo LönnerdalAbstract:Human Milk contains a multitude of bioactive Proteins with very diverse functions, which are beneficial for the rapidly growing neonate. The large variety of bioactivities is accomplished by the combination of bioactive Proteins per se and gastrointestinal release of bioactive peptides derived from them. The bioactivities exerted by these peptides include enhancement of mineral absorption, immunomodulation, opioid, antihypertensive and antimicrobial activities. Notably, several of the activities are not attributed to the parental Proteins, but exclusively to released bioactive peptides. This article reviews studies on bioactive peptides derived from major human Milk Proteins, such as caseins, α-lactalbumin and lactoferrin, during gastrointestinal digestion. Studies of bovine Milk counterparts are also cited as a comparison. © 2014.
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Human Milk Proteins
Advances in Experimental Medicine and Biology, 2004Co-Authors: Bo LönnerdalAbstract:Human Milk contains a wide array of Proteins that provide biologic activities ranging from antimicrobial effects to immunostimulatory functions. Proteins like lactoferrin, secretory IgA, κ-casein, lactoperoxidase, haptocorrin, lactadherin and peptides formed from human Milk Proteins during digestion can inhibit the growth of pathogenic bacteria and viruses and therefore protect against infection. At the same time, Proteins like lactoferrin, bile-salt stimulated lipase, haptocorrin, κ-casein, and folate-binding protein can facilitate the absorption of nutrients in the neonatal gut. However, the Proteins in human Milk themselves also provide adequate amounts of essential amino acids to the growing infant. This suggests a highly adapted digestive system, which allows the survival of some Proteins and peptides in the upper gastrointestinal tract, while still allowing amino acid utilization from these Proteins further down in the gut. It is now possible to produce recombinant human Milk Proteins in transgenic plants and animals, which makes it possible to further study the bioactivity of these Proteins. Provided these Proteins can be produced in large scale at low cost, that they show biologic activity and pose no safety concerns, it may be possible to add some human Milk Proteins to infant diets, such as formula and complementary foods. Human Milk Proteins produced in rice or potatoes, for example, could be added without much purification, because these staples commonly are used in weaning foods. Thus, some qualities provided by human Milk may be included into other diets, although it is highly unlikely that all unique components of human Milk can be copied this way.
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Human Milk Proteins: key components for the biological activity of human Milk.
Advances in experimental medicine and biology, 2004Co-Authors: Bo LönnerdalAbstract:Human Milk contains a wide array of Proteins that provide biologic activities ranging from antimicrobial effects to immunostimulatory functions. Proteins like lactoferrin, secretory IgA, kappa-casein, lactoperoxidase, haptocorrin, lactadherin and peptides formed from human Milk Proteins during digestion can inhibit the growth of pathogenic bacteria and viruses and therefore protect against infection. At the same time, Proteins like lactoferrin, bile-salt stimulated lipase, haptocorrin, kappa-casein, and folate-binding protein can facilitate the absorption of nutrients in the neonatal gut. However, the Proteins in human Milk themselves also provide adequate amounts of essential amino acids to the growing infant. This suggests a highly adapted digestive system, which allows the survival of some Proteins and peptides in the upper gastrointestinal tract, while still allowing amino acid utilization from these Proteins further down in the gut. It is now possible to produce recombinant human Milk Proteins in transgenic plants and animals, which makes it possible to further study the bioactivity of these Proteins. Provided these Proteins can be produced in large scale at low cost, that they show biologic activity and pose no safety concerns, it may be possible to add some human Milk Proteins to infant diets, such as formula and complementary foods. Human Milk Proteins produced in rice or potatoes, for example, could be added without much purification, because these staples commonly are used in weaning foods. Thus, some qualities provided by human Milk may be included into other diets, although it is highly unlikely that all unique components of human Milk can be copied this way.
H. Meisel - One of the best experts on this subject based on the ideXlab platform.
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biochemical properties of peptides encrypted in bovine Milk Proteins
Current Medicinal Chemistry, 2005Co-Authors: H. MeiselAbstract:Milk Proteins are precursors of many different biologically active peptides. These peptides are inactive within the protein sequence, requiring enzymatic proteolysis for release of the bioactive fragment from the Proteins precursor. It is evident that activated peptides originating from Milk Proteins should be taken into account as potential modulators of various regulatory processes in the body. Activated peptides are potential modulators of various regulatory processes in the living system: immunomodulatory peptides stimulate the activities of cells of the immune system and several cytomodulatory peptides inhibit cancer cell growth, antimicrobial peptides kill sensitive microorganisms, angiotensin-I-converting enzyme (ACE)-inhibitory peptides exert an hypotensive effect, opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, mineral binding peptides may function as carriers for different minerals, especially calcium, antithrombotic peptides inhibit fibrinogen binding to a specific receptor region on the platelet surface and inhibit aggregation of platelets. Moreover, many Milk-derived peptides reveal multifunctional properties, i.e. specific peptide sequences having two or more different biological activities have been reported. Bioactive peptides can interact with target sites (e.g. receptors, enzymes) at the luminal side of the intestinal tract, or they could be absorbed and reach any potential site of action in the system to elicit physiological effects. Bioactive peptides encrypted in bovine Milk Proteins can be produced on an industrial-scale and are claimed to be health enhancing components for functional foods, nutraceuticals and pharmaceutical preparations that are used to reduce risk of disease or to enhance certain physiological functions.
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Multifunctional peptides encrypted in Milk Proteins
BioFactors, 2004Co-Authors: H. MeiselAbstract:Many bioactivities of Milk are latent in that they are inactive within the protein sequence, requiring enzymatic proteolysis for release of bioactive peptides from Milk Proteins precursors. Bioactivities of peptides encrypted in major Milk Proteins are latent until released and activated, e.g. during gastrointestinal digestion or food processing. Bioactive peptides can be produced in vivo following intake of Milk Proteins, and the proteolytic system of bacterial species used in the production of fermented Milk products and cheese can contribute to the liberation of bioactive peptides or precursors thereof. Activated peptides are potential modulators of various regulatory processes in the living system: immunomodulatory peptides stimulate the activities of cells of the immune system and several cytomodulatory peptides inhibit cancer cell growth, antimicrobial peptides kill sensitive microorganisms, angiotensin-I-converting enzyme (ACE)-inhibitory peptides exert an hypotensive effect, opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, mineral binding peptides may function as carriers for different minerals, especially calcium. Many Milk-derived peptides reveal multifunctional properties, i.e. specific peptide sequences having two or more different biological activities have been reported. Milk protein-derived bioactive peptides are claimed to be health enhancing components that can be used to reduce the risk of disease or to enhance a certain physiological function.
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biofunctional peptides from Milk Proteins mineral binding and cytomodulatory effects
Current Pharmaceutical Design, 2003Co-Authors: H. Meisel, Richard J FitzgeraldAbstract:The protein fraction of Milk contains many valuable components and biologically active substances. Moreover, Milk Proteins are precursors of many different biologically active peptides which are inactive within the sequence of the precursor protein but can be released by enzymatic proteolysis. Many Milk protein-derived peptides, such as caseinophosphopeptides, reveal multi-functional bioactivities. Caseinophosphopeptides can form soluble organophosphate salts and may function as carriers for different minerals, especially calcium. Furthermore, they have been shown to exert cytomodulatory effects. Cytomodulatory peptides inhibit cancer cell growth or they stimulate the activity of immunocompetent cells and neonatal intestinal cells, respectively. Several bioactive peptides derived from Milk Proteins are potential modulators of various regulatory processes in the body and thus may exert beneficial physiological effects. Caseinophosphopeptides are already produced on an industrial-scale and as a consequence these peptides have been considered for application as ingredients in both 'functional foods' and pharmaceutical preparations. Although the physiological significance as exogenous regulatory substances is not yet fully understood, both mineral binding and cytomodulatory peptides derived from bovine Milk Proteins are claimed to be health enhancing components that can be used to reduce the risk of disease or to enhance a certain physiological function.
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stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine Milk Proteins
FEBS Letters, 1996Co-Authors: Holger Kayser, H. MeiselAbstract:The in vitro modulation of the proliferation of human peripheral blood lymphocytes by different synthetic peptides derived from Milk Proteins was investigated. Therefore, proliferation changes were followed up after incorporation of BrdU into the DNA, and the influence on protein biosynthesis was measured using the [3H]leucine incorporation test. Tyr-Gly and Tyr-Gly-Gly significantly enhanced (maximal 90 and 35%, respectively) the proliferation of PBL. For beta-casomorphin-7 and beta-casomorphin-10,lymphocyte proliferation was suppressed at lower concentrations, but stimulated at higher concentrations (> or = 10(-7) mol/l). Protein synthesis was stimulated (maxima at 25%) only with Tyr-Gly and Tyr-Gly-Gly. The findings point to a need for further studies on the possible function of peptides derived from Milk Proteins as orally bioavailable immunopotentiatory compounds.
Carlito B Lebrilla - One of the best experts on this subject based on the ideXlab platform.
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human Milk Proteins and their glycosylation exhibit quantitative dynamic variations during lactation
Journal of Nutrition, 2019Co-Authors: Elisha Goonatilleke, Jincui Huang, Jennifer T. Smilowitz, Bruce J German, Carlito B LebrillaAbstract:BACKGROUND Proteins in human Milk are essential and known to support the growth, development, protection, and health of the newborn. These Proteins are highly modified by glycans that are currently being recognized as vital to protein structure, stability, function, and health of the intestinal mucosa. Although Milk Proteins have been studied, the quantitative changes in Milk Proteins and their respective site-specific glycosylation are unknown. OBJECTIVE This study expanded the analytical tools for Milk Proteins and their site-specific glycosylation and applied these tools to a large cohort to determine changes in individual protein concentrations and their site-specific N-glycosylation across lactation. DESIGN A tandem mass spectrometry method was applied to 231 breast-Milk samples from 33 mothers in Davis, California, obtained during 7 different periods of lactation. Dynamic changes in the absolute abundances of Milk Proteins, as well as variation in site-specific N-glycosylation of individual Proteins, were quantified. RESULTS α-Lactalbumin, β-casein, k-casein, and α-antitrypsin were significantly increased from colostrum to transitional Milk (4.37 ± 1.33 g/L to 6.41 ± 0.72 g/L, 2.25 ± 0.86 g/L to 2.59 ± 0.78 g/L, 1.33 ± 0.44 g/L to 1.60 ± 0.39 g/L, and 0.09 ± 0.10 g/L to 0.11 ± 0.04 g/L, respectively; P < 0.002). α-Lactalbumin (37%), β-casein (9%), and lysozyme (159%) were higher in mature Milk than in colostrum. Glycans exhibited different behavior. Fucosylated glycans of lactoferrin and high-mannose, undecorated, fucosylated, sialylated, and combined fucosylated + sialylated glycans of secretory immunoglobulin A increased during lactation even when the concentrations of the parent Proteins decreased. CONCLUSIONS Proteins in healthy mothers vary dynamically through lactation to support the development of infants. Individual Milk Proteins carried unique glycan modifications that varied systematically in structure even with site specificity. The role of glycosylation in human Milk Proteins will be important in understanding the functional components of human Milk. This trial was registered at clinicaltrials.gov as NCT01817127.
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quantitation of human Milk Proteins and their glycoforms using multiple reaction monitoring mrm
Analytical and Bioanalytical Chemistry, 2017Co-Authors: Jincui Huang, Jennifer T. Smilowitz, Muchena J Kailemia, Elisha Goonatilleke, Evan A Parker, Qiuting Hong, Rocchina Sabia, Bruce J German, Carlito B LebrillaAbstract:Human Milk plays a substantial role in the child growth, development and determines their nutritional and health status. Despite the importance of the Proteins and glycoProteins in human Milk, very little quantitative information especially on their site-specific glycosylation is known. As more functions of Milk Proteins and other components continue to emerge, their fine-detailed quantitative information is becoming a key factor in Milk research efforts. The present work utilizes a sensitive label-free MRM method to quantify seven Milk Proteins (α-lactalbumin, lactoferrin, secretory immunoglobulin A, immunoglobulin G, immunoglobulin M, α1-antitrypsin, and lysozyme) using their unique peptides while at the same time, quantifying their site-specific N-glycosylation relative to the protein abundance. The method is highly reproducible, has low limit of quantitation, and accounts for differences in glycosylation due to variations in protein amounts. The method described here expands our knowledge about human Milk Proteins and provides vital details that could be used in monitoring the health of the infant and even the mother.
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quantitation of human Milk Proteins and their glycoforms using multiple reaction monitoring mrm
Analytical and Bioanalytical Chemistry, 2017Co-Authors: Jincui Huang, Jennifer T. Smilowitz, Muchena J Kailemia, Elisha Goonatilleke, Evan A Parker, Qiuting Hong, Rocchina Sabia, Bruce J German, Carlito B LebrillaAbstract:Human Milk plays a substantial role in the child growth, development and determines their nutritional and health status. Despite the importance of the Proteins and glycoProteins in human Milk, very little quantitative information especially on their site-specific glycosylation is known. As more functions of Milk Proteins and other components continue to emerge, their fine-detailed quantitative information is becoming a key factor in Milk research efforts. The present work utilizes a sensitive label-free MRM method to quantify seven Milk Proteins (α-lactalbumin, lactoferrin, secretory immunoglobulin A, immunoglobulin G, immunoglobulin M, α1-antitrypsin, and lysozyme) using their unique peptides while at the same time, quantifying their site-specific N-glycosylation relative to the protein abundance. The method is highly reproducible, has low limit of quantitation, and accounts for differences in glycosylation due to variations in protein amounts. The method described here expands our knowledge about human Milk Proteins and provides vital details that could be used in monitoring the health of the infant and even the mother. Graphical Abstract The glycopeptides EICs generated from QQQ.
Yasuaki Wada - One of the best experts on this subject based on the ideXlab platform.
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bioactive peptides derived from human Milk Proteins an update
Current Opinion in Clinical Nutrition and Metabolic Care, 2020Co-Authors: Yasuaki Wada, Bo LönnerdalAbstract:Purpose of review Human Milk contains a variety of bioactive Proteins, and some of the bioactivities are exerted only after Proteins are digested in the gastrointestinal tract. This review aims to overview recent studies on bioactive peptides in human Milk and gastric digesta of breast-fed infants. Recent findings Milk protein-derived peptides are endogenously present in human Milk, and some of them have been reported to be bioactive peptides, such as a homologue of caseinophosphopeptide, an antimicrobial peptide, and an immunomodulatory peptide. A larger number of peptides are identified in gastric aspirates from breast-fed infants, and bioactive peptides such as angiotensin I-converting enzyme-inhibitory peptides, an antioxidative peptide, opioid agonist peptides are only found in the digesta of human Milk but not in human Milk per se. Casein is the greatest source of released bioactive peptides. Summary Technological advances have considerably increased our capability to identify and characterize peptides derived from human Milk Proteins. However, their physiological significance and the roles of these bioactive peptides in growth and development of breast-fed infants have not yet been sufficiently elucidated, and further in-vivo experiments and clinical trials are warranted.
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in vivo digestomics of Milk Proteins in human Milk and infant formula using a suckling rat pup model
Peptides, 2017Co-Authors: Yasuaki Wada, Brett S Phinney, Darren Weber, Bo LönnerdalAbstract:Human Milk is the optimal mode of infant feeding for the first several months of life, and infant formulas serve as an alternative when breast-feeding is not possible. Milk Proteins have a balanced amino acid composition and some of them provide beneficial bioactivities in their intact forms. They also encrypt a variety of bioactive peptides, possibly contributing to infant health and growth. However, there is limited knowledge of how Milk Proteins are digested in the gastrointestinal tract and bioactive peptides are released in infants. A peptidomic analysis was conducted to identify peptides released from Milk Proteins in human Milk and infant formula, using a suckling rat pup model. Among the major Milk Proteins targeted, α-lactalbumin and β-casein in human Milk, and β-lactoglobulin and β-casein in infant formula were the main sources of peptides, and these peptides covered large parts of the parental Proteins' sequences. Release of peptides was concentrated to specific regions, such as residues 70-92 of β-casein in human Milk, residues 39-55 of β-lactoglobulin in infant formula, and residues 57-96 and 145-161 of β-CN in infant formula, where resistance to gastrointestinal digestion was suggested. In the context of bioactive peptides, release of fragments containing known bioactive peptides was confirmed, such as β-CN-derived opioid and antihypertensive peptides. It is therefore likely that these fragments are of biological significance in neonatal health and development.
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Bioactive peptides derived from human Milk Proteins - mechanisms of action
Journal of Nutritional Biochemistry, 2014Co-Authors: Yasuaki Wada, Bo LönnerdalAbstract:Human Milk contains a multitude of bioactive Proteins with very diverse functions, which are beneficial for the rapidly growing neonate. The large variety of bioactivities is accomplished by the combination of bioactive Proteins per se and gastrointestinal release of bioactive peptides derived from them. The bioactivities exerted by these peptides include enhancement of mineral absorption, immunomodulation, opioid, antihypertensive and antimicrobial activities. Notably, several of the activities are not attributed to the parental Proteins, but exclusively to released bioactive peptides. This article reviews studies on bioactive peptides derived from major human Milk Proteins, such as caseins, α-lactalbumin and lactoferrin, during gastrointestinal digestion. Studies of bovine Milk counterparts are also cited as a comparison. © 2014.
David C. Dallas - One of the best experts on this subject based on the ideXlab platform.
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Milk Proteins Are Predigested Within the Human Mammary Gland
Journal of Mammary Gland Biology and Neoplasia, 2017Co-Authors: Soren D Nielsen, Robert L Beverly, David C. DallasAbstract:Previous work demonstrates that proteases present in human Milk release hundreds of peptides derived from Milk Proteins. However, the question of whether human Milk protein digestion begins within the mammary gland remains incompletely answered. The primary objective of this study was to determine whether proteolytic degradation of human Milk Proteins into peptides begins within the mammary gland. The secondary objectives were to determine which Milk proteases participate in the proteolysis and to predict which released peptides have bioactivity. Lactating mothers ( n = 4) expressed their Milk directly into a mixture of antiproteases on ice followed by immediate freezing of the Milk to limit post-expression protease activity. Samples were analyzed for their peptide profiles via mass spectrometry and database searching. Peptidomics-based protease prediction and bioactivity prediction were each performed with several different approaches. The findings demonstrate that human Milk contains more than 1,100 unique peptides derived from Milk protein hydrolysis within the mammary gland. These peptides derived from 42 Milk Proteins and included 306 potential bioactive peptides. Based on the peptidomics data, plasmin was predicted to be the Milk protease most active in the hydrolysis of human Milk Proteins within the mammary gland. Milk proteases actively cleave Milk Proteins within the mammary gland, initiating the release of functional peptides. Thus, the directly breastfed infant receives partially pre-digested Proteins and numerous bioactive peptides.
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Peptidomic analysis reveals proteolytic activity of kefir microorganisms on bovine Milk Proteins
Food Chemistry, 2016Co-Authors: David C. Dallas, Florine Citerne, Vitor L.m. Silva, Steven A. Frese, Randall C Robinson, Karen M Kalanetra, David A Mills, Tian Tian, Daniela BarileAbstract:Scope The microorganisms that make up kefir grains are well known for lactose fermentation, but the extent to which they hydrolyze and consume Milk Proteins remains poorly understood. Peptidomics technologies were used to examine the proteolytic activity of kefir grains on bovine Milk Proteins. Methods and results Gel electrophoresis revealed substantial digestion of Milk Proteins by kefir grains, with mass spectrometric analysis showing the release of 609 protein fragments and alteration of the abundance of >1500 peptides that derived from 27 Milk Proteins. Kefir contained 25 peptides identified from the literature as having biological activity, including those with antihypertensive, antimicrobial, immunomodulatory, opioid and anti-oxidative functions. 16S rRNA and shotgun metagenomic sequencing identified the principle taxa in the culture as Lactobacillus species. Conclusion The model kefir sample contained thousands of protein fragments released in part by kefir microorganisms and in part by native Milk proteases.