The Consequences Of Cheese As A Main Source Of Protein

[Amazoniac]

For those that have missed, here's a summary of what has been discussed so far that might help making casein work better (it's clearly beyond replenishing what has been refined). I forgot two that were added later:

Creatine, magnesium;
Niacin, choline(, perhaps pantothenic acid);
B12, carotenes (papayas with the benefit of papain), vit E;
[Travo's] bromelaid from pineapfels;
Molybdenum, manganese; (tyw, 2016?)
B6, folate (low doses);
Gelatin, taurine, vitamin C;
Straight glutathione;
Fermentable carbs;
Zinc, selenium, iodine;
Potassium acetate/citrate.

Then, if those don't work:
Digestive enzymes;
Betaine HCl;
Thyroid hormones.

 

[Amazoniac]

I'm with burtlan and Travo on this: A1-dominant casein tends to be more problematic and Raj is being generous in overlooking what has been publicized about it. If someone has access to alternatives, by all means try them to know if they're more digestible for you. But then we have a great deal of people who don't have access to those and are after a clean source of protein, often in a position of having to choose between a sub-optimal protein ingestion or going for the casein in question. In this situation, a robust body should make the benefits outweight the potential adverse effects, if not eliminating them altogether.

An attempt to boycott it is unnecessary since as soon as people have the option to choose between a more and a less digestible casein, the change will happen naturally.

There are people on those therapeutic diets that refrain from troubling foods for a while, get stronger, improve digestion, the intestines heal and they later add the problematic foods without issues, living happy forever with daily aerial heel click.

But it's another factor to watch for when casein is the main source of protein.


Fermentation must help:
Degradation of food-derived opioid peptides by bifidobacteria

I remember someone posting about adding lemon juice to yogurt to sterilize it. If people are going to be adding supplemental vitamins, it might be better to add them topically or with other meals to avoid potential problems in this regard.

Gelatin was mentioned. People that are interested on this thread are likely trying to shoot at some troubles regarding casein consumption. If the issue is not related to missing nutrients but to problems with protein, adding collagen to the same meal can complicate things. It might be better to consider including it on different meals.
The content of glycine in the diet by itself can dictate how increases in protein consumption affects people, and its lack might make casein not work properly. The more concentrated in protein is the dairy, the more likely it is to increase its need.

 

[Amazoniac]

Degradation of food-derived opioid peptides by bifidobacteria

Cocoa Positively Modulates The Gut Microbe And Lowers TLRs And Inflammation

You can find recipes for cottage cheese and (yellow?) bell pepper, which has an inhibitory effect on cholinesterase and it might help to get things going initially. It should also replace lactose to some degree and aid in such acidification, but I suspect it has to be raw. It must be a Terma-approved combination.

But if the craving isn't there, I guess it just doesn't work.

 

[Amazoniac]

Below is an improved graph. Now including more amino acids, gelatin was added, and the values are even more precise.

Spoiler

They're still for more or less:

• 2 containers (2x 6 oz)- Generic greek yogurt
• 2 containers (SAMe)- Fage
• 340 g - Cottage cheese
• 200 g - Pot cheese
• 150 g - Atlantic cod
• 110 g - Chicken breast
• 120 g - Beef steak
• 40 g - Gelatin (typical serving is usually 10-12 g)

Spoiler: With values included

Cheeses and yogurts have a disappointing glycine to methionine ratio in relation to meats. One more factor to consider when a lot is consumed.

Spoiler: Gly/Met ratio

• 00.9 - Generic greek yogurt
• 00.9 - Fage
• 00.8 - Cottage cheese
• 00.4 - Pot cheese
• 01.6 - Atlantic cod
• 01.8 - Chicken breast
• 01.8 - Beef steak
• 31.5 - Gelatin

--
Dairy protein is not intended to be consumed without fermentable carbs. I don't know for sure how it compares to meats, but if it's more anabolic than them, it should require more nutrition. Those carbs not only might encourage growth of desirable bacteria and prevent some problems with casein (post above), but during fermentation they can provide extra B-vitamins. This can be decisive for someone to tolerate casein decently.

--
Can I Live Off Of Milk And Orange Juice Alone? (it's found in whey, not sure how much greek yogurts conserve)

 

[Amazoniac]

I had to modify it because the values for gelatin provided by Cron-o-meter were suspicious. This time I used Great Lakes'.

Spoiler: Amino acid composition of proteins

They're still for more or less:

• 2 containers (2x 6 oz) - Generic greek yogurt
• 2 containers (SAMe) - Fage
• 340 g - Cottage cheese
• 200 g - Pot cheese
• 150 g - Atlantic cod
• 110 g - Chicken breast
• 120 g - Beef steak
• 40 g - Gelatin (typical serving is usually 10-12 g)

Spoiler: With values included

Spoiler: Updated and ranked Gly/Met ratio

• 00.4 - Pot cheese
• 00.8 - Cottage cheese
  
• 00.9 - Fage
  
• 00.9 - Generic greek yogurt
• 01.6 - Atlantic cod
• 01.8 - Chicken breast
• 01.8 - Beef steak
• 29.0 - Gelatin

 

[Lolinaa]

@Amazoniac: so what do you advice to always have cheese with fruits or jam? I do eat liver every Sunday or Saturday. I might add a bit complex though. Do you recommend any brand? Right now at home I have thiamine, riboflavine, niacinamide and biotin. Each individually. I might just take them like on Wednesday or Thursday to prevent lack of b vitamins.

 

[Amazoniac]

@Amazoniac: so what do you advice to always have cheese with fruits or jam? I do eat liver every Sunday or Saturday. I might add a bit complex though. Do you recommend any brand? Right now at home I have thiamine, riboflavine, niacinamide and biotin. Each individually. I might just take them like on Wednesday or Thursday to prevent lack of b vitamins.

People can eat cheeses and yogurts in surprising ways, not limiting you to pair them with fruits. This thread has less relevance for someone that consumes them sparingly. If you consume them often, I find it's still wrong to tell you what to eat; it's best to correct what diet isn't providing through supplementation. In terms of compensation for processing losses, it's more supportive when nutrients are provided with the meal.

B-vitamins function better when all are present, but individual needs will require adjustment, and in some cases some might be left out.

Casein is also intented by nature to be consumed with fat-soluble vitamins, removing the fat can have undesirable effects. Many fruits provide some carotenes: not all them are enough to make a difference for someone who is in great debt, but they're usually enough to replenish what was lost when milk was processed. I don't know how much vit K whole milk has per gram of casein, but some fruits should provide equivalent amounts.

I have the impression that people who eat a more natural diet tend to find sodium chloride less appealing as the fructose content of a meal increases (same for the other way around). Eating concentrated protein such as cheeses and strained yogurts with fruits too often can leave you without sufficient sodium chloride intake.

 

[Lolinaa]

Thank you Amazoniac for a detailed response and the reference to the French dish aligot .
To be honest I try to eat more and more peaty. I buy and eat less and less food he doesn’t recommend and I do take thyroid as well. While I do apply his principles mainly, I listen more to my body too as my guidance. The more I do that, the more wisely I use supplements and the better I feel.0
The two supplements I take everyday with the weather getting colder and less sunny are vit K and d. 1 drop of 5000d from healthnatura on my feet and 1 drop of k.

 

[Amazoniac]

Although it's possible to make casein work, it can require a lot management, so it should be obvious at this point that there's more to the story than just missing nutrients. Even though this review had a focus on fetuses, I think the information is still practical for us.

Generalizing that 'it's not you, it's dairy' can be wrong, but so can the opposite.

Once again the following quote is relevant:

I do not want to make the mistake Winston Churchill expressed so clearly: "Men occasionally stumble over the Truth, but most pick themselves up and hurry off as if nothing had happened."

Just ignore if you feel great on dairy protein, but definitely don't if you have signs that you're already on fire, weakened (these can leave you as susceptible as an infant, if not more) or perhaps if casein is your major source of protein for concentrating it in an unusual way.


Casein: A Milk Protein with Diverse Biologic Consequences

"The digestion of bovine casein in cattle is intimately linked to the action of gastric rennet (rennin) on the a and K fractions. Rennet, at a low pH, promotes the formation of an irreversible curd. In contrast, while acidification of casein causes precipitation, this process is reversible upon alkalinization. Thus, in the absence of rennet a true curd is not formed (21). The purpose of curd formation is to slowly release casein into the small bowel where it is rapidly digested. Human milk does not contain a-casein and the human stomach is not known to secrete rennet. Thus, following consumption of bovine milk or casein by humans, curd formation is absent although a precipitate is formed. It is therefore possible that casein may then be delivered to the small bowel in quantities that may exceed the digestive process that is designed for human milk."

"Casein not digested in the stomach or the first portion of the small intestine may pass more distally and has been found in the ileum and colon of babies with necrotizing enterocolitis requiring surgical excision of the intestine (28). In the presence of an adequate source of carbohydrate, casein may be partly degraded and utilized by the colonic flora and yield ammonia, free peptides, and volatile fatty acids (29). The primary organic acids produced are acetic, propionic, butyric, and isovaleric acids (30). During intestinal transit, casein is less effective than either soy protein or egg albumin in stimulating the release of pancreatic carboxypeptidases A and B (31). It also binds to bile acids, limiting their capacity to solubilize fatty acids (32). Divalent cations preferentially complex to the casein micelle or bind to its phosphoseryl residues as phosphopeptides (33, 34). Although calcium, a constituent of the casein micelle, and iron have been most studied, zinc, magnesium, and manganese have also been found to bind to casein, thus potentially limiting their bioavailability (33-37)."

"Numerous metabolic effects have been associated with casein-predominant diets. Babies fed a casein-predominant formula have higher levels of blood urea nitrogen, phenylalanine, methionine tyrosine, and ammonia (39-41). They also have a lower serum pH (late metabolic acidosis) and lower levels of taurine and cystine (39-4 1). The aminograms of preterm newborn babies fed a whey-predominant formula more closely resemble the aminograms of breast-fed infants (41)."

"One measure of the protein quality of milk proteins involves determination of the protein efficiency ratio (PER) or the amount of weight gain divided by the amount of protein eaten. Although simple to perform, PER are not sensitive to small differences in protein quality and the number generated has no intrinsic meaning beyond its use for comparative purposes. In general, the whey fraction of cow’s milk generates higher PER than the casein fraction due to the higher percentages of essential amino acids and, in particular, cystine and threonine (6). Compared with the nonadjusted PER of cow milk (3.6), the casein (3.3) fraction is consistently lower than the average for whey (3.8), which summates the individual contributions of plactoglobulin (3.5) and a-lactalbumin (4.0) (6). These values agree with the nonadjusted PER values of 2.80 for casein and 3.4 for whey protein provided by the National Dairy Council."

"Low birthweight infants appear to be uniquely vulnerable to distortions of the amino acid profile associated with casein-predominant feedings. Raiha et al. (41) fed 106 low birthweight infants whey-predominant versus casein-predominant (cow milk) formulas varying in protein content of 1.5 or 3.0 g/100 ml of formula. Blood ammonia concentration was relatively elevated in the casein groups along with a more frequent, severe, and prolonged state of metabolic acidosis. Metabolic acidosis and failure to thrive have also been reported in formulas containing 100% casein hydrolysate. Healy (45) observed that infants receiving Nutramigen (a casein hydrolysate) developed metabolic acidosis and weight loss that was corrected by the addition of a base solution or the substitution of another formula. Shenai et al. (46) also observed that casein-predominant formulas increased the risk of metabolic acidosis in low birthweight infants, although casein predominant and whey predominant achieved similar nitrogen retention."

Failure of Dietary-Casein-Induced Acidosis to Explain the Hypercholesterolemia of Casein-Fed Rabbits | The Journal of Nutrition | Oxford Academic​

"Imbalances in plasma amino acid levels may influence the transport of neurotransmitter precursors into the brain (47). Hence, the elevated levels of tyrosine and phenylalanine seen in the casein-dominant formulas may affect or modify catecholamine levels in the brain resulting from increased substrate availability. The elevated levels of threonine commonly seen in whey-predominant formulas (47, 48) do not have known neurotoxicity and/or act as neurotransmitter precursors. Tyrosine and phenylalanine have been shown to be highly neurotoxic when fed to rats in excess of daily requirements, whereas threonine was the least neurotoxic amino acid. Similarly, threonine is only moderately toxic in terms of growth suppression if fed to rats; tyrosine and phenylalanine caused more severe growth depression (49)."

"Whey and casein proteins differ in binding affinities and release of certain cations, e.g. calcium, manganese, magnesium, zinc, and iron, during digestion. Bovine b-casein (25-35% of total casein) exists in a fully phosphorylated form containing four to five phosphate groups per molecule versus the much lower phosphorylation (zero to five) of human casein (52). This probably accounts for the great binding of magnesium, iron, copper, and zinc in the bovine versus human casein micelle (8). These authors note that the casein in cow’s milk may not be completely digested due to the low digestion capacity of the newborn. The casein in human milk, found in much lower quantities, is structurally different, forms a relatively soft or nonexistent curd, and binds mineral to a lesser extent, all of which may help account for the high solubility and bioavailability of mineral in human milk."

"Using the suckling rat pup model, Lonnerdal (53) demonstrated a depressant effect of casein on zinc absorption. Casey et al. (54) also noted a significantly depressed plasma zinc response in adult females consuming a casein-predominant formula. An even lower plasma response was obtained with a 100% casein hydrolysate formula. A similar effect of casein is also evident in primates; in infant rhesus monkeys, zinc absorption is lower when they are fed casein-predominant compared with whey-predominant formulas (55). Singh et al. (56) were concerned that the relatively high zinc-binding capacity and poorer digestibility of casein could lead to complexing and loss of this essential nutrient. In their experiments, the enzymatic dephosphorylation of casein with acid phosphatases markedly reduced, but did not eliminate, zinc binding. Although whey may also bind zinc, a substantial portion of zinc is trapped with colloidal calcium phosphate."

"Cow’s milk casein binds a large proportion of iron, zinc, and copper due to phosphorylated amino acid residues on a- and b-casein and the large intrinsic potential for exogenous mineral affinities (53). Hegenauer et al. (57) observed the ability of the casein micelle to bind iron when added to cow’s milk. Lonnerdal et al. (58) extrinsically labeled 54Mn and found that 71% of manganese is in breast milk whey (lactofemn) versus 67% in cow milk casein."

"The caseins have numerous interactions with bacteria from the mouth to anus. Bovine casein (milk phosphoprotein) can be incorporated into dental plaque and prevents enamel subsurface demineralization (61). It does not produce a significant change in the quantity or composition of plaque bacteria but rather increases the plaque calcium phosphate content. Furthermore, its buffering capacity attenuates calcium leaching associated with organic acid production by plaque bacteria (61)."

"Casein may indirectly affect bacterial growth. The attenuation of salmonellae growth that is associated with cow’s milk acidification can be reversed by the addition of casein in a dose-dependent manner (63). Five percent cocoa powder in a nutrient broth is bactericidal to the salmonellae but the addition of 5% bovine casein to this broth neutralizes this bactericidal effect (62). A 1:1 molar ratio of casein to cocoa powder allows for uninhibited salmonellae growth."
@Salmonamb (..coincidences.)

"Casein may also interfere with neutrophil function. The phagocytosis of Staphylococcus aureus by milk leukocytes was impaired in a manner that can be directly attributed to the casein content of milk (64). Immunofluorescence studies reveal that both milk neutrophils and blood neutrophils, when incubated in milk, absorb casein on the cell surface and that casein is also ingested by the neutrophil. In addition, the combination of fat and casein inhibits both the phagocytosis and intracellular killing of S. aureus by neutrophils (65)."

"The production of b-lactamase by Enterobacter cloacae is enhanced by casein derivatives in the presence of glycine (66). Casein digests and hydrolysates induce accelerated carbohydrate fermentation in enteric gram-negative rods by inducing the lactose operon and increasing b-galactosidase activity (67). This results in more rapid fermentation of carbohydrate to organic acids, which may then lower intraluminal pH. This has been proposed as an important component in the initiation of neonatal necrotizing enterocolitis (neonatal inflammatory bowel disease) (68). Lifschitz et al. (69) in a recent report provided evidence that cow’s milk formulas may accelerate carbohydrate fermentation by intestinal flora in healthy term infants. Breast-fed infants have a significantly slower rate of carbohydrate fermentation to organic acids than formula-fed infants. The profile of organic acid production differed between the two groups; formula-fed infants produce considerably more propionate whereas breast-fed infants produce more homolactate. These diet-related differences in the way infants’ bowels respond to colonic substrate (carbohydrate) loading may explain why acute gastroenteritis in breast-fed infants tends to be less severe than in formula-fed infants. As neonatal necrotizing enterocolitis is more evident in formula-fed infants, these alterations in carbohydrate fermentation by intestinal flora may then set the stage for the devastating form of intestinal inflammation-neonatal necrotizing enterocolitis."

"Bovine casein enhances the shift of fluid into the bowel in response to enterotoxins produced by colonic flora (70, 7 1). In rabbit intestine, bovine a-casein promoted a 90% increase in intestinal loop fluid accumulation to cholera enterotoxin, whereas whey proteins attenuate this response (71). In contrast to the synergism seen with bovine casein, human casein decreased the intestinal fluid response to cholera enterotoxin by more than 25%. An intact bovine casein structure is necessary for this potentiation of the cholera toxin effect. b-Casomorphins, potent opioid peptides formed during casein digestion, partially block the secretory effect of cholera toxin (72). Murine and bovine casein are able to bind the heat-stable enterotoxin of enterotoxigenic Escherichia coli. The binding is pH dependent with 75% of the toxin bound to casein at pH 2.3 and 7.4% bound at pH 10.1. The binding of the toxin does not destroy its biologic activity. Consequently upon casein digestion, the active toxin, bound by casein in the stomach, may be released in the lower gastrointestinal tract (73)."

"Casein has considerable proinflammatory characteristics. Unlike the whey proteins (albumin, immunoglobulins, and lactoferrin) which do not cause adverse reactions when administered systemically, parenteral administration of casein can cause extensive cellular injury. Caseins, primarily a- and b-casein, are chemotactic for leukocytes (74, 75). This can be demonstrated in Boyden chambers or in vivo where casein administration into the peritoneal cavity is a standard technique for harvesting peripheral neutrophils of experimental animals (76, 77). Casein not only promotes leukocyte migration but it induces the activity and release of phospholipase A2 (77, 78), thereby promoting arachidonic acid metabolism by both cyclo-oxygenase and lipoxygenase pathways in neutrophils and neighboring cells. Casein also stimulates the activity of 5-lipoxygenase, the enzyme responsible for the formation of leukotrienes (79). These lipoxygenase products (e.g., LTB4, LTC4, and LTD4) may exacerbate the inflammatory response through additional cellular activation and recruitment, as well as modulating local vascular tone and permeability (80, 81)."

"Casein-induced activation of neutrophils and monocytes also leads to increased formation of inflammatory cytokines. Recently, Goto et al. (82) described increased release and formation (mRNA expression) of interleukin 1b by peritoneal neutrophils, lymphocytes, and macrophages harvested after casein administration."

"The mechanism by which casein elicits a chemotactic response is still unclear but it requires an intact structure as casein hydrolysates are not chemotactic (83). There is potential for some biologically active fragments of casein to modify leukocyte function. u and k opioid receptor agonists inhibit human granulocyte chemotaxis to agents like casein, raising the possibility that b-casomorphins, potent preceptor agonists derived from casein (84, 85), oppose the actions of intact casein. Fragments of human casein have been reported to stimulate the phagocytic activity of human monocytes (86, 87)."

"The binding characteristics of casein include cell specificity. Casein binds primarily to neutrophils, although some binding to monocytes and lymphocytes is demonstrable; binding to erythrocytes is negligible (74). It is worth noting that the limited chemotactic activity of other proteins, e.g., serum albumin, increases upon denaturing, when their tightly folded structure unravels and assumes a structure which is more comparable to monomeric casein (83)."

"Local inflammation of the intestine in the form of mucosal damage, edema, lymphatic dilation, exaggerated release of histamine, LTB4, PGE2, 6-keto PGF1a, and TXB2 is characteristic of a model of necrotizing enterocolitis (NEC) initiated by a luminal solution of acidified casein (89, 90). This model reproduces the intraluminal biochemistry of infants with NEC. While damage may be elicited by combination of any protein with organic acids, the greatest damage is induced by casein (68). Low intraluminal pH, as a result of carbohydrate fermentation by enteric flora, can increase epithelial permeability (91). The resultant access of luminal casein to mucosal defenses initiates a local inflammatory response and cellular necrosis. Anaerobic isolates taken from the bowel of infants with NEC greatly increase their rate of carbohydrate fermentation when exposed to tryptone, a pancreatic digest of casein (67, 92). The active moiety appears to be a di- or tripeptide."

"Casein alone or in combination with bacterial toxins has been implicated in the neutropenia associated with NEC, which is the result of neutrophil activation and not a depletion of bone marrow stores (76). Under these circumstances, activated neutrophils “stick” to the vascular wall and/or migrate into tissue sites, thereby decreasing circulating number. The link between bovine casein and NEC is also supported by data demonstrating that NEC is associated with enteral feeding, particularly aggressive feeding patterns (93) and especially with cow’s milk formula versus human milk (94). As premature infants have an epithelial barrier that may be easily compromised, NEC may represent a devastating form of feeding-induced inflammation of the bowel."

"Adult inflammatory bowel disease (ulcerative colitis, Crohn’s disease) has an unknown etiology. Increased levels of serum antibodies to cow’s milk proteins, including casein, bovine serum albumin, b-lactoglobulin, and a-lactalbumin, are associated with adult inflammatory bowel disease (95)."

"As intestinal permeability is enhanced with inflammatory bowel disease, [] antibody responses are suggestive of an increased uptake of macromolecules secondary to bowel damage. Thus, it is possible that when the epithelial barrier is compromised, undigested or partly digested milk proteins have access to mucosal defenses which may promote further mucosal damage or retard the healing process."

"[..]it is now recognized that soy proteins are as antigenic as bovine milk proteins (99-101)."

"A recent study by Walker-Smith et al. (102) noted that children with cow milk-sensitive enteropathy improved when switched to formulas based on hydrolysates of either casein or whey. However, infants on a whey hydrolysate formula tended to gain more weight. After whey hydrolysate feeding, the small intestinal mucosa showed a significant improvement in mucosal thickness and villus height, whereas after casein hydrolysate feeding intestinal architecture did not improve."

"Casein has a lower molecular weight than the majority of whey proteins, which may facilitate its passage across the epithelial barrier. This is supported by the observation that antibody titers tend to be higher to casein than individual whey proteins. Of the whey proteins, b-lactoglobulin and a-lactalbumin possess molecular weights comparable to casein and are also implicated in milk protein allergy (103, 104). Since casein can directly activate inflammatory and immune cells (i.e., without antibody recognition), circulatory titers of antibody classes to casein may not be predictive of its deleterious effects, particularly in the gastrointestinal tract."

"The sensitivity of some infants to bovine casein is extraordinary. There are reports of anaphylactic reaction to casein from such unexpected sources as diaper rash ointment (105) and breast milk (106). In the latter report, the infants’ adverse reactions to breast milk ceased when the mother stopped consuming cow’s milk, indicating that intact casein or another cow’s milk protein or at least their antigenic fragments were absorbed in the mother’s gut, transported to, and secreted or released into breast milk in sufficient quantities to elicit anaphylaxis in the infant."

"The immaturity of the gut’s epithelial bamer in infants (100) and the strong association of bovine milk consumption with iron-deficiency anemia (107), occult gastrointestinal bleeding (108-110), cataracts (111), and the various manifestations of food allergy (112, 113) have raised sufficient concern among pediatricians that some advocate that intact bovine milk should be totally avoided in infants (114)."

"Diet appears to play a major role in the development of spontaneous autoimmune diseases in animals. For example, rabbits fed cow’s milk develop joint lesions akin to early rheumatoid arthritis (115). This response is characterized by increased numbers of nucleated cells and increased percentages of T lymphocytes in synovial fluid in a manner consistent with the severity of the joint lesions. Rabbits drinking cow’s milk develop high titers of serum and synovial fluid C1q-binding activity (116). However, these values did not correlate with the degree of damage and there was no evidence of glomerulonephritis, suggesting that deposition of immune complexes is not a key event. The precise mechanism underlying this effect of cow’s milk, and presumably casein, remains unresolved."

"Casein appears to augment murine systemic lupus erythematosus, as mice fed a casein-free diet display increased longevity, lower anti-DNA antibodies, and decreased immunoreactants in glomeruli (117). As with rabbit rheumatoid arthritis, the mechanisms for this deleterious effect of bovine casein are unknown. Casein-fed mice display compromised humoral immunity (118); specifically, splenocytes exhibited a marked suppression of their antibody response to the T-dependent antigen, sheep red blood cells, and the T-independent antigen, dinitrophenyl-Ficoll."

"In contrast to casein, dietary whey proteins appear to be immunoenhancing, as evidenced by plaque-forming cell response to sheep red blood cells (119); an effect not evident with casein or soy protein. The immunoenhancing properties of dietary whey relative to casein were also confirmed in dimethylhydrazine-induced colon carcinogenesis in A/J mice (119a). Dietary whey increased three-fold the number of plaque-forming cells in the spleen and reduced the incidence and size of tumors induced by dimethylhydrazine, although body weight curves were comparable in whey- and casein-fed groups."

"Rats fed casein-predominant diets die 13.5% sooner than rats fed a comparable soy diet, primarily from chronic nephropathy (120). Similarly, increasing the casein content in the diets of mice (CBL/65) is associated with decreased longevity (121), whereas diet enriched lactalbumin, a whey protein, is associated with increased longevity in Syrian hamsters (122). The renal stress associated with reduced renal mass, which mimics reduced glomerular reserve, also is exacerbated by a diet of 24% casein. This diet is associated with more proteinuria, greater effective renal plasma flow and glomerular filtration rate, greater blood urea and serum cholesterol, reduced survival, and more extensive histological damage and renal hypertrophy than rats fed a 24% soy protein diet (123, 124). It has been well understood that low protein diets can retard renal damage due to reduced renal mass or glomerular number (125), but these results demonstrate that the form of protein is also important. Casein in particular appears to overtax compromised kidneys, causing greater morbidity and mortality."
@ecstatichamster @yerrag

"Casein promotes atherosclerotic disease experimentally and may have similar effects in humans (126, 127). The mechanisms by which this occurs are not clear. However, casein is associated with hypercholesterolemia, decreased binding of b very low-density lipoprotein to hepatic receptors and a diminished very low-density lipoprotein catabolism (127-130). Experimentally, casein appears to enhance the intestinal absorption of cholesterol (131, 132). Although casein does not interfere with the biliary efflux of steroids and bile acids, this increased cholesterol absorption is linked to diminished bile acid excretion. Casein also directly binds bile acids, disturbing the micellular solubilization of fatty acids by bile acids, prior to their absorption (133). This effect was not observed with elemental diets, which may account for their effectiveness in the treatment of patients with steatorrhea."

"There are marked species differences in the hypercholesterolemic effect of dietary casein. The rabbit appears to be particularly susceptible; in rabbits dietary casein can establish atherosclerosis in cholesterol-free diets. The rat requires both cholesterol and casein feeding in order to elicit marked hypercholesterolemia. This may be due to the marked differences between the rat and rabbit in their ability to regulate low-density lipoprotein receptor activity. Alternative suggestions are that the rabbit, in contrast to rat and man, has low levels of intestinal phosphatase and more glycine conjugation of bile acids. Casein is highly phosphorylated, and, in the rabbit, intact casein or phosphopeptide fragments will interfere with the binding of insoluble calcium phosphate to bile acids. As a result more bile acids, and hence more cholesterol, are absorbed and less excreted (126, 132, 134). The relatively lower sensitivity of the rat to casein may also be due to the extraordinary capacity of rats to metabolize casein in the stomach, with negligible intact casein entering the duodenum to affect bile acid absorption (135-137)."

"Supplementation of fish meal diets with tyrosine elevated serum cholesterol in rats to a level similar to casein-fed rats (casein is particularly rich in tyrosine), suggesting that tyrosine may also contribute to the hypercholesterolemic effects of casein (138). Generally, reports indicate that intact casein is more effective."

"Does casein have similar effects in primates and in particular, humans? Rhesus monkeys alternatively fed diets of soy protein or casein for 13 to 17 weeks consistently displayed elevations of serum cholesterol with casein diets, mostly due to elevated low-density lipoprotein (131). Manipulation of dietary protein alone with low cholesterol diets was reported not to elevate serum cholesterol in humans (1 39). However, the same authors, in a follow-up cross-over design study, demonstrated that normolipidemic subjects consuming 500 mg/day of cholesterol and a 20% casein diet exhibited a 10% higher concentration level of low-density lipoprotein cholesterol and a 10% lower concentration of high-density lipoprotein cholesterol ( 140). Thus, casein may adversely alter serum lipoproteins in normal humans, but relative to species like the rabbit, it is only evident if dietary cholesterol is also raised. However, educational programs continue to focus on the fat content of dairy products, ignoring the potential contributions of casein on the development of atherosclerosis and the other disease states which might be adversely influenced by casein."

"There is growing appreciation that the biologic effects of casein may be mediated by fragments [such as the casomorphins] generated during digestion or directly administered in the form of acidic or enzymic hydrolysates (Table III). Reported effects of these fragments are diverse, encompassing immunomodulation, inflammation, opioid effects, metabolic, endocrine, as well as modification of gut flora and function. In some instances the structure of the biologically active products is known. Little is known about the generation of these products during digestion, their bioavailability and metabolism, their interactions with other components in the diet as well as species differences in generation, handling, and responsiveness. Although food has been often jokingly referred to as a drug, there is now sufficient evidence to ponder hormone or drug-like actions of some foods. For example, does the warm cup of milk that aids the induction of sleep act via the generation of potent opioids like b-casomorphin? A recent report noted that b-casomorphin administered intraperitoneally enhances the time spent in quiet sleep (141). This effect can be reversed by the opiate antagonist, naloxone, and is consistent with the calming effect of milk on the newborn."
@Travis

"Of all of the fragments of casein which may act as food hormones, b-casomorphins are the best characterized. An excellent review of this growing field has been recently published by Hamosh et al. (142). Briefly, b-casomorphins are a class of opioid peptides generated from bovine or human b-casein, which are structurally distinct from the endogenous opioids, endorphins, or enkephalins. b-Casomorphins act via the u receptor; they are of seven amino acids in length or less. They are generated from b-casein; those from bovine casein are more potent than b-casomorphins from human milk (143, 144). Similar opioid agonists called exorphins may also be generated during the digestion of the wheat protein, gluten (145, 146)."

"The b-casomorphin structure is resistant to degradation by gastric and pancreatic enzymes (149). Following milk consumption, b-casomorphins have been detected in the intestinal contents (150, 151); this can be duplicated in vitro by replication of the digestive process (152)."

"b-casomorphins are effective agonists when directly applied to the serosal surface (158), where they can stimulate electrolyte absorption and inhibit intestinal propulsion (159). The latter effect is primarily due to a reduction in periodicity rather than the amplitude of peristaltic waves (160), effects which are similar to other opioid agonists used in the treatment of diarrhea (157). b-Casomorphins have also been found to negate the secretory effects of cholera toxin (73)."

"Although the gastrointestinal tract is likely to be the major target organ of b-casomorphins, there is considerable evidence suggesting that other organs may be involved. Ingestion of milk, casein hydrolysates, or casomorphins have been reported to increase the release of somatostatin (161) and pancreatic polypeptide (162), impair cardiac glycogen stores, and stimulate insulin release (163-165). Hamosh et al. (142) proposed that the higher incidence of obesity in bottle-fed children may be related to the generation of the more potent bovine b-casomorphins, as endogenous opiates are important regulators of food intake (166)."

"The central nervous system is also a potential target. b-Casomorphins have been detected in the cerebral spinal fluid of lactating women where they may affect mood (167). In newborns the gastrointestinal tract is more permeable (168) and may allow an increased uptake of b-casomorphins. This may lead to respiratory depression (169) and has prompted some suggestions that sudden infant death syndrome may be related to the effects of casomorphins (170). Premature infants are often susceptible to irregular respiratory and cardiac reflexes and their immature gastrointestinal barrier may lead to a higher rate of absorption of casomorphins and other casein-derived products."

"Research by Jolles and co-workers (85, 171, 172) has demonstrated that a number of fragments obtained from enzymic digests of human casein possess immunostimulatory properties, as evidenced by a stimulation of opsonized sheep erythrocyte phagocytosis by murine peritoneal macrophages and in vivo killing of Klebsiella pneumoniae. The biologically active fragments include a hexapeptide and two tripeptides and are derived from human casein. There is no convincing evidence that digests of bovine casein contain comparable compounds. Rather, there is evidence reviewed above that bovine casein may be associated with immunosuppression, or at least a deleterious modification of immune-related diseases. Thus, while casein has been proposed as a prohormone with an immunomodulatory role, particularly in the newborn (173), we need to define the importance of potential differences in the source of casein (bovine versus human) as well as the effects of specific fragments."

"Jolles et al. (174) have also compared blood clotting and curd formation and noted that there is a strong functional and structural analogy between fibrinogen and k-casein. Furthermore, an undecapeptide derived from k-casein inhibits ADP-induced platelet aggregation and fibrinogen binding to ADP-treated platelets (175). This undecapaptide was related to a dodecapeptide C-terminal fragment of human fibrinogen. Thus, it appears that blood clotting and curd formation have similar mechanisms and potentially share biologic ancestry."

"Infant formulas which are based on protein hydrolysates are potentially a rich source for biologically active fragments. In addition to the casomorphins, it has been reported that casein hydrolysate formulas contain high levels of histidyl-L-proline diketopiperazine. This compound was recovered in the urine of infants only when they were fed these formulas (176); similar findings have been reported in the urine of phenylketonurics receiving Lophenalac (177). Histidyl-L-proline diketopiperazine may have marked effects on the central nervous system. It is produced endogenously as a metabolite of thyrotropin-releasing hormone (178) and may affect thermoregulation, prolactin release, natriuresis, as well as cause depression of the central nervous system through opioid-like activities (179-181). This compound is also found endogenously in the gastrointestinal tract of the rat (182)."

"Casein and casein digests affect bacterial function and growth (66, 70, 73, 92, 182) as discussed above. The gastrointestinal system may be particularly susceptible to compromise because it is exposed to high concentrations of casein and the modification of gut flora simultaneously."

"Henrique et al. (183) have demonstrated that a tryptic digest of bovine a-casein potentiated the proinflammatory and musculotropic responses to bradykinin. Although this factor(s) inhibited kininase II activity, the full response was not solely due to inhibition of the degrading enzyme kininase II alone, as the effects were two- to three-fold greater in magnitude than those observed with captopril or enalapril, potent inhibitors of kininase II (angiotensin-converting enzyme). As bradykinin is a potent proinflammatory agent implicated in inflammatory bowel disease (184), it is possible that bovine casein or its tryptic hydrolysates could exacerbate intestinal inflammation through bradykinin-dependent mechanisms."

"The consequences of bovine milk consumption are diverse, some of which are potentially deleterious. Although certain cultures shun cow’s milk or milk-based products, Western societies consume large quantities of cow’s milk. Although there are stronger similarities between bovine whey proteins and human whey proteins, the quantity and nature of casein in cow’s milk differ markedly from human milk. We propose that the consequences of diets based on bovine casein should be more closely evaluated and certainly expanded beyond the simplistic approach of growth. What is good for the goose may be good for the gander, but what is good for the cow could be harmful to the human."​

You can't complain about the pink color, this time it helped to avoid monotony (nice).

Whey (quite nutritious) with gelatin can be an alternative.

 

[ecstatichamster]

Thank you @Amazoniac

 

[paymanz]

, zinc, magnesium, and manganese have also been found to bind to casein, thus potentially limiting their bioavailability (33-37)."

that is bad

 

[Lolinaa]

Thank you @Amazoniac. Wow, I think I will consume less milk and cheese now.

 

[Amazoniac]

Thank you @Amazoniac. Wow, I think I will consume less milk and cheese now.

It's up to you. As long as you replace what you're excluding, there should be no problem.

 

[Nighteyes]

Interesting. I certainly feel better without cheese from cow milk. I still dont understand if points above may be attributable to goat/sheep casein? The opioid Effects are less but there are many other points above regarding digestion and acidification...

 

[Lolinaa]

@Nighteyes: its about cows milk only in the post.

 

[paymanz]

but for casein in order to bind to minerals and prevent their absorption it must be intact right? if you digest it into amino acids it could not binf them anymore. and casein has good digestibility i believe.

but need researching more.

 

[paymanz]

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[InChristAlone]

About casein causing high cholesterol and atherosclerosis I will have to come back to this after I get my blood labs in the next couple weeks as I eat quite a lot of cheese.

 

[Travis]

"Jolles et al. (174) have also compared blood clotting and curd formation and noted that there is a strong functional and structural analogy between fibrinogen and k-casein. Furthermore, an undecapeptide derived from κ-casein inhibits ADP-induced platelet aggregation and fibrinogen binding to ADP-treated platelets (175). This undecapaptide was related to a dodecapeptide C-terminal fragment of human fibrinogen. Thus, it appears that blood clotting and curd formation have similar mechanisms and potentially share biologic ancestry."

This interesting, and κ-casein could be the biochemical mechanism for casein-induced atherosclerosis. The single serum factor most correlated with atherosclerosis is lipoprotein(a), most commonly found in the LDL fraction yet not routinely looked-for. Lipoprotein(a) is very similar to plasminogen (63.8%), having multiple near-identical lysine-binding kringle domains that ostensibly bind to frayed collagen on the vascular wall. This protein is not correlated with any other common risk factor, yet according to Linus Pauling it is induced in vitamin C deficiency. It could also be worth noting that the only animal species known to produce Lp(a) are primates, guinea pigs, and the fruit bat—or those that have lost the ability to synthesize vitamin C. Lipoprotein(a) appears to have the function of strengthening arterial walls under low vitamin C states, which do need to be fortified due to the concomitant low collagen turnover. Vitamin C is necessary for physically-hydroxylating proline and lysine into hydroxyproline and hydroxylysine, respectively, making it intuitive why vitamin C increases procollagen synthesis fourfold (at 100 μM).

 

[InChristAlone]

Yes, hoping my heart is good despite lots of dairy and fat consumption as I get a lot of vitamin C.