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PubMed1975

Regulation of casein messenger RNA during the development of the rat mammary gland.

Casein mRNA was isolated and partially purified from RNA extracts of rat lactating mammary glands and translated in a teterologous cell-free protein synthesizing system derived from wheat germ. Casein mRNA activity was assayed by immunoprecipitation using a specific antiserum prepared against a mixture of the purified rat caseins. Properties of rat casein mRNA were examined using a variety of sizing techniques, including chromatography on Sepharose 4B, sedimentation on sucrose gradients after heat denaturation, and electrophoresis on 2.5% agarose gels in 6 M urea. Casein mRNA activity was found in an 8-16S region after gradient centrifugation with the peak occurring at 10.5 S. In addition, the binding of rat casein mRNA to dT-cellulose was examined. Only 40% of the total casein mRNA activity was selectively retained. A partial purification of casein mRNA was accomplished by a combination of these sizing and affinity chromatography techniques. In the purified preparations casein mRNA activity comprises approximately 90% of the total mRNA activity. Characterization of this material by agarose gel electrophoresis revealed two main bands of RNA at approximately 12 and 16 S, both containing casein mRNA activity. These mRNAs were of the correct size to code for two of the principal rat caseins of approximately 25,000 and 42,000 molecular weights. Casein mRNA and total mRNA activities were then compared in total RNA extracts at various stages of normal mammary gland development in the rat, i.e. during pregnancy, lactation, and involution following weaning. A selective induction of casein mRNA activity compared to total mRNA activity was found to occur during pregnancy and lactation. Moreover, a selective loss of activity was also observed during mammary gland involution. A surprisingly high level of casein mRNA activity was found in RNA extracts from early and midpregnant mammary glands.

Animals↗
PubMed1994

Milk composition and lactation of beta-casein-deficient mice.

beta-Casein is a major protein component of milk and, in conjunction with the other caseins, it is assembled into micelles. The casein micelles determine many of the physical characteristics of milk, which are important for stability during storage and for milk-processing properties. There is evidence that suggests that beta-casein may also possess other, nonnutritional functions. To address the function of beta-casein, the mouse beta-casein gene was disrupted by gene targeting in embryonic stem cells. Homozygous beta-casein mutant mice are viable and fertile; females can lactate and successfully rear young. beta-Casein was expressed at a reduced level in heterozygotes and was completely absent from the milk of homozygous mutant mice. Despite the deficiency of beta-casein, casein micelles were assembled in heterozygous and homozygous mutants, albeit with reduced diameters. The absence of beta-casein expression was reflected in a reduced total protein concentration in milk, although this was partially compensated for by an increased concentration of other proteins. The growth of pups feeding on the milk of homozygous mutants was reduced relative to those feeding on the milk of wild-type mice. Various genetic manipulations of caseins have been proposed for the qualitative improvement of cow's milk composition. The results presented here demonstrate that beta-casein has no essential function and that the casein micelle is remarkably tolerant of changes in composition.

Animals↗
PubMed1976

Nitrogen metabolism in calves. Effect of giving different amounts of dietary casein with and without formaldehyde treatment.

I. Calves were given a basal diet of straw and flaked maize (12 g nitrogen/kg dry matter (DM)) or diets with some flaked maize replaced by untreated (UT) casein or formaldehyde-treated (FT) casein to give 19, 29 or 34 g N/kg DM. 2. At all intakes rumen ammonia concentrations were lower and amounts of total-N, non-ammonia-N and amino acid-N entering the duodenum were high when FT-rather the UT-casein supplements were given. 3. Direct measurement of casein entering the duodenum indicated that giving FT rather than UT casein led to much greater amounts of dietary casein escaping degradation in the rumen (70--90% compared to 10--20%). Calculated values for fermentable N indicated that with this low degradability diets containing FT-casein would have provided inadequate N for maximum microbial synthesis in the rumen, and this probably accounted for the marked reduction in amounts of non-casein-N entering the duodenum when FT rather than UT casein was given. 4. Amino acid patterns in duodenal digesta samples after giving the basal diet or diets containing UT-casein were similar. Giving diets containing FT-casein led to changes in this pattern which could sometimes, although not always, be accounted for by estimated differences in proportions of dietary and microbial proteins. 5. At the highest level of N intake FT-casein-supplemented diets led to significantly higher concentrations of most essential amino acids and lower concentrations of most non-essential amino acids in plasma than did UT-casein-supplemented diets. Plasma urea concentrations increased with increasing N intake but were not significantly different for UT- and FT-casein-supplemented diets.

Amino Acids↗
PubMed1989

Comparison of the hypocholesterolemic effects of dietary soybean protein with those of formaldehyde-treated casein in rabbits.

Treatment of casein with formaldehyde changes its tertiary structure and decreases its hypercholesterolemic properties in rabbits. To investigate whether formaldehyde-treated casein exerts this hypocholesterolemic effect in the same manner as soybean protein, rabbits were fed high or low cholesterol diets containing soybean protein, casein, formaldehyde-treated casein or a mixture of casein and formaldehyde-treated casein. Formaldehyde-treated casein was hypocholesterolemic when fed in a low, but not in a high, cholesterol diet. The hypocholesterolemic effect of soybean protein was independent of the amount of cholesterol included in the diet. In contrast to rabbits fed soybean protein, steroid absorption in those fed formaldehyde-treated casein did not differ from that in rabbits fed native casein. Furthermore, the absorption of phosphorus and nitrogen was lower in rabbits fed formaldehyde-treated casein than in those fed native casein, whereas the absorption found in rabbits fed soybean protein resembled that of their casein-fed counterparts. The diets containing soybean protein and formaldehyde-treated casein produced a comparable ratio of lysine to arginine in serum. The results presented in this paper indicate that the hypocholesterolemic action of dietary formaldehyde-treated casein does not resemble that of soybean protein.

Amino Acids↗
PubMed1992

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

A Dictyostelium discoideum cDNA encoding an alpha-type subunit of casein kinase II was isolated, and its cDNA was used to study developmental expression of casein kinase II during the Dictyostelium life cycle. The 1.3-kb cDNA insert contained an open reading frame of 337 amino acids (M(r) 39,900). The deduced amino acid sequence has high homology with those of casein kinase II alpha subunits from other species. Genomic Southern blot analysis suggested that there is a single gene encoding casein kinase II alpha subunit in D. discoideum. Northern (RNA) blot analysis showed that the casein kinase II alpha-subunit gene is expressed constitutively as a 1.9-kb mRNA throughout vegetative growth and multicellular development. Casein kinase purified from normal vegetative cells contained a major protein band of approximately 36 kDa, which was recognized by antisera raised against rat testis casein kinase II. Comparison of the in vitro transcription/translation product of the alpha-subunit cDNA clone and the purified 36-kDa protein by partial proteolysis indicated that the isolated cDNA clone encodes the Dictyostelium casein kinase II alpha subunit. No protein corresponding to a beta subunit was detected in purified casein kinase. Immunoblot analysis using anti-rat casein kinase II sera showed that the alpha subunit of casein kinase II is expressed constitutively like its mRNA during the life cycle of D. discoideum. Casein kinase II activity measured by using a specific peptide substrate paralleled the level of alpha subunit detected by immunoblotting during the life cycle, with a maximum variation of approximately 2-fold. We were unable to obtain disruptants of the casein kinase II alpha gene, suggesting that there is a single casein kinase II alpha gene, which is essential for vegetative growth of D. discoideum.

Amino Acid Sequence↗
PubMed1984

Expression of kappa-casein in normal and neoplastic rat mammary gland is under the control of prolactin.

An 820-nucleotide-long cDNA clone for the kappa-casein (the casein micelle-stabilizing protein) from rat mammary gland was isolated, and its nucleotide sequence was determined. The deduced amino acid sequence from the nucleotide sequence revealed a signal peptide, 21 amino acids long, and a mature protein of 157 amino acids. The signal peptide of rat kappa-casein was highly homologous to that of the precursor to ovine kappa-casein. However, little homology was apparent when the mature kappa-casein protein sequences from ovine or bovine sources were compared with rat kappa-casein. The kappa-casein mRNA content of the mammary tissue was found to increase during its functional differentiation. Prolactin appears to modulate the production of kappa-casein mRNA. Mammary glands of virgin females had no detectable kappa-casein mRNA; however, a marked induction of kappa-casein mRNA was obtained by intravenous infusion of prolactin. Mammary carcinomas did not follow the same pattern. 7,12-Dimethylbenz[a]anthracene-induced mammary carcinomas had normally low levels of kappa-casein mRNA, but intravenous prolactin infusion increased the levels by 2-fold. The MTW9 mammary carcinoma that grows only in the presence of high levels of mammotropic hormones had kappa-casein mRNA content equivalent to that in 10-day lactating rat mammary gland. Continuous venous infusion of prolactin to MTW9 mammary carcinoma did not modify the kappa-casein mRNA levels. Nitrosomethylurea-induced mammary carcinomas had no detectable kappa-casein mRNA, and intravenous prolactin infusion was unable to induce it.

Amino Acid Sequence↗
PubMed1993

Molecular cloning, expression, and characterization of a 49-kilodalton casein kinase I isoform from rat testis.

We report the molecular cloning and characterization of a 49-kDa form of casein kinase I from rat testis. A cDNA clone encoding the enzyme, designated casein kinase I delta, contained an open reading frame of 1284 nucleotides that predicts a polypeptide of 428 amino acids with a M(r) of 49,121. The predicted amino acid sequence shares 76% identity with casein kinase I alpha, a 37-kDa form recently cloned from bovine brain (Rowles, J., Slaughter, C., Moomaw, C., Hsu, J., and Cobb, M. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 9548-9552), and 65% identity with HRR25, a 57-kDa form of casein kinase I from yeast shown to be involved in DNA repair (Hoekstra, M. F., Liskay, R. M., Ou, A. C., DeMaggio, A. J., Burbee, D. G., and Heffron, F. (1991) Science 253, 1031-1034). Northern analysis of rat or rabbit RNA revealed three hybridizing species of 3.5-4.1, 2.2, and 1.9 kilobase pairs (kb). The largest message was detected in all tissues examined, whereas the 1.9- and 2.2-kb species were found predominantly in testis. A probe corresponding to the 3'-untranslated region of the casein kinase I delta cDNA hybridized only to the 1.9-kb transcript. Expression of the casein kinase I delta cDNA in Escherichia coli resulted in active enzyme that phosphorylated casein, phosvitin, and the peptide substrate DDDDVASLPGLRRR. Enzyme activity was associated with a predominant polypeptide of 55-kDa, although COOH-terminal degradation products of 50 and 42 kDa were also present in partially purified enzyme. Recombinant casein kinase I delta was inhibited by the specific casein kinase I inhibitor, CKI-7, half-maximally at 12 microM. Heparin inhibited recombinant casein kinase I delta when phosvitin was the substrate, with half-maximal inhibition at 11.5 micrograms/ml. However, if the peptide substrate was used, heparin activated recombinant casein kinase I delta 4-5-fold, with half-maximal activation at 9.5 micrograms/ml. A truncated form of casein kinase I delta, lacking the COOH-terminal 111 amino acids, was no longer activated by heparin. Casein kinase I delta therefore represents a separate member of the casein kinase I family distinguished by its larger size and unique kinetic behavior with respect to heparin.

Amino Acid Sequence↗
PubMed1996

Detection of a kappa-casein-specific lymphocyte response in milk-responsive atopic dermatitis.

BACKGROUND: Bovine casein leads to an expansion of lymphocytes expressing the cutaneous lymphocyte antigen and to specific lymphocyte proliferation in a subgroup of patients with milk-responsive atopic dermatitis (AD). The casein fraction is composed of different proteins with defined and completely different sequences. OBJECTIVE: To define the stimulatory capacity of the major casein protein (alpha, beta and kappa) in lymphocyte proliferation assays with cells from milk-allergic and non-allergic individuals. METHODS: Proliferative responses of peripheral blood mononuclear cells to lipopolysaccharide-depleted casein subfractions were measured by thymidine incorporation. Lymphocytes from milk-responsive patients with AD were compared with cells from non-responsive patients with AD and to non-atopic individuals. Atopic individuals with immediate symptoms following consumption of cow's milk were included as positive controls. Casein-specific T-cell clones (TCC) from four patients with milk-responsive AD were restimulated with unfractionated casein and kappa-casein. RESULTS: Higher proliferative responses to unfractionated casein and alpha-, beta- and kappa-casein were observed in milk-responsive patients compared with non-responders. Unfractionated casein and kappa-casein discriminated best between the milk-responsive patients with AD and non-responders. Twenty-five of 31 TCG from patients with milk-responsive AD reacted to the mixed casein preparation and kappa-casein. CONCLUSION: A pronounced kappa-casein-specific T-cell-mediated immune response is found in the blood of many patients with a history of milk-related exacerbation of AD.

Adolescent↗
PubMed1999

Endogenous casein kinase I catalyzes the phosphorylation of the lens fiber cell connexin49.

The lens fiber cell-specific gap junction protein connexin49 is a substrate for a membrane-associated Ser/Thr protein kinase that can be extracted from lens cell membranes by 0.6 M KCl. However, the identity of this protein kinase has not been defined. In this report, evidence is presented indicating that it is casein kinase I. Thus, connexin49 was shown to be a substrate for purified casein kinase I but not for casein kinase II; the endogenous connexin49 protein kinase activity extracted from lens membranes with KCl was inhibited by the casein kinase I-specific inhibitor, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CKI-7); the connexin49 protein kinase activity in the lens membrane KCl extract, which could be partially purified by gel filtration and affinity purification with a casein-Sepharose 4B column, copurified with casein kinase activity; phosphopeptide analysis showed that casein kinase I and the connexin49 protein kinase activity in the lens membrane KCl extract probably share the same phosphorylation sites in connexin49. Reverse transcription-PCR using total ovine lens RNA and casein kinase I isoform-specific oligonucleotide primers resulted in the amplification of cDNAs encoding casein kinase I-alpha and -gamma, while an in-gel casein kinase assay indicated casein kinase activity in the lens membrane KCl extract was associated with a major 39.2-kDa species, which is consistent with the 36 to 40-kDa size of casein kinase I-alpha in other animal species. These results demonstrate that the protein kinase activity present in the lens membrane 0.6 M KCl extract that catalyzes the phosphorylation of connexin49 is casein kinase I, probably the alpha isoform.

Animals↗
PubMed1983

Demonstration of specific receptors for fluoresceinated casein on human neutrophils and monocytes using flow cytometry.

Casein is chemotactic for human neutrophils (PMNs) and monocytes. The binding of fluorescein (FITC)-conjugated casein (mixture of alpha, beta, and kappa-casein) and purified alpha-casein to PMNs, monocytes, and lymphocytes was analyzed using flow cytometry. These studies demonstrate that 75-95% of PMNs and 46-85% of monocytes have membrane receptors for casein while lymphocytes lack these receptors. The binding of FITC-casein and FITC-alpha-casein was specific and was blocked only by unlabeled casein and alpha-casein, but not by ovalbumin, bovine or human serum albumin, beta-casomorphin, C5a, or formyl-methionyl-leucylphenylalanine (fMLP). The binding of FITC-casein was reversible when PMNs were stained with this fluorescent agent and subsequently incubated with unlabeled casein. Double-labeling studies of mononuclear cells using FITC-casein and the OKM1 monoclonal antibody in conjunction with a rhodamine conjugated anti-Ig second antibody demonstrate that mononuclear cells binding FITC-casein also stain with the OKM1 monoclonal antibody, indicating a specificity for monocytes.

Binding, Competitive↗
PubMed1997

Structure and expression of the mouse casein gene locus.

The analysis of yeast artificial chromosomes (YACs) containing the complete mouse casein gene locus revealed the presence of five casein genes, alpha-, beta-, gamma-, delta-, and kappa-casein, in this order, in the locus. The alpha- and beta-casein genes are only 10 kb apart and have convergent transcriptional orientations. The distance between the beta-casein gene and the alpha s2-like gamma-casein gene is about 70 kb, and these genes have divergent transcriptional orientations. The gamma- and delta-casein genes, both encoding a alpha s2-like casein, are linked within 60 kb and convergently transcribed. The kappa-casein gene is located about 100 kb from the delta-gene. Except for the presence of the delta-casein gene, the organization of the mouse casein locus resembles that of the bovine locus, including the transcriptional orientation of the genes. In contrast to the other casein genes, which are strongly induced at mid-lactation, expression of the delta-casein gene is abruptly induced upon parturition. Comparative analysis of alpha s2-like sequences from various species suggests that the ancestral alpha s2-like gene duplicated around the time of radiation of the rodent and artiodactylid ancestors.

Amino Acid Sequence↗
PubMed1984

Anomalous behavior of bovine alpha s1- and beta-caseins on gel electrophoresis in sodium dodecyl sulfate buffers.

Electrophoresis in the presence of sodium dodecyl sulfate (SDS) provides a relatively simple means of determining molecular weights of proteins. This technique relies on the validity of a correlation between some function of Mr and the mobility of the protein through the gel matrix. However, bovine caseins (especially alpha s1-casein) have lower mobilities than expected on the basis of their known Mr. The binding of SDS to both alpha s1-casein (Mr 23,600) and beta-casein (Mr 24,000) reached a maximum at the slightly low value of 1.3 g SDS/g protein. Gel-filtration chromatography showed, however, that the alpha s1-casein:SDS complex was larger than the beta-casein:SDS complex at pH 6.8 or 7.0, but that they were similar in size at pH 2.9 or 3.0. Circular dichroism spectra indicated that the low helical structure content of both alpha s1- and beta-casein increased with the addition of SDS and/or decreasing the pH to 1.5. 13C NMR results showed that SDS bound to alpha s1- and beta-casein in the same way as it did to bovine serum albumin. Either esterification or dephosphorylation followed by amidation of alpha s1-casein increased its mobility in SDS-gel electrophoresis, but neither modification affected beta-casein mobility. These and other results indicate that the low electrophoretic velocity of alpha s1-casein in SDS-gel electrophoresis results from its unexpectedly large hydrodynamic size. This is caused by localized high negative charges on certain segments of alpha s1-casein, which would induce a considerable amount of inter- and intrasegmental electrostatic repulsion, leading to an expanded or extended structure for portions of the alpha s1-casein molecule in the presence of SDS. It is clear that the conformation, and hence the equivalent radius, of an SDS:protein complex is determined by the sequence of amino acids in the protein and that, a priori, it cannot be anticipated that the electrophoretic mobility of such a complex will bear more than a casual relationship to the Mr of the protein.

Animals↗
PubMed1995

Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests.

The modulating effect of bovine milk casein components and their digests on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced or not induced by mitogens has been studied with a colorimetric assay using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. All the casein components and their digests tested had little mitogenic effect on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells. Intact kappa-casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and Peyer's patch cells induced by mitogens such as lipopolysaccharide from Salmonella typhimurium, concanavalin A, phytohaemagglutinin and pokeweed mitogen. In contrast, intact alpha s1-casein and beta-casein had little effect. kappa-Casein had an inhibitory effect after digestion by pancreatin or trypsin, but not after pepsin or chymotrypsin digestion. Both pancreatin and trypsin digests of alpha s1-casein and beta-casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced by mitogens, whereas pepsin and chymotrypsin digests of both caseins were without effect. Moreover, the trypsin digest of each casein component had an inhibitory effect on mouse spleen lymphocyte proliferation in the absence of mitogen. Since trypsin is a major proteinase in pancreatin, the substrate specificity of trypsin seems to be important for the formation of the inhibitory peptides from casein components. These observations suggest that intact kappa-casein and some peptides formed from milk casein components by the action of trypsin may suppress the immune responsiveness of neonates.

Animals↗
PubMed1996

Comparative study of methods for the isolation and purification of bovine kappa-casein and its hydrolysis by chymosin.

kappa-Casein was purified from a single batch of whole acid casein (kappa-A variant) using different methods in order to compare their merits in producing a purified material with a carbohydrate and phosphate heterogeneity representative of the whole kappa-casein complement in milk. Ion-exchange methods of purification gave products of higher purity than precipitation techniques involving final purification by ethanol fractionation, but all methods resulted in kappa-caseins of apparently similar heterogeneity and chemical composition. The purified kappa-caseins were hydrolysed with chymosin and the derived macropeptides isolated. These were all virtually identical as determined by reversed-phase chromatography and gel electrophoresis. Some observations on chymosin hydrolysis of kappa-casein were made. In addition to formation of the major para-kappa-casein (Glu1-Phe105) and macropeptide (Met106-Val169), chymosin hydrolysis at pH 6.6 also resulted in two minor para-kappa-caseins with N-termini corresponding to Phe18 and Ser33 of kappa-casein. At pH 5.5 and 4.5 para-kappa-casein was rapidly hydrolysed into at least six fragments, one of which had an N-terminus corresponding to Trp76 of kappa-casein. At pH 6.6, 5.5 and 4.5 the kappa-casein macropeptide was stable to chymosin, but at pH 2.3 it was hydrolysed by chymosin into fragments with N-termini corresponding to Met106, Ile125, Ala138, Val139, Thr145 and Glu147 of kappa-casein.

Animals↗
PubMed1982

Chemical and immunochemical characterization of caseins and the major whey proteins of rabbit milk.

Caseins were separated from whey proteins by acid precipitation of skimmed rabbit milk. Whole casein was resolved by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis into three major bands with apparent relative molecular masses (Mr of 31 000, 29 000 and 25 000. On agarose/urea-gel electrophoresis whole casein gave three bands with electrophoretic mobilities alpha, beta and gamma. The three components were purified by DEAE-cellulose chromatography under denaturing and reducing conditions. Each was shown to have a different amino acid, hexose and phosphorus content, as well as non-identical peptide fragments after proteinase digestion. The 31 000 Da (dalton) protein, of alpha-electrophoretic mobility, had a high phosphorus content (4.38%, w/w); the 29 000 Da peptide, of gamma-mobility, had the highest hexose content (2.2%, w/w), contained 0.8 cysteine residue per 100 amino acid residues and was susceptible to chymosin digestion corresponding thus to kappa-casein; the 25 000 Da protein migrated to the beta-position. The rabbit casein complex is composed of at least three caseins, two of which (alpha- and kappa-caseins) are analogous to the caseins from ruminants. Although caseins are poor immunogens, specific antibodies were raised against total and purified polypeptides. The antiserum directed against whole casein recognized each polypeptide, each casein corresponding to a distinct precipitation line. The antisera directed against each casein polypeptide reacted exclusively with the corresponding casein and no antiserum cross-reaction occurred between the three polypeptides. From whey, several proteins were isolated, characterized and used as antigens to raise specific antibodies. An iron-binding protein with an apparent Mr of 80 000 was shown to be immunologically and structurally identical with serum transferrin.

Amino Acids↗
PubMed2006

Translational efficiency of casein transcripts in the mammary tissue of lactating ruminants.

Caseins are essentially concentrated in the colloidal fraction of ruminant milks as highly hydrated and mineralized spherical particles, termed casein micelles. They form a group of four peptide chains (alpha(s1), beta, alpha(s2) and kappa), encoded by four structural genes (CSN1S1, CSN2, CSN1S2 and CSN3, respectively) of which the expression is regulated by lactogenic hormones. These phosphoproteins are synthesized, essentially during lactation, in the mammary epithelial cells and we show, for the first time, that their regulation is also controlled at the translational level. Apparently, the four casein messenger are not translated with the same efficiency. Specific amplification systems have been developed and optimized to quantify, by real time quantitative PCR (qPCR), transcripts encoding the four caseins starting from total RNA extracted from mammary tissues taken on goats (n = 4), ewes (n = 3) and cows (n = 3), in lactation. The relative proportions of each specific messenger (% of casein mRNA) were compared to the relative amounts of the corresponding caseins (% of whole casein) in milks sampled from the same animals, determined after fractionation by reverse phase HPLC and integration of the corresponding peak areas. From qPCR data, the four casein transcripts appeared to be present approximately at the same level of abundance (ca. 25%, except for defective genotypes at the CSN1S1 locus, in the goat) whereas the amounts of the corresponding proteins in milk were ranging between 9 and 38% of the whole casein fraction. A comparison of specific translational efficiencies (% of protein in milk/% of transcript in the mammary tissue), showed that alpha(s1)- and beta-casein transcripts are translated ca. 3- to 4-fold more efficiently than alpha(s2)- and kappa-casein transcripts. This seems to be the rule in the three ruminant species studied. More or less optimal contexts for initiation of translation (Kozak recognition sequence of the start codon) as well as 3' untranslated region (UTR) sequences and length might explain, at least in part, our results. These preliminary results which have now to be confirmed with a larger number of individuals to strengthen our findings and conclusions, provides, however, a rational explanation to the unbalanced casein distribution (approximate proportions 4:1:4:1 for alpha(s1):alpha (s2):beta:kappa, respectively) reported for ruminant milks. The possible effects of specific secondary structures in the 5' and 3' UTRs of casein messengers still have to be considered.

3' Untranslated Regions↗
PubMed1984

Treatment of dietary casein with formaldehyde reduces its hypercholesterolemic effect in rabbits.

Rabbits were fed cholesterol-free, semipurified diets containing 42% (wt/wt) casein or 21% casein plus one of the following nitrogen sources: soy isolate, amino acid mixture simulating casein, amino acid mixture simulating soy isolate, formaldehyde-treated casein or formaldehyde-treated soy isolate. Two additional groups of rabbits were fed the 42% casein diet and the diet containing casein plus soy isolate to which 0.4% (wt/wt) pure formaldehyde was added, this amount being identical to the amount of formaldehyde present in the diets with formaldehyde-treated proteins. Growth was somewhat reduced on the three diets containing 42% casein. The diet containing 42% casein to which no formaldehyde had been added induced severe hypercholesterolemia, the level of serum cholesterol after 8 weeks being about 10 mmol/L. The hypercholesterolemia was markedly reduced by the replacement of half of the casein by soy isolate, formaldehyde-treated soy isolate or formaldehyde-treated casein. No significant reduction of the concentration of serum cholesterol was seen when half of the 42% casein was replaced by an amino acid mixture imitating either casein or soy isolate. Formaldehyde per se did not significantly influence the level of serum cholesterol. We conclude that the differential tertiary structure of intact casein and soy isolate is an important factor in determining the cholesterolemic responses in rabbits to these proteins.

Animals↗
PubMed1987

The prevention of sub-surface demineralization of bovine enamel and change in plaque composition by casein in an intra-oral model.

The ability of bovine milk phosphoprotein (casein) to be incorporated into plaque, prevent enamel sub-surface demineralization, and affect bacterial composition was determined using a modified intra-oral caries model. The intra-oral model consisted of a removable appliance containing a left and right pair of bovine enamel slabs placed to simulate an approximal area. Supragingival plaque was collected and impacted into the left and right inter-enamel spaces. The left side of the appliance was exposed to various sugar and salt solutions, while the right side was exposed to sugar and casein solutions. Sodium caseinate, the major fraction alpha s1-casein, and a tryptic digest of alpha s1-casein (TD-casein) were studied. Sodium caseinate at a level of 2% w/v in a 3% sucrose-3% glucose-salt solution (pH 7.0) prevented sub-surface enamel demineralization over a ten-day period as shown by microradiography and microhardness. Two exposures of a 2% w/v sodium caseinate, alpha s1-casein, or TD-casein solution (pH 7.0) per day prevented sub-surface enamel demineralization caused by six exposures of a 3% sucrose-3% glucose-salt solution per day over a ten-day period. Intact alpha s1-casein and tryptic peptides were shown immunochemically to be incorporated into the inter-enamel plaque. The incorporation of casein and its breakdown in plaque did not produce a significant change in the amount or composition of plaque bacteria. The ability of casein and tryptic peptides to prevent enamel demineralization was related to their incorporation into plaque, thereby increasing plaque calcium phosphate and acid-buffering capacity by the phosphoseryl, histidyl, glutamyl, and aspartyl residues and indirectly through catabolism by plaque bacteria.

Adolescent↗