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PubMed1994

Digestion and fermentation of proteins in rats fed keratin, albumin, cooked casein and antibiotics.

Dietary cooked casein promotes colon cancer in rats. We speculated and tested the hypothesis that cooking reduces the digestibility of casein, and increases the yield of bacterial metabolites, which are potential promoters of cancer. We investigated dietary means to manipulate nitrogen transfer and fermentation in the caecum. The caecal digestion of casein (cooked or not), keratin (hydrolysed or not) and bovine serum albumin (oxidized or not) was measured in rats. Protein fermentation was estimated by assaying caecal ammonia and branched-chain fatty acids. Keratin and cooked casein were digested to a very low extent, and were poorly fermented. Rats given cooked casein had 2-3 times more ammonia in their caecum than animals given the other proteins. Antibiotics (bacitracin, chlortetracycline, neomycin and spiramycin, at either 20 and 80 micrograms/ml water) decreased caecal ammonia in rats eating cooked casein, with spiramycin being most efficient. These data support the hypothesis given above, and provide ways to manipulate caecal ammonia.

Ammonia↗
PubMed2002

Antibodies to bovine beta-casein in diabetes and other autoimmune diseases.

Cow's milk is thought to be an environmental trigger for autoimmune response in Type 1 diabetes. In the present study, our aim was to investigate the antibody response to bovine beta-casein in different immune- and non-immune-mediated diseases and to establish whether such an antibody response is specific to Type 1 diabetes. We measured antibodies to bovine beta-casein using an enzyme-linked immunosorbent assay in a total of 519 sera from subjects as follows: 71 patients with Type 1 diabetes, 33 patients with coeliac disease, 100 patients with latent autoimmune diabetes in adults (LADA), 50 patients with autoimmune thyroid disease (ATD), 50 patients with Type 2 diabetes, 24 patients with multiple sclerosis (MS), and 3 different groups of controls (n = 191). Significantly increased levels of antibodies to beta-casein were found in patients with Type 1 diabetes, coeliac disease and in LADA compared to age-matched controls (p = 0.01, p = 0.02 and p = 0.01, respectively). No differences were observed in beta-casein antibody titres between patients with other disease conditions (MS, and ATD) and age-matched controls. The highest antibody response to beta-casein in Type 1 diabetic patients and in patients with coeliac disease could reflect the gut mucosal immune disorders common to Type 1 diabetes and coeliac disease. Furthermore, the elevated beta-casein antibody levels found in LADA patients suggest that the antibody response to this protein may be relevant in autoimmune diabetes.

Adolescent↗
PubMed1986

Hormonal regulation of the synthesis of casein and alpha-lactalbumin in a primary mammary cell culture system.

The addition of 5 micrograms/ml of both insulin and prolactin, 3 microM cortisol and 5% fetal bovine serum stimulated casein synthesis during a 5 day culture of mammary epithelium from lactating mice using a floating collagen gel as a culture substratum. Omission of any of the three hormones or serum decreased casein synthesis substantially. The use of 10% serum or the attached gel culture system also decreased casein synthesis. Cells cultured with the combination of the three hormones and 5% serum contained a low level of casein mRNA on day 2, but it increased to much higher levels on day 4 and 5, amounting to over 30% of total mRNA on day 5. In contrast to casein synthesis, the maximal increase in alpha-lactalbumin synthesis required the presence of 0.03 microM cortisol. The combination of insulin, prolactin and 3 microM cortisol or insulin and prolactin elicited smaller increases. The translatable mRNA for alpha-lactalbumin in cells cultured with insulin, cortisol and prolactin for 5 days was detected, but not in cells with insulin and cortisol. Both a high and low concentration of cortisol in combination with insulin increased prolactin binding capacity of cultured cells to the same extent, whereas cells cultured with insulin alone contained much lower levels of prolactin binding. The difference in the capacity of prolactin binding between cells cultured with insulin alone and those cultured with insulin and cortisol correlated well with their ability to synthesize casein in response to prolactin.

Animals↗
PubMed1999

[The significance of A1 and A2 antibodies against beta-casein in type-1 diabetes mellitus].

BACKGROUND AND OBJECTIVE: The hypothesis that cow's milk components may constitute environmental factors in the pathogenesis of insulin-dependent diabetes mellitus (IDDM) is increasingly gaining in importance. This study for the first time determined, in a family study, antibodies against the most common variants of the beta-casein (A1 and A2). PATIENTS AND METHODS: A total of 1,257 sera--from 287 patients with IDDM, 386 siblings, 477 individual parents and 107 healthy controls--were tested by enzyme-linked immunosorbent assay (ELISA) for anti-beta casein A1- and A2-IgG antibodies. RESULTS: Antibodies against casein were present in all four groups, highest titres being found in diabetics. In all four groups there was an inverse correlation between A1 and A2 antibodies and age (p < 0.001). Increased amounts of anti-casein A1 antibodies were found among patients with IDDM and their siblings. On the other hand, the serum samples from parents and control persons contained antibodies against the A2 variant. The preferential binding of sera to the one or other casein variant was in all four groups statistically significant (p < 0.001). CONCLUSION: Because the A1 variant of beta-casein correlates with the onset of IDDM, but can also occur in normal controls, this may confirm the hypothesis of a defective oral immunotolerance to cow's milk antigens in IDDM.

Adolescent↗
PubMed1979

Plasmin-mediated proteolysis of casein in bovine milk.

Plasminogen was found to be present in bovine milk by crossreactivity between rabbit antiserum to plasminogen and casein prepared from milk by acid precipitation. This result was further supported by recovery of intact 125I-labeled plasminogen from rabbit milk after its intravenous injection. Freshly isolated whole bovine casein was observed to undergo slow autoproteolysis at 37 degrees C. Polyacrylamide gel electrophoresis revealed gradual disappearance of major caseins accompanied by appearance and increase in intensity of numerous electrophoretic bands. This autoproteolysis was inhibited by low concentrations of epsilon-aminocaproic acid (0.1 mM) and diisopropyl fluorophosphate (1 mM); catalytic amounts of urokinase accelerated the process. Autoproteolysis of isolated bovine beta-casein was shown by both urea and sodium dodecyl sulfate gel electrophoresis to result in formation of gamma 1- and gamma 2-caseins. Similar electrophoretic bands were formed when beta-casein was degraded by plasmin prepared from bovine blood serum. These results support the hypothesis that bovine plasmin occurs in milk and is identical to alkaline milk protease.

Animals↗
PubMed1990

Casein expression in cytotoxic T lymphocytes.

A cDNA that expresses a mRNA restricted to cytotoxic T lymphocytes (CTL) and mammary tissue has been isolated and characterized. The deduced amino acid sequence from this cDNA shows extensive homology with the previously reported amino acid sequence for rat alpha-casein. Indeed, the presence of a six-residue-repeated motif that is specific for rodent alpha-caseins strongly supports the identification of this cDNA as mouse alpha-casein. Northern (RNA) blot analysis of many hematopoietic cell types revealed that this gene is restricted to CTL, being expressed in four of six CTL lines examined. Furthermore, CTL that express this gene were also found to express other members of the casein gene family, such as beta- and kappa-casein. These results suggest that caseins may be important in CTL function, and their potential role in CTL-mediated lysis is discussed.

Amino Acid Sequence↗
PubMed1997

Casein kinase II binds to and phosphorylates cytoplasmic dynein.

We have isolated a 27-kDa protein that binds to cytoplasmic dynein. Microsequencing of a 17-amino acid peptide of this polypeptide yielded a sequence which completely matched the predicted sequence of the beta subunit of casein kinase II, a highly conserved serine/threonine kinase. Affinity chromatography using a dynein column indicates that both the alpha and beta subunits of casein kinase II are retained by the column from rat brain cytosol. Although dynactin is also bound to the column, casein kinase II is not a dynactin subunit. Casein kinase II does not co-immunoprecipitate with dynactin, and it binds to a dynein intermediate chain column which has been preblocked with excess p150(Glued), a treatment that inhibits the binding of dynactin from cytosol. Bacterially expressed and purified rat dynein intermediate chain can be phosphorylated by casein kinase II in vitro. Further, native cytoplasmic dynein purified from rat brain can also be phosphorylated by casein kinase II in vitro. We propose that CKII may be involved in the regulation of dynein function possibly by altering its cargo specificity or its ability to interact with dynactin.

Animals↗
PubMed2002

Casein is an essential cofactor in autoantibody reactivity directed against the C-terminal SmD1 peptide AA 83-119 in systemic lupus erythematosus.

The C-terminal peptide SmD1(83-119) has been identified as an important autoantigen in systemic lupus erythematosus (SLE). ELISA studies have shown that roughly 70% of all sera from patients with SLE react with this peptide. Previous findings revealed that the addition of blocking agents and sample dilution buffers influences the discrimination between positive and negative anti-SmD1(83-119) sera in SLE. The aim of the present study was to identify possible cofactors in the anti-SmD1(83-119) reactivity. We therefore tested SLE sera (n=6) for anti-SmD1(83-119) reactivity by ELISA and analysed the effects of different blocking agents (1% skim milk, 1% gelatin, and 1% BSA). In our investigation, lipids were extracted from skim milk using dichlomethane, and the putative fraction was tested to assess the assay's ability to discriminate between positive and negative sera. The effects of enzymatic digestion by casein were analyzed, and different concentrations of casein were used to determine the role of this protein in the detection of anti-SmD1(83-119) antibodies by ELISA. Furthermore, rabbits were immunized with SmD1(83-119) adsorbed to casein and control proteins. One percent skim milk was the most effective blocking agent and sample dilution buffer for the discrimination between positive and negative sera. As demonstrated by SDS electrophoresis, the discriminative capacity was influenced by enzymatic digestion of skim milk proteins, but not by lipid extraction. Differences in anti-SmD1(83-119) reactivity upon variation of the casein concentration suggest that the protein plays a significant role in the detection of anti-SmD1(83-119) antibodies. However, our immunisation studies did not show any effect of casein on anti-SmD1(83-119) reactivity, suggesting that it has no immunogenic effect on the anti-SmD1(83-119) response. In conclusion, casein seems to be an important cofactor in autoantibody reactivity directed against the C-terminal SmD1(83-119) peptide and probably functions by changing the conformation of the peptide's critical epitope.

Animals↗
PubMed1977

Responses to postruminal infusions of graded levels of casein in lactating goats.

1. A study was made in goats of the response in terms of milk production, nitrogen utilization, plasma amino acids and amino acid uptake by the mammary gland, to postruminal infusion of casein. Goats in early lactation, housed in metabolism cages, were fed on 2-5 kg basal ration/d (containing 111 g crude protein (N X 6-25)/kg) and were given, by infusion into the abomasum, 0, 15, 30 or 45 g casein/d. 2. Milk production increased from 2-41 kg/d on the basal ration to 2-52, 2-80 and 2-94 kg/d in response to infusions of 15, 30 and 45 g casein/d respectively. Milk composition was unaffected except for milk fat, which was slightly decreased during infusions of the higher levels of casein. 3. The goats were found to be in positive N balance on the basal ration. Milk N output increased with casein infusion; the increase was equvalent to a miximum of 49% of the infused N. 4. The concentration of glucose in arterial blood plasma was decreased at the highest level of casein infusion but that of plasma urea N was unaffected by treatments. 5. Casein infusions increased the concentrations of total indispensable amino acids and the ratio, indispensable: dispensable amino acids in arterial plasma. Arterial concentrations and mammary extractions of most indispensable amino acis were increased, but only a few increases were statistically significant (Pless than 0-05); 6. Comparison of individual indispensable amino acids absorbed from the intestine with output in milk indicated that methionine was probably the first limiting amino acid. 7. The results of the experiment were compared to those of similar experiments with cows that have been reported by other workers. The possible ways in which the infused casein may have caused the responses were discussed. However, no firm conclusions regarding the mechanism involved could be drawn from the results of the present study.

Abomasum↗
PubMed1988

The phosphorylation state of casein and the species-dependency of its hypercholesterolaemic effect.

1. The present study concerns the question whether the hypercholesterolaemic effect of casein, a phosphorylated protein, is modified in species differing both in glycine-taurine conjugation of bile acids and in intestinal alkaline phosphatase (EC 3.1.3.1). 2. Since these two variables are entirely different in rabbits and rats, identical (cholesterol-free) semi-purified diets containing either casein or soya-bean protein were given to both species. 3. In rabbits casein, as compared with soya-bean protein, did not affect calcium absorption but immediately increased phosphate absorption and decreased faecal excretion of bile acids. These effects preceded the accumulation of apo B-cholesterol in serum, which indicates a cause-and-effect relation. 4. In contrast, none of these casein-specific effects were observed in rats. 5. These results suggest that the hypercholesterolaemic potential of casein is expressed mainly in species (like the rabbit) with a low activity of intestinal phosphatase and with a high glycine conjugation of bile acids. This might explain why species (like rat and man) are rather insensitive to dietary casein.

Animals↗
PubMed1993

The effects of abomasal infusions of casein or soya-bean-protein isolate on the milk production of dairy cows in mid-lactation.

The effects of abomasal infusion of casein or soya-bean-protein isolate (SPI) on milk production were investigated in four Friesian cows in mid-lactation receiving a basal diet of grass silage and barley which supplied energy and protein considerably in excess of requirements for milk production by conventional rationing standards. Three levels of infusion were used for each protein source, the corresponding doses being isonitrogenous for each of the proteins: 100, 220 and 330 g/d for casein and 115, 230 and 345 g/d for SPI. Casein produced much greater effects on the yield of milk and milk constituents than did SPI. On the highest dose of casein, milk yield was increased by 3.5 kg/d, fat output by 15% and protein output by 36%; corresponding values for the highest dose of SPI were 1.6 kg/d, 12% and 13% respectively. Increases in the yield of milk-protein were linear for casein but for SPI there was no increase beyond the first level of infusion. It was calculated that casein infusion had a marked effect on the utilization of energy: the increases in milk production could be explained either by a channelling of an extra 12 MJ metabolizable energy (ME)/d away from body tissue synthesis and into milk synthesis or by an increase in the efficiency of utilization of ME for lactation from 0.50 on the basal diet to 0.58; the measurements made did not allow the two mechanisms to be clearly differentiated.

Abomasum↗
PubMed2003

Na+/glucose co-transporter abundance and activity in the small intestine of lambs: enhancement by abomasal infusion of casein.

The purpose of the present study was to determine the effect of abomasal casein infusion on glucose uptake and abundance of the Na+/glucose co-transporter (SGLT1) 1 in the ovine small intestine. Lambs (body weight 35 (sem 1.0) kg) were surgically fitted with abomasal infusion catheters and were fed diets containing equal portions of wheat hay and cracked maize. Lambs were infused with either 500 g water/d or with 500 g water containing 35 g casein/d. The infusion period lasted 10 d, after which lambs were killed, exsanguinated and eviscerated. Brush border membrane vesicles (BBMV) were prepared using mucosa from different small intestinal regions. Intake and total tract digestibility of nutrients were similar between treatments and averaged 1134, 1142 and 486 g/d and 67, 70, and 94 % for DM, organic matter and non-structural carbohydrates respectively. Crude protein (Nx6.25) digestibility was 15 % greater in the casein-infused than control lambs. Glucose uptake to BBMV ranged from 101 to 337 pmol/mg protein per s along the small intestine and was greatest in the mid-section of the small intestine. In the mid-jejunum, glucose uptake was greater (P<0.07) in lambs infused with casein and averaged 120 pmol/mg protein per s compared with 68 pmol/mg protein per s in the control group. SGLT1 affinity was similar between treatments and averaged 104 microm in the different segments of the small intestine of lambs. However, lambs infused with casein exhibited similar values along the small intestine and affinity averaged 106 microm, while in the control group a greater affinity (85 microm) was measured in the mid-jejunum. SGLT1 protein abundance was correlated with glucose uptake in the BBMV in the casein-treated lambs, but not in the control group. These results suggest that glucose uptake along the small intestine of lambs is influenced by casein or its derivatives in the small intestine via SGLT1 affinity and activity at the brush border membrane, and that SGLT1 activity may be regulated by post-translational events affected by amino acids and peptides.

Abomasum↗
PubMed1975

[Lysine resorption in rats fed on heated casein].

Male Wistar rats six month old were fed on a diet containing 10% casein heated for 4 h at 140 degrees C; control rats got untreated casein. The content of available lysine (as determined according to RAO et al.) was 5.8 g/16g N in heated and 8.5 g/16 gN in untreated casein. The contents of free and total lysine and of epsilon-DNP-lysine were estimated in deproteinized portal blood plasma and in urine. In the former the contents of the remaining amino acids before and after acid hydrolysis were also determined. Deproteinized portal blood plasma of rats fed on untreated or heated casein contained, respectively, un mumoles per 10 ml: total lysine 9.0 and 9.9; free lysine 3.7 and 2.8; bound lysine (total lysine -free lysine) 5.3 and 7.1; peptide-bound lysine (determined as epsilon-DNP-lysine) 4.9 and 4.6; and epsilon-bound lysine (bound lysine - peptide-bound lysine) 0.5 and 2.6. The data indicate that lysine with blocked epsilon-amino group was released in the course of digestion of the heated casein and absorbed. This is additionally substantiated by the presence of this form of lysine in the urine of rats given heated casein.

Animals↗
PubMed1982

Construction and identification by partial nucleotide sequence analysis of bovine casein and beta-lactoglobulin cDNA clones.

Double stranded (DS) DNA molecules obtained by reverse transcription of a partially purified lactating bovine mammary gland mRNA fraction were cloned into pBR322. Restriction maps for four recombinants were constructed and partial nucleotide sequence analysis of these revealed coding sequences corresponding to alpha s1-, beta-, and kappa-casein and beta-lactoglobulin. The specific single-stranded (SS) cDNAs representing each of these species were identified and their nucleotide lengths estimated. Evidence is presented that these are essentially full-length transcripts of the major mRNA species. On this basis, the cDNA clones range in size from 50% for beta-casein to about 95% for alpha s1-casein in comparison with their respective mRNAs. The DNA sequence spanning all eight phosphoserine residues in alpha s1-casein is presented. These data, together with other serine codon usage data, indicate that the mammary gland phosphoseryl tRNA does not play a role in the incorporation of serine phosphate residues during casein synthesis. The observation that the nucleotide sequences for the serine phosphate cluster in bovine alpha s1-and rat beta-casein exhibit close homology supports the suggestion that these regions have evolved from a common primordial sequence.

Animals↗
PubMed1976

Characteristic inhibition of in vitro swelling of purified rat liver mitochondria induced by Ca2+ or thyroxine by feeding rats a low casein diet.

It has been shown previously by the author that the structure of rat liver mitochondria is changed by a low casein diet. In the present experiments, using the free fatty acid producing substances Ca2+ and thyroxine, and the free fatty acid sodium oleate, the influence of a 4% casein diet on the in vitro swelling process of purified rat liver mitochondria was investigated by following the decrease in optical density at 520 nm after addition of one of the swelling agents. Swelling due to hypotonicity was also investigated. Rats were fed the test diets for 80 to 100 days. Mitochondria were purified by washing three times; after each wash the isotonic suspension was centrifuged at 3,000 X g for 6 minutes. The results show that the in vitro swelling of mitochondria induced by Ca2+ or thyroxine was inhibited greatly in the early period of swelling in rats fed a low casein diet. By comparison to this, there was not a notable effect of a low casein diet on the rate of swelling induced by sodium oleate. But in the case of sodium oleate, the values of optical density were always higher in rats fed a low casein diet, and the differences between two groups were always significant. Swelling due to hypotonicity was not affected at all by a low casein diet.

Animals↗
PubMed1981

Effect of casein and starch infusion in the large intestine on nitrogen metabolism of growing swine.

Eight crossbred female pigs (40 kg) with cannulae placed in the terminal ileum were used to evaluate the effect of infusions of casein starch and casein plus starch on organic matter fermentation and microbial protein synthesis in the large intestine, and their effect on urinary urea and orotic acid excretion, and on nitrogen (N) retention. Infused casein and starch were both totally digested. Nitrogen retention was increased (P greater than 0.05) when casein was infused. Starch infusion resulted in an increase (P greater than 0.05) in fecal N in the form of total protein (amino acids). The high correlation (P greater than 0.01) between fecal total protein and RNA indicates that the increase in fecal N resulted from an increase in microbial protein synthesis. About 5.2 g of bacterial protein was synthesized per 100 g of cornstarch fermented in the large intestine. Casein infusion increase (P greater than 0.05) total urinary N. Differences between treatments for urinary N were entirely because of changes in urinary urea. Urinary ammonia and unaccounted N were not affected by treatments. Urinary orotic acid was a good indicator of the urea cycle activity because of its hig correlation (P greater than 0.0) with urinary urea. Plasma urea N concentration was increased (P greater than 0.05) only when casein plus starch was infused.

Animals↗
PubMed1992

Dietary casein and soybean protein affect the concentrations of serum cholesterol, triglyceride and free amino acids in rats.

This work was undertaken to investigate the concentrations of free amino acids in blood after food was withheld from growing, male Wistar rats fed cholesterol-free, low fat (1 g corn oil/100 g) diets with casein or soybean protein for 2 wk. A diet containing 22.5 or 23.5 g/100 g of soybean protein was hypocholesterolemic compared with a diet containing 20.0 g casein/100 g diet. A comparison of serum amino acids in soybean protein-fed vs. casein-fed rats showed that, whereas concentrations of many amino acids were lower in the soybean protein-fed rats compared with the casein-fed groups, glycine was the only amino acid having a higher concentration. Further, alanine was significantly lower in the soybean protein-fed rats compared with the casein-fed rats, and the protein-induced differences in glycine and alanine concentrations of unfed rats were reproducible. When diets containing 15.0% casein or 30.0% soybean protein, a casein diet supplemented with glycine and a soybean protein diet supplemented with methionine were compared, the changes in serum glycine and alanine correlated with the changes in serum cholesterol. Concentrations of several amino acids, particularly valine, leucine and tyrosine, also changed when serum cholesterol concentrations varied, but these effects could not be explained by our experiments. The results suggest that a change in serum concentration of glycine and alanine of unfed rats may be related to the change in serum cholesterol concentration.

Alanine↗
PubMed1993

Dietary soybean protein compared with casein retards senescence in the senescence accelerated mouse.

The effects of replacing dietary casein with soybean protein on mean life span, mean life span of the last one-tenth of a group, grading scores of senescence and deposition of senile amyloid were investigated in senescence accelerated mice (SAM-P/1) compared with a control strain (SAM-R/1). SAM-R/1 mice fed the soybean protein-containing diet had mean life spans of 618 +/- 42 d (males) and 578 +/- 62 d (females), 58% (males) and 44% (females) longer than those of corresponding casein fed mice (P < 0.01). Similarly, in SAM-P/1 mean life-spans were 265 +/- 16 d (males) and 307 +/- 23 d (females) in the soybean diet group, 27% (males) and 30% (females) longer than in the casein diet groups (P < 0.01). The mean life span of the last one-tenth of each group fed soybean protein was significantly longer than the corresponding group fed casein. In SAM-R/1 mice, pathological studies revealed that severe secondary amyloid deposition (amyloid A protein) in the kidneys, spleen, stomach and liver was significantly suppressed, in males only, by replacing casein with soybean protein (P < 0.01). The occurrence of contracted kidneys caused by the infiltration of amyloid A protein was suppressed in SAM-R/1 mice fed the soybean protein-containing diet (P < 0.05). The deposition of senile amyloid in SAM-P/1 mice with aging was retarded by replacing casein with soybean protein (P < 0.01). These results indicate that dietary protein source is important in modulating the advance of senescence in SAM mice.

Aging↗