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PubMed2005

A comparison of the effects of A1 and A2 beta-casein protein variants on blood cholesterol concentrations in New Zealand adults.

Beta-casein is a cow's milk protein that occurs predominantly in two forms, A1 and A2. Epidemiological evidence suggests that per capita consumption of beta-casein A1 is associated with national mortality rates from ischaemic heart disease. A biological mechanism was proposed after rabbits fed diets containing beta-casein A2 had lower serum cholesterol concentrations and less aortic intimal thickening than rabbits fed beta-casein A1. We tested whether beta-casein A1 and A2 variants differentially affect plasma cholesterol concentrations in humans. In a randomised crossover trial of two four-and-a-half week periods without washout, 62 participants replaced all dairy products in their diet with 500 mL of low-fat milk and 28 g of full-fat cheese that differed in the proportion of beta-casein A1 and A2 variants. Duplicate blood samples were taken on non-consecutive days at the end of each treatment period from 55 people who completed the study. Mean (S.D.) plasma total, low-density and high-density lipoprotein cholesterol concentrations were 5.60 (0.77), 3.73 (0.70) and 1.26 (0.34) mmol/L after the A1 diet and 5.63 (0.81), 3.75 (0.75) and 1.27 (0.37) mmol/L after the A2 diets. We found no evidence that dairy products containing beta-casein A1 or A2 exerted differential effects (P > 0.05) on plasma cholesterol concentrations in humans.

Adult↗
PubMed2006

Stability of casein mRNA is ensured by structural interactions between the 3'-untranslated region and poly(A) tail via the HuR and poly(A)-binding protein complex.

The maintenance of mRNA stability has emerged as a mechanism of post-transcriptional control. We demonstrate that beta-casein mRNA stability is dictated by the poly(A) tail and sequences in the 3'-UTR. An in vitro mRNA decay assay revealed that beta-casein mRNA with a long poly(A) tail had higher stability than that with a short poly(A) tail. The addition of poly(A) homopolymer and 3'-UTR cRNA as competitor induced rapid degradation of beta-casein mRNA. The interaction between full-length beta-casein mRNA and poly(A) homopolymer was inhibited by the addition of the 3'-UTR cRNA in the lysates, which indicates that one region of the 3'-UTR associates with the poly(A) tail through an RNA-protein interaction. The putative AU-rich element (ARE) is present at nt 897-905; deletion and mutation analysis showed that the ARE site was required for maintaining the stability of the beta-casein 3'-UTR. In the immunoprecipitation analysis, the poly(A)-binding protein (PABP) and the RNA-binding protein HuR were pulled down by 3'-UTR cRNA, and the absence of the ARE site reduced the binding of these proteins. These experiments further revealed that the rapid degradation of beta-casein mRNA was induced by incubation with HuR- and PABP-depleted RRLs. Collectively, our results suggest that beta-casein mRNA is protected from degradation by virtue of the structural interaction between the 3'-UTR and poly(A) tail via a protein complex of HuR and PABP.

3' Untranslated Regions↗
PubMed2005

Chaperone-like activity of beta-casein.

The caseins are major components of milk for most mammals and are secreted as large colloidal aggregates termed micelles. They have less ordered secondary and tertiary structures in comparison with typical globular proteins. In this work, beta-casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity, being able to suppress the thermal and chemical aggregation of such substrate proteins as insulin, lysozyme, alcohol dehydrogenase, and catalase by forming stable complexes with the denaturing substrate proteins. Meanwhile, beta-casein was found to not only prevent aggregation of the substrate proteins, but also solubilize the protein aggregates already formed. Data also show that beta-casein exhibits a higher chaperone-like activity than alpha-casein, likely due to the difference in the number of proline residues present and/or in the extent of exposed hydrophobic surfaces. The implications for their in vivo functions of the caseins, based on their exhibiting such in vitro chaperone-like activities, are discussed.

Alcohol Dehydrogenase↗
PubMed2006

Effect of proteins from beef, pork, and turkey meat on plasma and liver lipids of rats compared with casein and soy protein.

OBJECTIVE: We assessed the effect of dietary proteins isolated from beef, pork, and turkey meat on concentrations of cholesterol and triacylglycerols in plasma, lipoproteins, and liver and the composition of the microsomal membrane (fatty acids, phosphatidylcholine/phosphatidylethanolamine ratio) compared with that of casein and soy protein in rats. METHODS: Five groups of 12 rats each were fed semisynthetic diets for 20 d that contained 200 g/kg of proteins isolated from beef, pork, or turkey meat or, as controls, casein or soy protein. RESULTS: Rats fed beef, pork, or turkey proteins did not differ in cholesterol concentrations of plasma, lipoproteins, and liver and in composition of microsomal membrane from rats fed the casein diet. All groups fed a protein from an animal source had higher very low-density lipoprotein (VLDL) and liver cholesterol concentrations than did rats fed soy protein. However, rats fed pork protein had lower concentrations of triacylglycerols in liver, plasma, and VLDL and lower mRNA concentrations of sterol regulatory element binding protein-1 and glucose-6-phosphate dehydrogenase than did rats fed casein. However, concentrations of plasma and VLDL triacylglycerols in rats fed pork protein were not as low as those observed in rats fed soy protein. CONCLUSION: Proteins isolated from beef, pork, or turkey meat do not differ from casein in their effects on cholesterol metabolism. Pork protein decreases plasma triacylglycerol concentrations compared with casein but not compared with soy protein. The triacylglycerol-lowering effect of pork protein compared with casein is suggested to be caused by decreased hepatic fatty acid synthesis.

Animals↗
PubMed1986

Transcriptional and post-transcriptional roles of glucocorticoid in the expression of the rat 25,000 molecular weight casein gene.

In the presence of hydrocortisone, plus insulin and prolactin, rat mammary explants transcribe the 25K casein gene, and the half-life of the transcript is about 20 h. The first detectable effect of the withdrawal of glucocorticoid is reduction of the half-life of the casein mRNA to about 1 h, with full retention of the rate of transcription of the casein gene. A later effect of the withdrawal of glucocorticoid is loss of the ability to transcribe the casein gene. Both aberrations can be rectified by hydrocortisone in vitro. The instability of the 25K casein mRNA in the absence of glucocorticoid appears to be related to degradation in the nucleus. Accumulation of actin mRNA in the nuclear fraction is not dependent on glucocorticoid. The results indicate that glucocorticoid exerts a profound, selective effect on the stabilization of rat 25K casein mRNA, and is essential for the transcription of the casein gene. These effects can be dissociated temporally from one another.

Adrenalectomy↗
PubMed1985

Casein production during differentiation of mammary epithelial cells in collagen gel culture.

Mouse mammary epithelial cells cultivated on floating collagen gels secrete, as judged by immunoblotting, the full array of caseins found in mouse milk. The secreted caseins are all phosphorylated and have estimated minimum molecular weights (MWs) of 45, 40, 27, and 23 kD in SDS-PAGE. Intracellular caseins of epithelia from collagen gel cultivation or from lactating mammary glands are a combination of mature caseins identical with the secreted molecules and novel caseins whose apparent size in SDS-PAGE is different from the secreted molecules. The novel caseins were shown to be non-phosphorylated species apparently insufficiently mature for secretion. Our data indicate that, with regard to casein expression, cultivation of mouse mammary epithelia on collagen gels essentially duplicates their behavior in the lactating mouse mammary glands.

Alkaline Phosphatase↗
PubMed1988

Detection by high-performance liquid chromatography of polyamines formed by clostridial putrefaction of caseins.

Casein incorporated in building materials is degraded by species of alkali-tolerant Clostridia. A whole range of compounds have previously been detected in degraded building materials containing casein as an additive by gas chromatography (GC), including volatile and non-volatile organic acids, alcohols, ketones, aldehydes and monoamines. Using high-performance liquid chromatography (HPLC) it was possible, however, also to detect polyamines formed in degraded caseins. Histamine, agmatine, serotonine, tyramine, tryptamine, putrescine and cadaverine were detected in solutions containing casein in which the alkali-tolerant Clostriadia had been grown. Uninoculated, sterile incubated caseins contained no detectable amounts of polyamines. This gives clear evidence of the role of the biotic environment in the degradation of caseins. A combination of GC and HPLC therefore, provides a convenient set of techniques for studying the degradation products of casein.

Caseins↗
PubMed2000

Evaluation of the effect of rennet type on casein proteolysis in an ovine milk cheese by means of capillary electrophoresis.

Capillary electrophoresis was used to study the evolution of casein throughout the ripening process of Roncal Denomination of Origin ewe's milk cheese and to assess the type of rennet in its hydrolysis. Two manufactures were prepared, each with four vats; two of them had added lamb artisan rennet, batch A [clotting activity of 97.54 rennet units (RU) ml(-1)] and batch B [clotting activity of 16.26 RU ml(-1)]; one vat included calf industrial rennet, batch I (clotting activity of 45.70 RU ml(-1)); and the fourth vat had added mixed rennet, batch M, a 50:50 mixture of lamb (batch A) and calf (batch I) (clotting activity of 77.53 RU ml(-1)). The content of casein nitrogen in fractions alpha-casein1CE, alpha-casein2CE, beta-casein1CE and beta-casein2CE was quantified in cheese after 1, 15, 30, 60, 120 and 180 days of ripening. Beta-casein fractions undergo lesser degradation during the ripening time than alpha-casein proteins. The degradation of alpha-caseins is very much influenced by the clotting activity of the rennet used, so that the more active the clotting activity the greater the hydrolysis of those caseins. Nevertheless, it is at the level of beta-caseins that we observe the evidence of the influence of the type of rennet, thus noting a less intense proteolytic activity in the batch made with calf rennet, batch I.

Animals↗
PubMed1997

Role of the O-phosphoserine clusters in the interaction of the bovine milk alpha s1-, beta-, kappa-caseins and the PP3 component with immobilized iron (III) ions.

alpha s1- and beta-Caseins have a sequence cluster -Ser(P)-Ser(P)-Ser(P)-Glu-Glu- which is not present in kappa-casein and the whey PP3 component. The affinity of these phosphoproteins for the iron(III)-iminodiacetic acid (IDA) complex immobilized on Sepharose was studied as a function of pH, urea concentration, calcium ion concentration, enzymatic dephosphorylation and temperature. The affinity of the three polyphosphorylated proteins (alpha s1- and beta-caseins, PP3) was similar. The sequence cluster was not a specific recognition pattern of the iron(III) ion. These three proteins presented a site of high affinity and a site of weak affinity. kappa-Casein, which had only one Ser(P) residue, presented only the site of weak affinity. Their primary site which was absent after dephosphorylation or calcium ion addition required the presence of at least two Ser(P) residues close in space. Their secondary site was sensitive to the presence of urea. It was sensitive to pH variation for PP3 and kappa-casein. The study of the affinity of a few free amino acids towards iron(III)-IDA showed that the secondary site involved tryptophan and tyrosine residues for alpha s1- and beta-caseins, histidine residues for PP3 and cysteine residues for kappa-casein.

Adsorption↗
PubMed1999

Conformational analysis of the hydrophobic peptide alphas1-casein(136-196).

Hydrophobic interactions are important in the self-association of milk proteins, including alphas1-casein. The extent to which casein interaction sites are influenced by local secondary structure is not widely known. Both primary amino acid sequence and local secondary structure are shown to affect the self-association of the hydrophobic peptide alphas1-casein(136-196). The peptide is aggregated at low concentrations (7 microM and above), as determined by 1H nuclear magnetic resonance (NMR) measurements at pH 6.0 in phosphate buffer. Increase in temperature is shown to induce side chain mobility (melting) as indicated by both 1H NMR and near-UV circular dichroism (CD) measurements. As determined by far-UV CD, there is also a loss in the global amount of extended structure with increasing temperature, while beta-turn structures and some aromatic dichroism are conserved at temperatures as high as 70 degrees C. Similar retention of structure occurs at pH 2 and in 6 M guanidine HCl. The observed stability of beta-turns and some side chains in alphas1-casein(136-196) supports previous assumptions that hydrophobic, proline-based turns are important interaction sites in the self-association of alphas1-casein, and possibly in the formation of the calcium transport complexes, the casein micelles. It may be speculated that these areas of the peptide represent a 'molten globule-like', heat stable, core structure for alphas1-casein.

Amino Acid Sequence↗
PubMed1981

Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases.

The fifty of so phosphorylated hydroxyamino acid residues hitherto investigated in caseins from different species have been found to occur in tripeptide sequences -Ser/Thr-X-A- where X represents any amino acid residue and A is an acidic residue. This strongly suggests that phosphorylation of caseins involves basically the stepwise enzymatic recognition of primary and secondary anionic amino acid triplets where the determinants are dicarboxylic residues and phosphoseryl residues, respectively. Studies of genetic variants of bovine caseins have provided clear-cut evidence for the actual occurrence of the former recognition sites. The occurrence of the above tripeptide sequences is a necessary but not a sufficient condition for phosphorylation of caseins to occur. Possible factors of constraint such as different intrinsic properties of both phosphate acceptor residues and acidic determinants, the characteristics of the local environment in terms of overall charge and hydrophilicity, secondary structure and steric hindrance, an insufficient available pool of casein kinase(s)... are discussed. All evidence now available supports the concept that phosphorylation of caseins is a posttranslational event and it is suggested that the process may occur during the transfer of completed polypeptide chains from the smooth endoplasmic reticulum to the Golgi apparatus where most of phosphate incorporation is presumably carried out. This organelle is rich in membrane-bound specific cyclic AMP-independent kinase(s) able in vitro to rephosphorylate specifically although not completely phosphatase-treated caseins and caseinophosphopeptides.

Amino Acid Sequence↗
PubMed2003

The effects of casein on diclofenac release from hydroxypropylmethylcellulose (HPMC) compacts.

The inclusion of casein, either as the acid or sodium salt form, was found to significantly modify the release of the acidic drug diclofenac from hydroxypropylmethycellulose (HPMC, Methocel grades K100LV and K15M)-based matrices. The presence of casein in diclofenac-K100LV matrices increased the drug release rate and rendered the release profile more linear. Furthermore, sodium caseinate appeared to retard the disintegrating tendency of the higher molecular weight HPMC-drug systems, apparently by enhancing the initial gel forming ability of these systems. Surprisingly, dissolution profiles of the salt and acid forms of the drug were similar when co-compressed with sodium caseinate, and addition of HPMC retarded release of both forms of drug to the same extent. Swelling and erosion experiments indicated that the presence of casein decreased the extent of medium uptake (swelling) of the matrices and accelerated the rate of erosion, while not altering the dissolution medium infiltration rate. Phase solubility analysis indicated that the solubility of the drug was also enhanced by sodium caseinate, consistent with complex formation between the drug and casein.

Caseins↗
PubMed2000

Dietary protein level and origin (casein and highly purified soybean protein) affect hepatic storage, plasma lipid transport, and antioxidative defense status in the rat.

The effects of different proportions (10, 20, and 30%) of dietary casein or highly purified soybean protein on lipid metabolism were studied in growing Wistar rats. Hepatic, plasma and lipoprotein lipid, and protein concentrations, plasma thiobarbituric acid-reactive substance (TBARS) levels, and resistance of red blood cells against free-radical attack were determined after a 4-wk dietary regimen. Compared with the 20% casein diet, the 20% soybean protein diet exhibited similar cholesterolemia but lower plasma triacylglycerol concentrations and very-low-density lipoprotein (VLDL) particle number, as measured by diminished contents of VLDL-triacylglycerol, VLDL-protein, and VLDL-apolipoprotein (Apo) B (B-100 and B-48). The soybean protein diet raised high-density lipoprotein (HDL)(2-3) particle number, as measured by enhanced concentrations of HDL(2-3) cholesterol, HDL-phospholipid, and HDL-ApoA-I. Increasing casein or soybean protein level (from 10 to 30%) in the diet involved higher VLDL-ApoB (B-100 and B-48), indicating an increase in the number of VLDL particles. Feeding the 30% casein or 30% soybean protein diet enhanced LDL-HDL(1) cholesterol contents. Despite similar HDL(2-3)-ApoA-I levels, the 30% casein diet enhanced the HDL(2-3) mass and its cholesterol concentrations. In contrast, feeding either the 10 or 30% soybean protein diet significantly lowered HDL(2-3) cholesterol and ApoA-I levels. These effects on cholesterol distribution in lipoprotein fractions occurred despite unchanged total cholesterol concentrations in plasma. Feeding 20% soybean protein versus 20% casein involved lower plasma TBARS concentrations. Decreasing casein or soybean protein levels in the diet were associated with higher plasma TBARS concentrations and had a lower resistance of red blood cells against free-radical attack. The present study shows that dietary protein level and origin play an important role in lipoprotein metabolism and the antioxidative defense status but do not affect total cholesterol concentrations in plasma.

Animals↗
PubMed2000

Bioavailability of zinc and its binding to casein in milks and formulas.

Differences in zinc bioavailability among milk and formulas may be attributed to binding of zinc to various ligands. We determined the distribution of zinc and protein at different pHs and zinc and calcium concentrations. We used radiolabelled cow's milk, human milk, whey-predominant (WPF) and casein-predominant (CPF) infant formula. Lowering the pH changed zinc and protein distribution: zinc shifted from pellet (casein) to whey in cow's milk, from fat to whey in human milk and from fat and pellet to whey in formulas. Protein shifted from whey to pellet in human milk and from whey and pellet to fat in formulas. Increasing zinc and calcium concentrations shifted protein and zinc from pellet to whey for cow's milk and from whey and pellet to fat for the formulas. Protein distribution was not affected by calcium or zinc addition in human milk or CPF, while zinc shifted from whey to fat in human milk and from fat and pellet to whey in CPF. Zinc and calcium binding to isolated bovine or human casein increased with pH. At 500 mg/L of zinc, bovine casein bound 32.0 +/- 1.8 and human casein 10.0 +/- 0.9 mg zinc/g protein. At 500 mg/L of calcium, calcium was preferentially bound over zinc. Adding calcium and zinc resulted in 32.0 +/- 1.8 mg zinc/g bound to bovine casein and 17.0 +/- 0.8 mg zinc/g to human casein, while calcium binding was low. Suckling rat pups dosed with 65Zn labelled infant diets were killed and individual tissues were gamma counted. Lower zinc bioavailability was found for bovine milk at pH = 4.0 (%65Zn in liver = 18.7+1.4) when compared to WPF (22.8 +/- 1.6) or human milk (26.9 +/- 0.8). Lowering the pH further decreased zinc bioavailability from human milk, but not from cow's milk or WPF. Knowledge of the compounds binding minerals and trace elements in infant formulas is essential for optimizing zinc bioavailability.

Animals↗
PubMed2000

Mineral and casein equilibria in milk: effects of added salts and calcium-chelating agents.

We have investigated the effects of adding a range of mineral salts and calcium-chelating agents on the distribution of casein and minerals between the non-pelleted and pelleted phases of milk obtained upon centrifugation at 78000 g for 90 min. Adding CaCl2 or mixtures of NaH2PO4 and Na2HPO4 to reconstituted skim milk (90 g milk solids/kg) at pH 6.65 increased both pelleted casein and pelleted calcium phosphate. Opposite effects were obtained by adding citrate or EDTA. The change in pelleted calcium phosphate was not simply related to casein release from the micelle. Upon adding 5 mmol EDTA/kg milk, 20% of the pelleted Ca, 22% of the pelleted phosphate and 5% of the micellar casein were removed. Increasing the concentration of EDTA to 10 mmol/kg milk decreased the pelleted Ca by 44% and the pelleted phosphate by 46%, and caused 30% of the micellar casein to be released. The effects of adding phosphate, citrate or EDTA at pH 6.65, followed by the addition of CaCl2, demonstrated the reversibility of the dissolution and formation of the micellar calcium phosphate. There were limits to this reversibility that were related to the amount of colloidal calcium phosphate removed from the casein micelles. Adding CaCl2 to milk containing > or = 20 mmol EDTA or > or = 30 mmol citrate/kg milk did not result in complete reformation of casein micelles. Light-scattering experiments confirmed that the dissolution of moderate amounts of colloidal calcium phosphate had little effect on micellar size and were reversible, while the dissolution of larger amounts of colloidal calcium phosphate resulted in large reductions in micellar size and was irreversible.

Animals↗
PubMed1978

Preparation and fractionation of goat kappa-casein: analysis of the glycan and peptide components.

Whole goat kappa-casein was prepared by chromatography of whole casein on hydroxyapatite. Chromatography of whole kappa-casein on DEAE-cellulose separated 5 fractions. All of them were sensitive to chymosin. Their amino acid and carbohydrate composition, phosphate content and molecular weight were determined. Galactose, N-acetylgalactosamine, N-acetyl and N-glycolyl neuraminic acids were identified in whole kappa-casein. It appears that goat kappa-casein, like cow, buffalo and ewe kappa-caseins, is composed of several fractions having identical peptide chains and differing in their carbohydrate contents. The main fraction, devoid of carbohydrate, was treated with chymosin. The para-kappa-casein and caseinomacropeptide were isolated. Their amino acid composition and phosphate content were determined.

Animals↗
PubMed1980

Heat-induced association of beta-lactoglobulin and casein micelles.

Heat-induced association of beta-lactoglobulin (beta-lg) and casein micelles, mainly at 85--90 degrees C, was studied by means of preparative ultracentrifugation, using [3H]-labelled beta-lg. Qualitative aspects were studied by gel electrophoresis and electron microscopy. In this association, the formation of intermolecular S-S bonds between beta-lg and kappa-casein plays a role, but hydrophobic bonds are also involved. After heating mixtures containing 25 g/kg casein and 4 g/kg beta-lg at 90 degrees C for 20 min, the amount of beta-lg sedimented with the casein micelles by ultracentrifugation decreased by approximately 30% when the milk salt buffer system was reduced to 0.25 of its normal concentration; it decreased by about 20% when the pH was increased from 6.8 to 7.3 and increased by 15% when the pH was reduced from 6.8 to 5.8. When the beta-lg concentration was decreased from 4 to 2 g/kg, the amount of sedimented beta-lg decreased by 25% after heating at 90 degrees C for 6 min. After heating in milk salt buffer, the amount of sedimented beta-lg was 15% higher than after heating in salt solution which contained neither Ca nor citrate ions. Although alpha-lactalbumin (alpha-la) is involved in the heat-association of beta-lg and casein micelles, no influence of alpha-la on the amount of associated beta-lg was found. In addition to the heat-association product of beta-lg and whole casein micelles, an association product consisting mainly of beta-lg and kappa-casein was also formed. This product was observed by electron microscopy as noodle-like particles. The size of these particles depended on the beta-lg/kappa-casein ratio.

Animals↗
PubMed1981

Binding of calcium ions to bovine beta-casein.

The isotherms for Ca++ binding to bovine alpha-casein have been measured at 5 temperatures in the range 4-40 degrees C and at 4 different ionic strengths. The results are interpreted by an interactive-site binding model, and are compared with results previously obtained on alpha s1-casein. The affinity of beta-casein for the first Va2+ to bind is similar to the affinity of alpha s1-casein for the same binding event: however, binding of subsequent Ca2+ to beta-casein is weaker than the binding to alpha s1-casein. The results are discussed in terms of precipitability of the 2 caseins caused by the binding of Ca2+.

Animals↗