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PubMed1977

Increase in cytochrome contents of liver mitochondria on feeding rats a low casein diet.

Williams et al. (1) investigated the changes in amounts of total mitochondrial protein and cytochromes in the liver of rats fed a protein-free diet for a long period, and found that there was a marked similarity between changes in amount of total mitochondrial protein and that of cytochromes. Present experiments were performed to clarify whether under a more mild protein-deficient state the relationships found by Williams are applicable or not by investigating the changes in contents of cytochromes per unit amount of mitochondrial protein when rats were fed a low case diet. A 4% casein diet was used as a low casein diet, and a 25% casein diet was used as a control diet. Rats were fed the test diets for 70 to 90 days. The results show that the contents of all cytochromes a, b, and c1 + c assayed and expressed as nmoles per mg of mitochondrial protein were significantly higher in rats fed a low casein diet than those in rats fed a control diet. These suggest that relationships found by Williams in a severe protein-deficient state would not be applicable in a more mild protein-deficient state.

Animals↗
PubMed1979

Minor components of reduced bovine kappa-casein.

Bovine kappa-casein reduced with 2-mercaptoethanol was fractionated on a DEAE-cellulose column to one nonadsorbed, five major adsorbed and two minor adsorbed fractions. The properties of the nonadsorbed and five major adsorbed fractions were reported in our previous paper (4). In this paper, the characteristics of two minor adsorbed fractions (P-X and P-Y) were reported. Gel electrophoretic patterns of these fractions were similar to kappa-casein. These fractions had the same amino acid composition and the same phosphorus content as the major components. P-X contained one residue each of N-acetylneuraminic acid, galactose and galactosamine, and P-Y two residues each. Furthermore, these fractions showed the stabilizing ability for alpha s1-casein in the presence of calcium ion. These results indicate that P-X and P-Y are minor components of reduced bovine kappa-casein.

Amino Acids↗
PubMed1983

Gelation of the complex between kappa-casein and beta-lactoglobulin.

The gelation of the complex between kappa-casein and beta-lactoglobulin was examined. The apparent viscosity of the mixture of kappa-casein and beta-lactoglobulin increased by heat treatment. The mixture formed a gel at the concentration of 8% (w/w). The gel formation was accelerated by the chymosin treatment. The mixture of kappa-casein and beta-lactoglobulin in each concentration of 1.5% gelled by the addition of chymosin after heat treatment. Forming the complex between kappa-casein and beta-lactoglobulin was necessary to the gel formation. Therefore, heat treatment of above 70 degrees C was demanded. Turbidity increased and the relative content of soluble protein decreased accompanied with gel formation. The addition of calcium ion to the heated solution produced an increase in turbidity. The larger the protein concentration was, the larger the breaking stress of the formed gel was. The addition of calcium ion weakened the breaking stress of the gel.

Calcium↗
PubMed1992

Effects of casein and soy-protein on alpha-linolenic acid metabolism in rats.

In order to study the effects of different proteins on alpha-linolenic acid (alpha-LnA) metabolism, rats were given the diet added respectively with milk casein and soy-protein isolate (SPI) as sources of proteins and perilla oil as a source of lipid. The results obtained are as follows. The ratio of (C20:3 + C20:4)/C18:2 in liver microsomal PL, liver PE fraction, and kidney PE and PC fractions was significantly lowered by the SPI treatment when compared to the casein treatment, similarly to the already established results. In the liver microsomal PL and PE and PC fractions of liver and kidney in rats treated with SPI, there was also observed a significant decrease or a decrease tendency in the (C20:4 + C20:5)/C18:3 ratio. A similar tendency was again shown in the sigma (n-3)M/C18:3 ratio indicating metabolic conversion from C18:3(n-3) to C22:6. On the other hand, contrary to the ratios of (C20:3 + C20:4)/C18:2, sigma (n-3)M/C18:3, and (C20:3 + C20:5)/C18:3, the (C22:5 + C22:6)/C20:5 ratio which is the parameter for metabolic conversion of C20:5(n-3) was elevated in the PE and PC fraction of liver, heart and kidney in the SPI group compared to the casein group. Then, further analysis of the metabolic process from C20:5 to C22:6 showed that the C22:5/C20:5 ratio increased while the C22:6/C22:5 ratio decreased in the SPI group compared to the casein group. Based on these results, it is assumed that the metabolic process from C18:3(n-3) to C20:5(n-3) and from C22:5 to C22:6 is affected by SPI but that the elongation process from C20:5(n-3) to C22:5(n-3), on the contrary, is rather accelerated by SPI.

Animals↗
PubMed1997

Action of 3 tyrphostin derivatives on casein kinase II from rat liver.

AIM: To study the action of tyrphostin on casein kinase (CK) II. METHODS: CK II was partially purified from rat livers by sequential DE52 and heparin-Sepharose chromatography. CK II activity was assayed by incubating CK II with dephosphorylated casein and [gamma-32P]ATP. RESULTS: AG34 inhibited the activity of CK II with IC50 33 (27-41) mumol.L-1. Both AG372 (121 mumol.L-1) and AG1112 (150 mumol.L-1) displayed inhibitory effects on the activity of CK II. Kinetic studies of AG34 on CK II showed that it was noncompetitive with casein and ATP. CONCLUSION: AG34, AG372, and AG1112 were potent inhibitors of CK II, and the inhibitory action of AG34 was noncompetitive with casein and ATP.

Animals↗
PubMed1976

Retinal degeneration in cats fed casein. II. Supplementation with methionine, cysteine, or taurine.

All cats fed a taurine-free casein diet for 23 weeks have shown a nondetectable electroretinogram (ERG) in association with a plasma and retinal taurine deficiency. In the present study, the casein diet was supplemented with either taurine or taurine precursors (methionine or cysteine) for 23 weeks to see if retinal function would be preserved. Cats fed the casein diet supplemented with methionine or cysteine showed ERG's reduced in amplitude and delayed in implicit time and had plasma and retinal taurine levels that were well below normal by 23 weeks. Only those cats given taurine in the diet (i.e., those fed chow or casein supplemented with taurine) retained normal ERG function and normal plasma and retinal taurine concentrations. These findings establish a role for taurine in maintaining normal retinal function in the cat.

Animals↗
PubMed1992

Structure-function analysis of casein kinase 2 with synthetic peptides and anti-peptide antibodies.

Casein kinase 2 (CK2) is a ubiquitous, multifunctional protein-seryl/threonyl kinase that has been implicated in cellular regulation. Synthetic peptides were patterned after three highly conserved regions in CK2: the N terminus (CK2-NT); the lysine-rich, kinase subdomain III segment (CK2-III) (nomenclature of Hanks et al. (Hanks, S. K., Quinn, A. M., and Hunter, T. (1988) Science 241, 42-52)); and a 10-residue segment located near kinase subdomain X that is shared between CK2 and p34cdc2 (CK2/cdc2). The CK2-III and CK2/cdc2 peptides markedly stimulated the autophosphorylation of the alpha- and alpha'-subunits of purified CK2 from sea star oocytes, and they elicited up to 2-fold increases in its casein or phosvitin phosphotransferase activity. These peptides completely reversed nearly total inhibition of CK2 phosphotransferase activity toward itself, casein, and phosvitin by either heparin or poly(Glu,Tyr; 4:1), whereas CK2-NT was ineffective. Elution of CK2 from heparin-agarose with the CK2-III peptide indicated that this region of CK2 might mediate heparin binding to CK2. Affinity-purified rabbit polyclonal antibodies developed against both CK2-III and CK2/cdc2, but not CK2-NT, also produced up to 1.8-fold enhancements of the casein and phosvitin phosphotransferase activities of purified CK2. All three of the antipeptide antibody preparations immunoreacted with the alpha- and alpha'-subunits of CK2 on Western blots. These studies indicate that kinase subdomains III and X are involved in the modulation of CK2 phosphotransferase activity.

Amino Acid Sequence↗
PubMed1992

[Effect of casein on the temporo-spatial organization++ of the contractile activity of the small intestine in the dog].

Some observations in man and experimental animals have demonstrated that casein decreases intestinal transit speed. However, its effects on intestinal motility have not been studied previously in a systematic fashion. The aim of this work was to study the temporospatial distribution of small bowel motility before and after the administration of calcium caseinate. Studies were performed in fasting dogs using 6 catheters perfused with a pneumo-hydraulic system. After the administration of 300 ml of a 10% solution of calcium caseinate, a global decrease in motor activity was observed, specially of grouped propulsive contractions, they were reduced in 64.9 to 19.5%. On the contrary, a significative increase, in 1.4 to 22%, of individual wave, non propulsive motor activity was observed. These quantitative changes in contractions, specially in their organization and temporo-spatial distribution, may be responsible for the decrease in intestinal transit after the administration of casein.

Animals↗
PubMed1992

Mutations away from splice site recognition sequences might cis-modulate alternative splicing of goat alpha s1-casein transcripts. Structural organization of the relevant gene.

alpha s1-Casein variants F and D, synthesized in goat milk at lower levels than variant A, essentially differ from it by internal deletions of 37 and 11 amino acid residues, respectively. Northern blot analysis of mRNAs encoding alpha s1-casein F and A and sequencing of the relevant cloned cDNAs, as well as sequencing of in vitro amplified genomic fragments, revealed multiple alternatively processed transcripts, from the F allele. Although correctly spliced messengers were identified, most of the FmRNAs lacked three exons. These exons, further identified as exons 9, 10, and 11, together encode the 37 amino acid residues present in alpha s1-casein variant A but missing in variant F. Exon 9 codes for the sequence present in variant A but deleted in variant D. A single nucleotide deletion in exon 9 and two insertions, 11 and 3 base pairs in length, in the downstream intron, were identified as mutations potentially responsible for the alternative skipping of these 3 exons. From a computer-predicted secondary structure it appeared that the 11-base pair insertion might be involved in base-pairing interactions with the intron 5' splice site which might consequently be less accessible to U1 snRNA. We also report here the complete structural organization of the goat alpha s1-casein transcription unit, deduced from polymerase chain reaction experiments. It contains 19 exons scattered within a nucleotide stretch nearly 17-kilobase pairs long.

Amino Acid Sequence↗
PubMed1992

[Cytoplasmic casein kinase 2 and its substrate proteins in the brain in Alzheimer's disease].

The absence of casein kinase 2 on blots of temporal cortex extracts from Alzheimer's disease patients (ADP) was shown using antiserum to casein kinase 2. Casein kinase 2 activity towards endogenous substrates and casein is 2-5 times less in ADP brain in comparison to normal controls. The fractions of heparin-binding proteins, containing protein substrates for phosphorylation, were isolated from temporal cortex of ADP and normal controls. The total amount of heparin-binding proteins from ADP brains is less than from control brains, and the polypeptide composition of these fractions is much more poop.

Aged↗
PubMed2004

[Study on a human tissue-type plasminogen activator mutant cDNA knocked-in the beta-casein gene site of murine ES cells].

A murine beta-casein gene targeting vector was constructed using the cloned genomic sequence. The short arm was 2.7 kb including mouse beta-casein gene 5' flanking sequence, exon1, intron1 and partial exon2. The long arm is a 3.4 kb fragment including partial intron2, exon3 approximately 7, intron3 approximately 6 and partial intron7. The human t-PA mutant cDNA was subcloned in the exon2 and fused with the mice beta-casein signal peptide sequence. The positive selective marker neo was placed in the middle of intron2. A tk negative selective marker was just outside the short arm. TC-1 ES cells were cultured and amplified on G418 resistant feeder layer. The linearized targeting construct DNAs of 45 microg were introduced into 2 x 10(7) ES cells by electroporation. Totally 192 ES clones were picked up after cultured in G418 and Gancyclovir for 7 days. The colonies were amplified and subjected to genomic DNA preparation. The genomic DNAs were digested with EcoR I and used for Southern blot analysis. A probe inside the 5' homologous arm was used for hybridization. A 9.8 kb band was found in wild type, but the band was shift down from 9.8 kb to 6.6 kb in the beta-casein gene targeted allele because a new EcoR I site was introduced into the exon2 along with the human t-PA mutant gene. There were 9.8 kb and 6.6 kb bands in targeted ES cells. One clone of targeted ES cells with correct homologous recombination events was obtained among 78 analyzed clones. It lays foundation for gene targeted mice making.

Animals↗
PubMed1992

3,4-dichloroisocoumarin-induced activation of the degradation of beta-casein by the bovine pituitary multicatalytic proteinase complex.

The breakdown of beta-casein (caseinolytic activity) by the bovine pituitary multicatalytic proteinase complex (MPC) is initiated by a fourth active site different from the previously described chymotrypsin-like activity (cleavage of Cbz-Gly-Gly-Leu-p-nitroanilide, where Cbz is benzyloxycarbonyl), trypsin-like activity (cleavage of Cbz-D-Ala-Leu-Arg-2-naphthylamide), and peptidylglutamyl peptide bond-hydrolyzing (PGP) activity (cleavage of Cbz-Leu-Leu-Glu-2-naphthylamide) (Yu, B., Pereira, M. E., and Wilk, S. (1991) J. Biol. Chem. 266, 17396-17400). 3,4-Dichloroisocoumarin, a serine proteinase inhibitor, stimulated the caseinolytic activity of bovine pituitary or lens MPC, 3-18-fold under conditions under which the other three catalytic activities were inactivated. Addition of hydroxylamine to the modified enzyme did not reverse the effects of the inhibitor. A form of the proteinase exhibiting only 2-4% of control chymotrypsin-like, trypsin-like, and PGP activities degraded beta-casein with no accumulation of intermediate peptides. 3,4-Dichloroisocoumarin, by reacting with the chymotrypsin-like, trypsin-like, and/or PGP-active sites, may promote a conformational change of MPC, rendering the caseinolytic active site accessible to the substrate. Once bound to the active site, beta-casein is rapidly degraded either by the caseinolytic component itself or by a cooperative interaction with catalytic centers that are not affected by the serine proteinase inhibitor. These results imply that the caseinolytic component does not belong to the class of serine proteinases. Other proteins tested were not degraded by the 3,4-dichloroisocoumarin-treated enzyme, suggesting that the conformation of beta-casein may be more adequate for degradation by the caseinolytic component.

Amino Acid Sequence↗
PubMed2005

Evaluation of the effect of somatic cell counts on casein proteolysis in ovine milk cheese by means of capillary electrophoresis.

The primary proteolysis of ewe's cheeses made from milk with different somatic cell counts (5CC) included three groups of study: cheeses made with milk with less than 500,000 somatic cells (SC); with milk containing 1 x 10(6) to 1.5 x 10(6) SC, the normal range for ewe's milk; and with milk containing more than 3.106 SC. These were examined by capillary eledrophoresis. Intact caseins as alpha(s1)-CN (I, II, and III), alpha(s2)-CN, and beta-CN (beta, beta1, and beta2) were identified. Some peptides resulting from casein proteolysis as gamma-CN and l-alpha(s1)-CN were also identified. The study reveals that proteolysis increased with ripening time and the extent of casein degradation depended on the content in SC, showing that residual intact casein, both alpha(s1)-CN and beta-CN, decreased as the SCC of milk increased because of their higher proteolytic enzyme levels. The proteolysis pattern indicated that several enzymes were implicated in increased proteolysis in high SCC cheeses.

Animals↗
PubMed1992

Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.

In human epidermal carcinoma A431 cells, the beta subunit of casein kinase II is phosphorylated at an autophosphorylation site and at serine 209 which can be phosphorylated in vitro by p34cdc2 (Litchfield, D. W., Lozeman, F. J., Cicirelli, M. F., Harrylock, M., Ericsson, L. H., Piening, C. J., and Krebs, E. G. (1991) J. Biol. Chem. 266, 20380-20389). Given the importance of p34cdc2 in the regulation of cell cycle events, we were interested in examining the phosphorylation of casein kinase II during different stages of the cell cycle. In this study it is demonstrated that the extent of phosphorylation of serine 209 in the beta subunit is significantly increased relative to phosphorylation of the autophosphorylation site when chicken bursal lymphoma BK3A cells are arrested at mitosis by nocodazole treatment. This result suggests that serine 209 is a likely physiological target for p34cdc2. In addition, the alpha subunit of casein kinase II also undergoes dramatic phosphorylation with an associated alteration in its electrophoretic mobility when BK3A cells or human Jurkat cells are arrested with nocodazole. Phosphopeptide mapping studies indicate that p34cdc2 can phosphorylate in vitro the same peptides on the alpha subunit that are phosphorylated in cells arrested at mitosis. These phosphorylation sites were localized to serine and threonine residues in the carboxyl-terminal domain of alpha. Taken together, the results of this study indicate that casein kinase II is a probable physiological substrate for p34cdc2 and suggest that its functional properties could be affected in a cell cycle-dependent manner.

Animals↗
PubMed1991

L-cell growth stimulation by a beta-casein peptide: the importance of its phosphorylation site for activity.

L-cell proliferation was markedly enhanced by addition to the medium of a synthetic peptide corresponding to residues 1-18 of human beta-casein. Experiments using several synthetic peptides of decreasing length demonstrated that L-S-S-S-E-E (residues 7-12), a major phosphorylation site in beta-casein, appeared to be important for the activity. The phosphorylated beta-casein peptide showed no activity. Recent findings have demonstrated that a similar sequence, S-E-E-E or S-D-D-E, is commonly present in many oncoproteins derived from nuclear oncogenes such as myc, myb and E1A, and plays an important role in transformation functions. The beta-casein peptide may affect mammalian cell proliferation through a modification of of the oncoprotein functions.

Amino Acid Sequence↗
PubMed1991

Influence of casein feeding to very-low-birth weight infants on the plasma amino acid concentrations and the renal amino acid excretion.

The response of plasma and urine amino acid concentrations to a casein formula and to supplemented human milk (both 1.4 gm protein/100 ml) was measured in very-low-birth weight (VLBW) infants (less than 1500 gm) at a postconceptional age of 36 and 40 weeks, respectively. A control group of infants was fed exclusively with fresh human milk (HM). Casein feeding to VLBW infants resulted in prefeeding plasma amino acid profiles and renal amino acid excretions which were not markedly different from those found in infants fed supplemented HM. In comparison with the control feeding group, the infants fed casein or supplemented HM responded with higher total plasma amino acid concentrations (114.4 +/- 33.7 vs 171.0 +/- 36.1 or 167.1 +/- 27.1 mumol/100 ml, respectively) reflecting the higher amount of protein provided by these two feedings. The critical amino acids (sulfur-containing and aromatic amino acids) were metabolized efficiently in infants fed the casein formula. Furthermore, a highly significant relationship (r = 0.795; p less than 0.001) between the plasma concentrations of tyrosine and valine was achieved in all infants independent of the food applied. This relationship could represent a control mechanism to prevent an inordinate influx of aromatic amino acids into the brain. In VLBW infants at a postconceptional age of 36-40 weeks, the metabolic and functional maturity reaches levels which were similar to those found in term newborns.

Aging↗
PubMed1991

Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calsequestrin.

Calsequestrin is an acidic Ca2(+)-binding protein of sarcoplasmic reticulum existing as different gene products in cardiac muscle and skeletal muscle. A unique feature of cardiac calsequestrin is a 31-amino acid-long COOH-terminal tail (Scott, B. T., Simmerman, H. K. B., Collins, J. H., Nadal-Ginard, B., and Jones, L. R. (1988) J. Biol. Chem. 263, 8958-8964), which is highly acidic and contains several consensus phosphorylation sites for casein kinase II. In the work described here, we tested whether this cardiac-specific sequence is a substrate for casein kinase II. Both cardiac and skeletal muscle calsequestrins were phosphorylated by casein kinase II, but cardiac calsequestrin was phosphorylated to a higher stoichiometry and at least 50 times more rapidly. The site of rapid phosphorylation of cardiac calsequestrin was localized to the distinct COOH terminus, where a cluster of three closely spaced serine residues are found (S378DEESN-DDSDDDDE-COOH). The slower phosphorylation of skeletal muscle calsequestrin occurred at its truncated COOH terminus, at threonine residue 363 (I351NTEDDDDDE-COOH). The similar sequence in cardiac calsequestrin (I351NTEDDDNEE) was not phosphorylated. Cardiac calsequestrin, as isolated, already contained 1.2 mol of Pi/mol of protein, whereas skeletal muscle calsequestrin contained only trace levels of Pi. The endogenous Pi of cardiac calsequestrin was also localized to the distinct COOH terminus. Our results indicate that the cardiac isoform of calsequestrin is the preferred substrate for casein kinase II both in vivo and in vitro.

Amino Acid Sequence↗
PubMed1991

Association of casein kinase II with immunopurified p53.

Viral and cellular oncogene products sometimes activate protein kinases, are protein kinases themselves, or share phosphorylation sequence motifs for different protein kinases. We have recently shown that a protein kinase activity is tightly associated with immunopurified p53. We have now expressed p53 in a baculovirus expression system and characterized this protein kinase activity in more detail. We found that casein could compete with p53 in the kinase reaction. Heparin efficiently inhibited the p53 associated protein kinase whereas the polyamine spermidine stimulated enzymatic activity. A synthetic peptide which was shown to be specifically phosphorylated by casein kinase II blocked the in vitro phosphorylation of p53, whereas a synthetic peptide with a potential phosphorylation site on human p53 at ser 315 was ineffective in blocking the phosphorylation of p53. GTP as well as ATP can be used as a phosphate donor in the in vitro kinase reaction. An antibody directed against casein kinase II coprecipitated p53 from insect cells as well as from mammalian cells. These data strongly indicate that casein kinase II is associated with immunopurified p53 and contributes to the phosphorylation of p53. A mutant p53 with a ser 389 to ala exchange was not phosphorylated in vitro by the p53 associated protein kinase.

Amino Acid Sequence↗