Ser71 of αS1‐Casein is Phosphorylated in Breast Milk—Evidence from Targeted Mass Analysis

König, Simone; Altendorfer, Irina; Saenger, Thorsten; Bleck, Ellen; Vordenbäumen, Stefan; Schneider, Matthias; Jose, Joachim

doi:10.1002/mnfr.201700496

Cited by 5 publications

(6 citation statements)

References 28 publications

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“…Therefore, S 33 and S 41 could be more easily accessible for kinases. In accordance, it was found before that S 33 and S 41 of human αS1-casein [31] and stretch 85-102 of bovine αS1-casein were phosphorylated in significant amounts. Opposite to this, only low levels of phosphorylation were described for the hydrophobic stretch 83-102 of human αS1-casein, especially for S 89 [14,31].…”

Section: Hydrophobicity Analysis Of Human αS1-casein and Comparison W...supporting

confidence: 90%

“…In accordance, it was found before that S 33 and S 41 of human αS1-casein [31] and stretch 85-102 of bovine αS1-casein were phosphorylated in significant amounts. Opposite to this, only low levels of phosphorylation were described for the hydrophobic stretch 83-102 of human αS1-casein, especially for S 89 [14,31]. The low level of phosphorylation in stretch 83-102 of human αS1-casein indicated that it was less accessible for kinases, although it was found to be more hydrophobic than in bovine αS1-casein.…”

Section: Hydrophobicity Analysis Of Human αS1-casein and Comparison W...supporting

confidence: 90%

“…It can be assumed that αS1-casein present in colostrum breast milk is unphosphorylated because, in a former analysis, high ratios of peptides with phosphorylation sites were detected in their unphosphorylated form [31].…”

Section: Prediction and Probability For Intrinsically Disordered Regi...mentioning

confidence: 99%

“…As shown in Figure 5A, the spectrum as obtained showed typical minima for high α-helical content of a protein at 207 nm (−729,060 Grad•cm 2 •dmol −1 ) and 222 nm (−489,105 Grad•cm 2 •dmol −1 ) with a ratio (222 nm/208 nm) of 0.74 (Figure 5A). To estimate It can be assumed that α S1 -casein present in colostrum breast milk is unphosphorylated because, in a former analysis, high ratios of peptides with phosphorylation sites were detected in their unphosphorylated form [31].…”

Section: Secondary Structure Analysis Of Human αS1-casein By Spectros...mentioning

confidence: 99%

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Structural Analysis of Breast-Milk αS1-Casein: An α-Helical Conformation Is Required for TLR4-Stimulation

Saenger,

Schulte,

Vordenbäumen

et al. 2024

IJMS

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Breast-milk αS1-casein is a Toll-like receptor 4 (TLR4) agonist, whereas phosphorylated αS1-casein does not bind TLR4. The objective of this study was to analyse the structural requirements for these effects. In silico analysis of αS1-casein indicated high α-helical content with coiled-coil characteristics. This was confirmed by CD-spectroscopy, showing the α-helical conformation to be stable between pH 2 and 7.4. After in vitro phosphorylation, the α-helical content was significantly reduced, similar to what it was after incubation at 80 °C. This conformation showed no in vitro induction of IL-8 secretion via TLR4. A synthetic peptide corresponding to V77-E92 of αS1-casein induced an IL-8 secretion of 0.95 ng/mL via TLR4. Our results indicate that αS1-casein appears in two distinct conformations, an α-helical TLR4-agonistic and a less α-helical TLR4 non-agonistic conformation induced by phosphorylation. This is to indicate that the immunomodulatory role of αS1-casein, as described before, could be regulated by conformational changes induced by phosphorylation.

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Section: Hydrophobicity Analysis Of Human αS1-casein and Comparison W...supporting

confidence: 90%

Section: Hydrophobicity Analysis Of Human αS1-casein and Comparison W...supporting

confidence: 90%

Section: Prediction and Probability For Intrinsically Disordered Regi...mentioning

confidence: 99%

Section: Secondary Structure Analysis Of Human αS1-casein By Spectros...mentioning

confidence: 99%

See 2 more Smart Citations

Structural Analysis of Breast-Milk αS1-Casein: An α-Helical Conformation Is Required for TLR4-Stimulation

Saenger,

Schulte,

Vordenbäumen

et al. 2024

IJMS

Self Cite

View full text Add to dashboard Cite

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“…α-S1-casein is best known as a highly phosphorylated protein harboring close to a dozen phosphorylation sites. Among these phosphorylation sites, Ser71, which has recently been reported to be phosphorylated in breast milk, 26 happens to be in the sequon of the N-glycosylation we found (NES) and, thus, on the peptide stretch we monitored. This opens the question of whether a potential positive or negative crosstalk between Nglycosylation and phosphorylation may occur.…”

Section: Identification Of Novel N-glycosylation Sitesmentioning

confidence: 99%

Quantitative Longitudinal Inventory of the N-Glycoproteome of Human Milk from a Single Donor Reveals the Highly Variable Repertoire and Dynamic Site-Specific Changes

et al. 2020

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Protein N-glycosylation on human milk proteins assists in protecting an infant's health and functions among others as competitive inhibitors of pathogen binding and immunomodulators. Due to the individual uniqueness of each mother's milk and the overall complexity and temporal changes of protein N-glycosylation, analysis of the human milk N-glycoproteome requires longitudinal personalized approaches, providing protein-and N-site-specific quantitative information. Here, we describe an automated platform using hydrophilic-interaction chromatography (HILIC)-based cartridges enabling the proteome-wide monitoring of intact Nglycopeptides using just a digest of 150 μg of breast milk protein. We were able to map around 1700 glycopeptides from 110 glycoproteins covering 191 glycosites, of which 43 sites have not been previously reported with experimental evidence. We next quantified 287 of these glycopeptides originating from 50 glycoproteins using a targeted proteomics approach. Although each glycoprotein, N-glycosylation site, and attached glycan revealed distinct dynamic changes, we did observe a few general trends. For instance, fucosylation, especially terminal fucosylation, increased across the lactation period. Building on the improved glycoproteomics approach outlined above, future studies are warranted to reveal the potential impact of the observed glycosylation microheterogeneity on the healthy development of infants.

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Which is the optimal choice for neonates’ formula or breast milk?

Hu,

Wu,

Zhou

et al. 2024

Nat. Prod. Bioprospect.

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The incidence of prematurity has been increasing since the twenty-first century. Premature neonates are extremely vulnerable and require a rich supply of nutrients, including carbohydrates, proteins, docosahexaenoic acid (DHA), arachidonic acid (ARA) and others. Typical breast milk serves as the primary source for infants under six months old to provide these nutrients. However, depending on the individual needs of preterm infants, a more diverse and intricate range of nutrients may be necessary. This paper provides a comprehensive review of the current research progress on the physical and chemical properties, biological activity, function, and structure of breast milk, as well as explores the relationship between the main components of milk globular membrane and infant growth. Additionally, compare the nutritional composition of milk from different mammals and newborn milk powder, providing a comprehensive understanding of the differences in milk composition and detailed reference for meeting daily nutritional needs during lactation. Graphical Abstract

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Ser71 of αS1‐Casein is Phosphorylated in Breast Milk—Evidence from Targeted Mass Analysis

Cited by 5 publications

References 28 publications

Structural Analysis of Breast-Milk αS1-Casein: An α-Helical Conformation Is Required for TLR4-Stimulation

Structural Analysis of Breast-Milk αS1-Casein: An α-Helical Conformation Is Required for TLR4-Stimulation

Quantitative Longitudinal Inventory of the N-Glycoproteome of Human Milk from a Single Donor Reveals the Highly Variable Repertoire and Dynamic Site-Specific Changes

Which is the optimal choice for neonates’ formula or breast milk?

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