A study of the enzymic dephosphorylation of β-casein and a derived phosphopeptide

West, David W.; Towers, Greta E.

doi:10.1016/0005-2795(76)90133-1

Cited by 11 publications

(5 citation statements)

References 14 publications

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“…West and Towers [12] reported that food-derived phosphopeptides were absorbed, at least in part, without dephosphorylation. Immunoblot analysis showed that soy glycinin contained more phosphorylated tyrosine than egg white (Figure 2).…”

Section: Resultsmentioning

confidence: 99%

“…In the present study, phosphorylated Cblin-like peptide, DIpYNP, effectively inhibited Cbl-b-mediated ubiquitination and degradation of IRS-1, although we could not determine the IC 50 value of dephosphorylated Cblin-like peptide. However, casein phosphopeptide (CPP) is a phosphorylated protein and resists dephosphorylation during digestion [12]. Furthermore, we noted that glycinin was remarkably phosphorylated, compared with egg white and bovine serum albumin proteins.…”

Section: Discussionmentioning

confidence: 99%

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Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Abe

Kohno

Yama

et al. 2013

International Journal of Endocrinology

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Background. Unloading stress induces skeletal muscle atrophy. We have reported that Cbl-b ubiquitin ligase is a master regulator of unloading-associated muscle atrophy. The present study was designed to elucidate whether dietary soy glycinin protein prevents denervation-mediated muscle atrophy, based on the presence of inhibitory peptides against Cbl-b ubiquitin ligase in soy glycinin protein. Methods. Mice were fed either 20% casein diet, 20% soy protein isolate diet, 10% glycinin diet containing 10% casein, or 20% glycinin diet. One week later, the right sciatic nerve was cut. The wet weight, cross sectional area (CSA), IGF-1 signaling, and atrogene expression in hindlimb muscles were examined at 1, 3, 3.5, or 4 days after denervation. Results. 20% soy glycinin diet significantly prevented denervation-induced decreases in muscle wet weight and myofiber CSA. Furthermore, dietary soy protein inhibited denervation-induced ubiquitination and degradation of IRS-1 in tibialis anterior muscle. Dietary soy glycinin partially suppressed the denervation-mediated expression of atrogenes, such as MAFbx/atrogin-1 and MuRF-1, through the protection of IGF-1 signaling estimated by phosphorylation of Akt-1. Conclusions. Soy glycinin contains a functional inhibitory sequence against muscle-atrophy-associated ubiquitin ligase Cbl-b. Dietary soy glycinin protein significantly prevented muscle atrophy after denervation in mice.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Abe

Kohno

Yama

et al. 2013

International Journal of Endocrinology

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“…Despite their different length and amino acid composition, CPP share a common ‘acidic motif’, consisting of three phosphoserines and two glutamic acids, Ser(P)‐Ser(P)‐Ser(P)‐Glu‐Glu, a sequence fully conserved among the species, and representing the binding site for di‐ and trivalent minerals, including calcium [10–13].…”

Section: Introductionmentioning

confidence: 99%

Casein‐derived bioactive phosphopeptides: role of phosphorylation and primary structure in promoting calcium uptake by HT‐29 tumor cells

et al. 2003

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Casein phosphopeptides L L-CN(1^25)4P and K K s1 -CN(59^79)5P, from L L-and K K s1 -casein, respectively, both carrying the characteristic 'acidic motif' Ser(P)-Ser(P)-Ser(P)-GluGlu, were chemically synthesized and administered to HT-29 cells di¡erentiated in culture, which are a used model of intestinal epithelium for absorption studies. Both casein phosphopeptides caused an increase of [Ca 2+ ] i due to in£ux of extracellular Ca 2+ . The response was quantitatively higher with L L-CN(12 5)4P than K K s1 -CN(59^79)5P. The synthetic peptide corresponding to the 'acidic motif' was ine¡ective and the dephosphorylated form of L L-CN(1^25)4P almost inactive. The lack of the N-terminally located ¢ve amino acids, or sequence modi¢-cations within the N-terminal segment of L L-CN(1^25)4P, caused a total loss of activity, whereas the lack of the C-terminal segment preserved activity. In conclusion, the in£ux of calcium into HT-29 cells caused by L L-CN(1^25)4P appears to depend on the phosphorylated 'acidic motif' and the preceding N-terminal region.

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“…wt of 80, so that it is easy to distinguish the loss of a phosphoserine residue in comparison with a loss of serine. Using phosphopeptides isolated from both a Sl - (West, 1977) and /?-casein (West & Towers, 1976), we have been able to confirm positively the original assignments for phosphoserine residues in these proteins. Furthermore, we have successfully applied the mass-spectrographic technique to defining the structures of partly dephosphorylated derivatives of the N-terminal /?-casein phosphopeptide.…”

Section: (D (?) (D® ®mentioning

confidence: 52%

“…Furthermore, we have successfully applied the mass-spectrographic technique to defining the structures of partly dephosphorylated derivatives of the N-terminal /?-casein phosphopeptide. Dephosphorylation of the phosphopeptide was carried out using both acid and alkaline phosphatases, and the resultant product mix was separated into peptides containing 0, 1, 2, 3 and 4 phosphoserine residues (West & Towers, 1976). Mass-spectrographic analysis applied to these products indicated the positions at which phosphates had been removed and demonstrated that the two enzymes used, bovine spleen acid phosphatase and Escherichia coli alkaline phosphatase, had attacked the phosphoseryl residues in a different sequence.…”

Section: (D (?) (D® ®mentioning

confidence: 99%

Structure and function of the phosphorylated residues of casein

West

1986

Journal of Dairy Research

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Introduction Phosphorylation of the caseins Determination of the position of phosphorylated residues Structure of the kinase recognition sites Limits to the extent of phosphorylation Properties of the casein kinase Importance of the casein phosphoseryl residues to the structure, function and properties of milk CONTENTS PAGE 333 335 335 338 340 342 343 Formation of micelles and binding of calcium Technological importance of casein phosphorylation Biological significance of casein phosphorylation Conclusion References

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A study of the enzymic dephosphorylation of β-casein and a derived phosphopeptide

Cited by 11 publications

References 14 publications

Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Soy Glycinin Contains a Functional Inhibitory Sequence against Muscle-Atrophy-Associated Ubiquitin Ligase Cbl-b

Casein‐derived bioactive phosphopeptides: role of phosphorylation and primary structure in promoting calcium uptake by HT‐29 tumor cells

Structure and function of the phosphorylated residues of casein

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