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PubMed1992

Different effects of casein and soyabean protein on gastric emptying of protein and small intestinal transit after spontaneous feeding of diets in rats.

The effects of dietary casein and soyabean-protein isolate (SPI) on gastric emptying and small intestinal transit were observed in rats fed on an 80 g casein or 80 g SPI/kg diet. After a 24 h fast, rats were given 2 g of both the test diets containing 10 g guanidinated casein/kg diet as a marker protein. The amounts of the marker protein remaining in the stomach of the rats fed on the casein or SPI diet were similar and decreased to about 50% after 20 min. The emptying rate then slowed, especially in the casein group, so that the amount leaving the stomach after 1 h in the SPI group was slightly higher (P < 0.05). The small intestinal transit of chyme was estimated by a bolus injection of colloidal carbon suspension or of colloidal carbon and 3H-labelled polyethylene glycol through an implanted duodenal catheter 6 min before death. The average value of transit at 12, 20, 40 and 60 min after feeding of SPI diet was about 25% faster than that after casein diet. The transit velocity of the SPI group was also faster than that of the non-protein group 40 min after feeding. These findings reveal that SPI enhances the small intestinal transit of the liquid phase of chyme. There was no correlation between the gastric emptying of homarginine and small intestinal transit. This result suggest that the small intestinal transit of lumen contents is controlled by the dietary protein regardless of the gastric emptying of protein.

Animals↗
PubMed1993

Lowering effect of dietary milk-whey protein v. casein on plasma and liver cholesterol concentrations in rats.

The effect of dietary whey protein v. casein on plasma and liver cholesterol concentrations was investigated in female, weanling rats. Balanced, purified diets containing either whey protein or casein, or the amino acid mixtures simulating these proteins, were used. The high-cholesterol diets (10 g cholesterol/kg feed) had either 150 or 300 g protein or amino acids/kg feed. The diets were fed for 3 weeks. At the low dietary protein level, whey protein v. casein did not affect plasma total cholesterol, but lowered the concentration of liver cholesterol. At the high dietary protein level, whey protein significantly lowered plasma and liver cholesterol and also plasma triacylglycerols. The hypocholesterolaemic effect of whey protein was associated with a decrease in very-low-density-lipoprotein cholesterol. At the high dietary protein concentration, whey protein reduced the faecal excretion of bile acids when compared with casein. The effects of intact whey protein v. casein were not reproduced by the amino acid mixtures simulating these proteins. It is suggested tentatively that the cholesterol-lowering effect of whey protein in rats is caused by inhibition of hepatic cholesterol synthesis.

Animals↗
PubMed1994

Casein and soya-bean protein have different effects on whole body protein turnover at the same nitrogen balance.

The present study examined whether different proteins have different effects on whole-body protein turnover in adult rats. The rats were either starved, given a protein-free but energy-sufficient diet (1 MJ/kg body weight (BW) per d) or a diet containing intact casein, hydrolysed casein, or hydrolysed soya-bean protein at a level of 9.1 g/kg BW per d. The diets, which were isoenergetic with the same carbohydrate: fat ratio, were given as a continuous intragastric infusion for at least 4 d. During the last 19 h 15N-glycine (a primed continuous infusion) was given intragastrically and 15N was recovered from urinary ammonia and urea during isotope steady state for measurement of protein synthesis and protein degradation. Compared with starvation the protein-free diet decreased N excretion by 75%, probably by increasing the rate of reutilization of amino acids from endogenous proteins for protein synthesis. The protein diets produced a positive N balance which was independent of the protein source. Intact and hydrolysed casein increased protein synthesis 2.6- and 2.0-fold respectively, compared with the protein-free diet. Protein degradation increased 1.4- and 1.2-fold respectively. Hydrolysed soya-bean protein did not increase protein synthesis but decreased protein degradation by 35% compared with the protein-free diet. Compared with the hydrolysed soya-bean protein, intact casein resulted in 2.2- and 2.8-fold higher rates of protein synthesis and degradation respectively. These results are not easily explained by known sources of misinterpretation associated with the 15N-glycine method. Hydrolysed casein and hydrolysed soya-bean protein produced similar concentrations of insulin-like growth factor-1, insulin, glucagon, and corticosterone. The difference in amino acid composition between the dietary proteins was reflected in plasma amino acid composition and this is suggested to be responsible for the different effect on protein turnover. Preliminary results from this study have previously been published in abstract form (Nielsen et al. 1991).

Amino Acids↗
PubMed1995

Colonic protein fermentation and promotion of colon carcinogenesis by thermolyzed casein.

Thermolyzed casein is known to promote the growth of aberrant crypt foci (ACF) and colon cancer when it is fed to rats that have been initiated with azoxymethane. We speculated that the promotion was a consequence of increased colonic protein fermentation (i.e., that the thermolysis of the casein decreases its digestibility, increases the amount of protein reaching the colon, and increases colonic protein fermentation and that the potentially toxic products of this fermentation promote colon carcinogenesis). We found that the thermolysis of casein reduces its digestibility and increases colonic protein fermentation, as assessed by fecal ammonium and urinary phenol, cresol, and indol-3-ol. Thermolysis of two other proteins, soy and egg white protein, also increases colonic protein fermentation with increased fecal ammonia and urinary phenols, and thermolysis of all three proteins increases the levels of ammonia and butyric, valeric, and i-valeric acids in the cecal contents. We found, however, that the increased protein fermentation observed with thermolysis is not associated with promotion of colon carcinogenesis. With casein, the kinetics of protein fermentation with increasing thermolysis time are clearly different from the kinetics of promotion of ACF growth. The formation of the fermentation products was highest when the protein was thermolyzed for one hour, whereas promotion was highest for protein that had been thermolyzed for two or more hours. With soy and egg white, thermolysis increased colonic protein fermentation but did not promote colon carcinogenesis. Thus, although thermolysis of dietary casein increases colonic protein fermentation, products of this fermentation do not appear to be responsible for the promotion of colon carcinogenesis. Indeed, the results suggest that protein fermentation products do not play an important role in colon cancer promotion.

Animals↗
PubMed1995

Lack of aberrant crypt promotion and of mutagenicity in extracts of cooked casein, a colon cancer-promoting food.

Dietary casein cooked at 180 degrees C promotes the growth of aberrant crypt foci and colon cancer in rats initiated with azoxymethane. We speculated that promotion was due to a product that could be extracted by a solvent, such as 5-hydroxymethyl-2-furaldehyde (HMF), with tumor- promoting activity or the carcinogenic heterocyclic aromatic amines (HAA). This hypothesis was tested by extracting cooked casein with solvents and water. The extracts were then 1) assayed by high-performance liquid chromatography for HMF and HAA, 2) measured for mutagenicity on a frame-shift-sensitive strain of Salmonella typhimurium, and 3) fed for 100 days to azoxymethane-initiated rats to test the promoting effect on aberrant crypt foci. Data show that 1) no HMF or HAA was detected in cooked casein, 2) no mutagenicity was detected on strain TA98, with or without metabolic activation, and 3) promotion was not associated with the extracts but with the cooked casein residue. Therefore the promotion by cooked casein would not appear to be associated with a product that can be extracted by solvents.

Animals↗
PubMed1993

Characterization of human kappa-casein purified by FPLC.

Because previous purification procedures for human kappa-casein may have caused the loss of some carbohydrate, relatively gentle methods were used. The protein was isolated by a four-step procedure which included isoelectric precipitation of whole casein, gel chromatography on Sephadex G-200 in the presence of SDS, removal of the SDS with Extracti-Gel D, and FPLC chromatography on Mono Q with buffers containing 6 M urea. The purified protein was nearly identical in amino acid composition to that found earlier by amino acid analysis and peptide sequencing and a molar extinction coefficient of 11.2 +/- 0.1 was determined on the basis of amino acid analysis with a norleucine internal standard. Hydrolysis, acylation, and methylsilylation of the carbohydrate, followed by gas chromatographic analysis on a fused silica column, yielded approximately 5% fucose, 17% galactose, 18% N-acetylglucosamine, 8% N-acetylgalactosamine and 7% sialic acid, totaling almost 55% by weight. The percentages from two different donors were almost the same. About 1 mole phosphorus per mole of kappa-casein was also detected. Using low-speed sedimentation equilibrium methods, a molecular weight of only 33,400 was obtained for human kappa-casein, suggesting carbohydrate lability. Human beta-casein with four phosphoryls was stabilized against precipitation by 10 mM Ca+2 ions at a level greater than 95% when the molar ratio of kappa/beta exceeded 0.15.

Amino Acids↗
PubMed2000

Energy metabolism and thyroid hormone levels of growing rats in response to different dietary proteins--soy protein or casein.

Energy balances were measured by indirect calorimetry in four experiments on male growing rats, fed restrictively on isoenergetic and isonitrogenous (10% CP) diets based on either casein supplemented with methionine, or soy protein isolate (experiments 1, 2 and 3) and soy protein isolate supplemented with methionine (experiment 0), respectively. At the end of experiments the rats were killed for body analysis and determination of thyroid hormones and lipids in blood as well as mitochondrial respiration in liver and heart. Feeding of non-supplemented soy protein resulted in a lower efficiency of energy utilisation as well as a lower protein utilisation compared to casein-fed and supplemented soy protein-fed rats. Chemical body composition was not markedly different between the dietary groups. After long-term feeding of soy protein (experiment 3) mass and mitochondrial protein content of the interscapular brown adipose tissue were increased compared to casein-fed rats. Serum thyroid hormone levels were not changed (T3 and free T3) or were significantly lowered (T4 and free T4) following soy protein feeding in comparison with casein feeding (except for experiment 2). Cholesterol and triglycerides were decreased on an average in response to soy protein or supplemented soy protein feeding. In two of three experiments a significant lower efficiency of hepatic mitochondrial respiration with succinate as substrate, expressed by the ratio of added ADP to oxygen consumed, was observed in soy protein-fed rats compared to casein-fed rats.

Animals↗
PubMed1987

Tubulin phosphorylation by casein kinase II is similar to that found in vivo.

Purified brain tubulin subjected to an exhaustive phosphatase treatment can be rephosphorylated by casein kinase II. This phosphorylation takes place mainly on a serine residue, which has been located at the carboxy-terminal domain of the beta-subunit. Interestingly, tubulin phosphorylated by casein kinase II retains its ability to polymerize in accordance with descriptions by other authors of in vivo phosphorylated tubulin. Moreover, the V8 phosphopeptide patterns of both tubulin phosphorylated in vitro by casein kinase II and tubulin phosphorylated in vivo in N2A cells are quite similar, and different from that of tubulin phosphorylated in vitro by Ca/calmodulin-dependent kinase II. On the other hand, we have found an endogenous casein kinase II-like activity in purified brain microtubule protein that uses GTP and ATP as phosphate donors, is inhibited by heparin, and phosphorylates phosphatase-treated tubulin. Thus it appears that a casein kinase II-like activity should be considered a candidate for the observed phosphorylation of beta-tubulin in vivo in brain or neuroblastoma cells.

Animals↗
PubMed1988

A casein kinase II-related activity is involved in phosphorylation of microtubule-associated protein MAP-1B during neuroblastoma cell differentiation.

A neuroblastoma protein related to the brain microtubule-associated protein, MAP-1B, as determined by immunoprecipitation and coassembly with brain microtubules, becomes phosphorylated when N2A mouse neuroblastoma cells are induced to generate microtubule-containing neurites. To characterize the protein kinases that may be involved in this in vivo phosphorylation of MAP-1B, we have studied its in vitro phosphorylation. In brain microtubule protein, MAP-1B appears to be phosphorylated in vitro by an endogenous casein kinase II-like activity which also phosphorylates the related protein MAP-1A but scarcely phosphorylates MAP-2. A similar kinase activity has been detected in cell-free extracts of differentiating N2A cells. Using brain MAP preparations devoid of endogenous kinase activities and different purified protein kinases, we have found that MAP-1B is barely phosphorylated by cAMP-dependent protein kinase, Ca/calmodulin-dependent protein kinase, or Ca/phospholipid-dependent protein kinase whereas MAP-1B is one of the preferred substrates, together with MAP-1A, for casein kinase II. Brain MAP-1B phosphorylated in vitro by casein kinase II efficiently coassembles with microtubule proteins in the same way as in vivo phosphorylated MAP-1B from neuroblastoma cells. Furthermore, the phosphopeptide patterns of brain MAP-1B phosphorylated in vitro by either purified casein kinase II or an extract obtained from differentiating neuroblastoma cells are identical to each other and similar to that of in vivo phosphorylated neuroblastoma MAP-1B. Thus, we suggest that the observed phosphorylation of a protein identified as MAP-1B during neurite outgrowth is mainly due to the activation of a casein kinase II-related activity in differentiating neuroblastoma cells. This kinase activity, previously implicated in beta-tubulin phosphorylation (Serrano, L., J. Díaz-Nido, F. Wandosell, and J. Avila, 1987. J. Cell Biol. 105: 1731-1739), may consequently have an important role in posttranslational modifications of microtubule proteins required for neuronal differentiation.

Animals↗
PubMed1997

Physical mapping of the murine casein locus reveals the gene order as alpha-beta-gamma-epsilon-kappa.

The murine casein locus has been characterized by long-range restriction mapping and the analysis of large fragment genomic clones. Cloned sequences from five mouse casein genes (alpha, beta, gamma, epsilon, kappa) were used to screen a murine (strain 129) genomic library in a bacterial artificial chromosome vector (BAC). Of the nine clones isolated, two contained three casein genes alpha, beta, gamma and gamma, epsilon, kappa, respectively. The following combinations were found in other clones: alpha + beta, beta + gamma; and gamma + epsilon. Thus, the gene order in the locus can be deduced to be alpha-beta-gamma-epsilon-kappa. This order was confirmed by restriction analysis of the clones. A contig map of the clones and flanking sequences has been established by characterizing seven BAC clones, which together span approximately 470 kb. Long-range restriction analysis of genomic DNA indicates that the murine casein locus is confined to a 250-kb partial Xho I fragment. The alpha and beta casein genes were shown to be arranged in a tail-to-tail orientation.

Animals↗
PubMed1982

Influence of diets containing casein, soy isolate, and soy concentrate on serum cholesterol and lipoproteins in middle-aged volunteers.

Fifty-seven healthy volunteers (mean age 46 yr) were fed for 45 days on diets containing 16% of energy as protein, 35% as fat (polyunsaturated/saturated fat ratio = 0.5) and about 375 mg cholesterol/day. Of the protein in the diets 60% was provided as caseinate, as soy protein isolate, or as soy protein concentrate. After a control period of 17 days during which all the subjects received the casein diet, 17 subjects continued on this diet for the next 28 days (test period), 20 subjects switched to the soy isolate diet, and the remaining 20 subjects switched to the soy concentrate diet. Serum cholesterol levels at the end of the control period were 207 +/- 36, 205 +/- 40, and 199 +/- 35 mg/dl (mean +/- SD) for the casein, isolate, and concentrate groups, respectively. Mean changes over the test period were -2 +/- 10, -8 +/- 12, and +1 +/- 10 mg/dl, respectively. Compared with the casein diet, the isolate diet caused a small, nonsignificant decline in both serum total cholesterol and low-density lipoprotein cholesterol (-6.5 mg/dl) and an increase in high-density lipoprotein cholesterol (+5.8 mg/dl) (p less than 0.05). These effects may have been more obvious if there had been no differences between groups in weight loss. No correlation was found between the response and the initial cholesterol level. No differences in lipoprotein composition were found between the casein and soy concentrate groups. Our data suggest that soy protein preparations do not have dramatic effects on the serum total cholesterol concentration in healthy subjects. However, pure soy protein might have some beneficial effect on the distribution of cholesterol over the lipoproteins. The lack of effect of the less refined soy protein concentrate suggests that the dietary fiber and other nonprotein components of soy concentrate do not have, at least in the short-term, a favorable effect on serum cholesterol and lipoproteins in healthy adults.

Adult↗
PubMed1985

Casein content of human milk.

Three methods for estimating the casein content of human milk were tested; isoelectric precipitation with washing and correction for co-precipitating proteins, sedimentation by ultracentrifugation, and indirect analysis (ie analyzing for the content of the major whey proteins and subtracting these from the total protein content). Gel electrophoresis and amino acid analysis were used to confirm some of the results. The casein content (mg/ml) of mature human milk (n = 9) was 2.33 +/- 1.69 by isoelectric precipitation, 1.80 +/- 0.48 by sedimentation and 2.96 +/- 1.08 by the indirect approach. A probable partition of nitrogen in breast milk would be casein N: whey protein N: non-protein N of 20:50:30; ie the correct ratio of casein nitrogen: whey nitrogen is approximately 20:80. Analysis of trace elements and minerals demonstrates that of total Ca 10%, Mg 5%, Zn 28%, Cu 17%, and Fe 27% is bound to casein when prepared by ultracentrifugation while isoelectric precipitation causes a redistribution of some of these elements. Since the protein ratio of human milk is considered a guideline when manufacturing infant formulas, these findings should be considered with regard to infant nutrition.

Amino Acids↗
PubMed2004

Postprandial lipid and carbohydrate responses after the ingestion of a casein-enriched mixed meal.

BACKGROUND: Postprandial lipemia is markedly modulated when carbohydrates are added to a fatty meal. The effect of added protein is less known, however, and the data are controversial. OBJECTIVE: We investigated the effects of casein added to various fat-rich meals in the absence and presence of oligosaccharides. DESIGN: Four different test meals were given to 24 healthy volunteers: 1) fat alone, consisting of 3 g cream/kg body wt; 2) fat plus 75 g oligosaccharides; 3) fat plus 50 g sodium caseinate; and 4) a combination of all 3 components. Blood samples were taken before the meals and 1, 2, 3, 4, 5, 6, 7, and 8 h thereafter. The variables measured were serum free fatty acids, arginine, glucose, insulin, and C-peptide as well as triacylglycerol in serum, in chylomicrons, and in VLDL. Gastric emptying was monitored with the use of a (13)C breath test. RESULTS: Addition of oligosaccharides resulted in the known delay and reduction in postprandial lipemia. Casein caused additional effects: chylomicrons were further reduced and delayed, independently of gastric emptying. C-peptide and insulin, as expressed by their areas under the curves, were raised not only during the early response to the glucose load but also in the postabsorptive state. Concentrations of free fatty acids, which were markedly suppressed by 24% after oligosaccharides alone, were lowered a further 20% after the addition of casein. CONCLUSIONS: Casein added to a fatty meal lowers free fatty acids markedly in the postprandial and postabsorption phases, probably via its insulinotropic activity. Postprandial lipemia is also moderately reduced.

Adult↗
PubMed1997

Nucleotide sequence evolution at the kappa-casein locus: evidence for positive selection within the family Bovidae.

Kappa-casein is a mammalian milk protein involved in a number of important physiological processes. In the gut, the ingested protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of digestion, prevention of neonate hypersensitivity to ingested proteins, and inhibition of gastric pathogens. Variation within this peptide has significant effects associated with important traits such as milk production. The nucleotide sequences for regions of kappa-casein exon and intron four were determined for representatives of the artiodactyl family Bovidae. The pattern of nucleotide substitution in kappa-casein sequences for distantly related bovid taxa demonstrates that positive selection has accelerated their divergence at the amino acid sequence level. This selection has differentially influenced the molecular evolution of the two kappa-casein split peptides and is focused within a 34-codon region of caseinomacropeptide.

Animals↗
PubMed1977

Effect of dietary amino acids, casein, and soybean trypsin inhibitor on pancreatic protein secretion in rats.

Pancreatic enzyme output in response to various purified diets was studied in rats surgically prepared so that pancreatic secretion could be continuously collected, assayed and returned to the intestine. Intraduodenal infusion of phenylalanine and tryptophan alone did not stimulate secretion. Diets containing phenylalanine, tryptophan, a mixture of amino acids, or hydroxyzed casein, fed intragastrically, evoked a small pancreatic response that was similar to the response to a protein-free diet. intragastric infusion of a diet containing 18% casein stimulated a large initial secretion of enzyme that remained elevated throughout the 5.5 hour experiment. Addition of soybean trypsin inhibitor (SBTI) to the diet increased the pancreatic response over that due to dietary casein alone. When pancreatic juice was diverted from the intestine, the large pancreatic responses to casein or to casein + SBTI were greatly reduced and the response was similar to that of the protein-free diet.

Amino Acids↗
PubMed1980

Digestion and absorption of casein at different dietary levels in the chick: effect on fatty acid and bile acid absorption.

The site of digestion and absorption of protein was determined in chicks fed diets containing 10, 30 and 45% casein as the protein source, 3% added oil with 91Y Cl3 added as a non-absorbed reference substance. Digestion of protein to low molecular weight (MW) peptides and amino acids was rapid in all diets with major absorption occurring between duodenum and lower jejunum. Increasing the dietary casein resulted in increases in low MW peptide levels in the duodenum. This increase was disproportionate with intake when 45% casein was fed, suggesting that absorptive capacity of the duodenum was exceeded. Overall nitrogen absorption was similar in all treatments reflecting the increased participation of the ileum in nitrogen absorption when high dietary casein levels were fed. Fatty acid and bile acid absorption was depressed when 45% casein was fed, mainly due to inhibition of absorption in the ileum, presumably by binding to undigested protein.

Animals↗
PubMed1981

Intestinal transport of amino acids in protein-deficient rats and the effect of rehabilitation using a casein diet.

The effects of protein deprivation and subsequent rehabilitation on the intestinal absorption of a mixture of amino acids were studied in albino rats. The absolute amounts of amino acids transported across the intestine were greater in rats fed for 28 days 17% casein diet than those fed 3% maize protein or no-protein diets. The absorption per unit intestinal DNA (termed as absorptive capacity) of amino acids, except L-arginine in males, was more in rats fed the 3% maize protein diet than those fed the casein diet. The changes in the absorptive capacity of two sexes, when fed the protein-free diet, were not similar. The males absorbed L-arginine and L-methionine, and females L-histidine and L-tryptophan at rates faster in the protein-free group than their counterparts in the casein group. The differences between protein-free and casein groups in the absorption of L-tryptophan and L-histidine in males and L-arginine and L-methionine in females were not significant. The augmentation in absorptive capacity of intestinal cells in protein-deficient rats was a temporary adaptation to the condition that resulted in reduced intestinal cell population. Rehabilitation of protein-deficient rats for 32 days on the casein diet, resulted in an increase in intestinal cell population, return of absorptive capacity of intestinal cells to normal, and improvement in net absorption rates.

Amino Acids↗
PubMed1984

High density lipoprotein composition in rats fed casein or soy protein isolate.

We investigated the effects of dietary plant and animal proteins on high density lipoprotein (HDL) composition of rats fed diets containing either casein or soy protein isolate for 5 weeks. Rats fed casein had increased plasma total cholesterol, triglycerides, very low density and low density lipoprotein (VLDL + LDL) and HDL while HDL cholesterol was unchanged. HDL from casein-fed rats had an increase in percent protein and a decrease in percent cholesterol leading to a decreased cholesterol to protein ratio. Of the individual HDL apoproteins, only the C apoproteins were significantly elevated by casein. In addition, casein-fed rats had an increased proportion of the less sialylated forms of apo C-III. Liver cholesterol was not significantly affected by protein source but was negatively correlated with both HDL cholesterol and HDL protein levels. Addition of cholesterol to the diets largely eliminated any effect of protein source on HDL composition. These data demonstrate that dietary protein source can significantly influence HDL composition despite a lack of effect on HDL cholesterol levels.

Animals↗