BACKGROUND: About 70-80% of children with cow's milk allergy (CMA) become outgrown clinically by the age of 3 years. Casein, one of the three major cow's milk proteins (casein, beta-lactoglobulin (BLG), alpha-lactoalbumin (ALA) ) has been reported to play an important role in the persistence of CMA. The aim of this study was to determine different effects of causative milk proteins on the persistence of CMA between two age groups. METHODS: A total of 65 patients with CMA were enrolled in this study. Their cow's milk-specific IgEs were positive ( 0.7 U/ml by Pharmacia CAP). After dividing 65 patients into two age groups, under the age of 3 years and over 3 years (persistent CMA), we compared the levels of casein-, BLG- and ALA-specific IgE antibodies between the two groups. RESULTS: There were 44 patients in the group of less than 3 years of age and 21 patients in the group of more than 3 years of age. The concentrations of the specific IgE antibodies to casein, BLG and ALA were not significantly different between the two groups. However, although statistically insignificant, those more than 3 years of age had higher mean values of casein-specific IgE antibodies and lower mean values of whey protein (BLG and ALA) - specific IgE antibodies compared with those less than 3 years of age. A single dominant allergenic milk protein was not identified within either of the two age groups, but the con centrations of the casein-specific IgE antibodies in children with more than 3 years of age tended to be higher than those of whey protein-specific IgE antibodies. CONCLUSION: Although statistically insignificant, the concentrations of the casein-specific IgE antibodies were higher in the group of more than 3 years of age than in the younger group. Moreover, the concentrations of the casein-specific IgE antibodies in children more than 3 years of age tended to be higher than those of whey proteins. These findings implicate that casein plays a certain role in the persistence of CMA.
Antibodies ; Caseins ; Child* ; Humans ; Immunoglobulin E* ; Lactoglobulins ; Milk Hypersensitivity* ; Milk Proteins ; Milk* ; Whey Proteins

Milk proteins are composed of casein, further classified into αS1-casein, αS2-casein, β-casein, and κ-casein, and whey protein, which is separated into α-lacatalbumin, β-lactoglobulin, serum albumin, and some minor proteins, such as lactoferrin and immunoglobulin. To reduce the allergenicity of protein, heat treatment and enzymatic protein hydrolysis by endopeptidase are necessarily required. Additionally, membrane technology should be applied to produce a protein hydrolyzate, which has consistent molecular weight of peptide and low in free amino acid without allergenic peptide or protein. Extensive casein hydrolyzate and whey protein hydrolyzate are used for protein source of mainly extensively hydrolyzed protein formula (eHF) intended for the treatment of cow's milk allergy. Also, partially hydrolyzed formula (pHF) is developed, which is using a single protein source e.g., whey protein hydrolyzate. The allergenicity of infant formula can be determined according to molecular weight profile and antigenicity reduction compared to intact protein. More than 90% peptides are present in eHF have a molecular weight of <3,000 Da. Peptide molecular weight profiles of pHF range mainly between 3,000 and 10,000 Da, but have a small percentage of >10,000 Da. Generally, antigenicity reduction in eHF and pHF is 10-6 and 10-3, respectively. Even if protein hydrolyzate is manufactured under strict quality control, there is still a risk of cross contamination of allergenic milk components through environmental conditions and the shared manufacturing process. Thus, quality assessment of protein hydrolyzate formula must be performed routinely.
Caseins ; Hot Temperature ; Humans ; Hydrolysis ; Immunoglobulins ; Infant Formula* ; Infant* ; Lactoferrin ; Membranes ; Milk ; Milk Hypersensitivity ; Milk Proteins ; Molecular Weight ; Peptides ; Quality Control ; Serum Albumin ; Whey Proteins

PURPOSE: Cow's milk protein is one of the most common and strongest food allergen. We investigated the effects of heat treatment on the distribution and antigenicities of major allergens from cow's milk. We also compared the protein distribution and antigenicities among cow's milk formula and its substitutes. METHODS: We heated alpha-casen, beta-lactoglobulin (BLG), alpha-lactalbumin (ALA), and crude extract of cow's milk in 100degrees C boiling water for 1 hour. We prepared crude extracts from cow's milk formula, partially hydrolyzed milk formula (pHF) and extensively hydrolyzed milk formula (eHF). The protein compositions of all the samples were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The antigenicities were determined by IgE immunoblotting with pooled serum collected from 11 patients with milk allergy. RESULTS: After heating, no significant alteration was found in casein, and the aggregates of ALA and BLG were detected with molecular weights of about 30 and 45 kDa, respectively. The antigenicities of newly detected aggregates were increased. The new aggregates of BLG with increased antigenicities were also found in heated milk total protein. Major milk allergens were not found in pHF, and residual components with a molecular weight below 10 KDa did not show IgE-binding activity. We failed to observe the residual components and antigenicities of eHF. CONCLUSION: Changes in protein distribution and antigenicity of milk total protein induced by heat treatment may not be significantly different from those of each major allergen. The residual components of pHF could have little IgE-binding capacity, and there may be few or no antigenic components in eHF.
Allergens ; Caseins ; Complex Mixtures ; Electrophoresis ; Heating ; Hot Temperature* ; Humans ; Hydrolysis* ; Immunoblotting ; Immunoglobulin E ; Lactalbumin ; Lactoglobulins ; Milk ; Milk Hypersensitivity ; Milk Proteins* ; Molecular Weight ; Sodium ; Water

OBJECTIVETo examine the effects of the whey basic protein on bone metabolism of Sprague-Dawley (SD) rats and healthy mid-aged women.

METHODSForty-four female SD rats were randomized by weight into four groups of eleven rats each and fed 10 mg x kg BW(-1) x d(-1), 20 mg x kg BW(-1) x d(-1), 30 mg x kg BW(-1) x d(-1) of whey basic protein and control diet was given respectively by intragastrically injection for 90 days. Bone mineral density of femur was measured by dual-energy X-ray absorptiometry in vitro. Sixty-three health women [(37.9 +/- 4.3) years old] were randomly assigned to treatment with placebo, 30 mg whey basic protein per day or 60 mg whey basic protein per day for 24 weeks. The bone mineral density (BMD) of the lumbar vertebrae L2-LA, femoral neck and right calcaneus of each subject were measured by dual-energy X-ray absorptiometry (DXA) at 0 and the 24th week of treatment. Serum bone specific alkaline phosphatase and N-telopeptide (NTX) were measured at 0 and the 14th week.

RESULTSThe mean BMD value of the distal end of the femur in 10 mg x kg BW(-1) x d(-1) whey basic protein group was significantly higher than that of the control group at the end of the trail. But after treatment by doses of whey basic protein used in the study, there were no differences between the control group and others groups on bone mineral density in the human trail.

CONCLUSIONWhey basic protein should enhance the bone mineral density of the rats' femur and no obvious effect was detected in the human trail.

Adult ; Animals ; Bone Density ; drug effects ; Female ; Food, Formulated ; Humans ; Lactalbumin ; pharmacology ; Milk ; Milk Proteins ; pharmacology ; Rats ; Rats, Sprague-Dawley ; Whey Proteins

Whey protein concentrate (WPC 80) and sodium caseinate were hydrolyzed by Protamex to 5%, 10%, 15%, and 20% degree of hydrolysis (DH). WPC 80, sodium caseinate and their hydrolysates were then analyzed, compared and evaluated for their nutritional qualities. Their chemical composition, protein solubility, amino acid composition, essential amino acid index (EAA index), biological value (BV), nutritional index (NI), chemical score, enzymic protein efficiency ratio (E-PER) and in vitro protein digestibility (IVPD) were determined. The results indicated that the enzymatic hydrolysis of WPC 80 and sodium caseinate by Protamex improved the solubility and IVPD of their hydrolysates. WPC 80, sodium caseinate and their hydrolysates were high-quality proteins and had a surplus of essential amino acids compared with the FAO/WHO/UNU (1985) reference standard. The nutritive value of WPC 80 and its hydrolysates was superior to that of sodium caseinate and its hydrolysates as indicated by some nutritional parameters such as the amino acid composition, chemical score, EAA index and predicted BV. However, the E-PER was lower for the WPC hydrolysates as compared to unhydrolyzed WPC 80 but sodium caseinate and its hydrolysates did not differ significantly. The nutritional qualities of WPC 80, sodium caseinate and their hydrolysates were good and make them appropriate for food formulations or as nutritional supplements.
Amino Acids ; chemistry ; Caseins ; chemistry ; metabolism ; Dietary Proteins ; analysis ; Evaluation Studies as Topic ; Hydrolysis ; Milk Proteins ; chemistry ; metabolism ; Models, Statistical ; Nutritive Value ; Protein Hydrolysates ; chemistry ; Solubility ; Temperature ; Time Factors ; Tryptophan ; chemistry ; Whey Proteins

Hemo-Q (R) and Albumax (R) solution are widely used antianemics. Hemo-Q (R) contains cow's milk protein (casein) and Albumax (R) contains egg white protein (ovalbumin). Cow's milk protein and egg protein can cause common allergic diseases in infants and young children. We reported two cases of young children with milk and egg allergy who presented skin symptoms after ingestion or cutaneous contact with Hemo-Q (R) or Albumax (R) solution. When Hemo-Q (R) or Albumax (R) solution was taken or rubbed on, erythematous papules and wheals were developed in 10-20 minutes, but other antianemics which don't contain milk or egg protein contents didn't show skin manifestations.
Caseins ; Child ; Eating ; Egg Hypersensitivity ; Egg White* ; Food Hypersensitivity ; Humans ; Infant ; Milk Proteins* ; Milk* ; Ovalbumin ; Ovum* ; Skin ; Skin Manifestations ; Urticaria*

No abstract available.
Child* ; Humans ; Immunoglobulins ; Infant, Newborn* ; Lactoglobulins ; Milk Proteins* ; Milk* ; Mothers* ; Postpartum Period*

PURPOSE: Soy-based formulas are widely used as dairy substitutes to treat milk allergy patients. However, reactions to soy have been reported in a small proportion of patients with IgE-mediated milk allergies. The aim of this work was to explore whether P34, a mayor soybean allergen, is involved in this cross-reactivity. METHODS: In vitro recognition of P34 was evaluated by immunoblotting, competitive ELISA and basophil activation tests (BAT) using sera from allergic patients. In vivo cross-reactivity was examined using an IgE-mediated milk allergy mouse model. RESULTS: P34 was recognized by IgE antibodies from the sera of milk allergic patients, casein-specific monoclonal antibodies, and sera from milk-allergic mice. Spleen cells from sensitized mice incubated with milk, soy or P34 secreted IL-5 and IL-13, while IFN-gamma remained unchanged. In addition, the cutaneous test was positive with cow's milk proteins (CMP) and P34 in the milk allergy mouse model. Moreover, milk-sensitized mice developed immediate symptoms following sublingual exposure to P34. CONCLUSIONS: Our results demonstrate that P34 shares epitopes with bovine casein, which is responsible for inducing hypersensitivity symptoms in milk allergic mice. This is the first report of the in vivo cross-allergenicity of P34.
Animals ; Antibodies ; Antibodies, Monoclonal ; Basophils ; Caseins* ; Enzyme-Linked Immunosorbent Assay ; Epitopes ; Food Hypersensitivity ; Humans ; Hypersensitivity ; Immunoblotting ; Immunoglobulin E ; Interleukin-13 ; Interleukin-5 ; Mice ; Milk ; Milk Hypersensitivity ; Milk Proteins ; Soy Milk ; Soybeans* ; Spleen

This study focused on the contamination mechanism and regeneration strategies of sulfopropyl ion exchange resin (SP Sepharose FF) during the separation of recombinant human lactoferrin from transgenic bovine milk. We analyzed primary constituents' contents in chromatorgraphic material and fractions. The results showed that the lipid in milk can clog the column or adhere to the resin through hydrophobic interaction, leading to an increase in column pressure. Some casein molecules were found to adsorb onto the resin through electrostatic interaction, therefore the adsorption capacity was decreased. There was no direct interaction between lactose and the resin in the chromatorgraphic process. Increased continuous chromatographic cycles and prolonged time interval between protein purification and column regeneration could enhance the undesirable interaction between the contaminants and resin, thus lowering the regeneration efficiency. NaOH was found to be effective in the removal of lipid and casein molecules from the column. Furthermore, normal microstructure and chromatographic performance of the ion exchanger was recovered after this cleaning procedure.
Adsorption ; Animals ; Animals, Genetically Modified ; genetics ; metabolism ; Caseins ; chemistry ; Cattle ; Chromatography, Ion Exchange ; methods ; Female ; Humans ; Ion Exchange Resins ; chemistry ; Lactoferrin ; biosynthesis ; genetics ; isolation & purification ; Mammary Glands, Animal ; metabolism ; Milk ; chemistry ; Milk Proteins ; isolation & purification ; metabolism ; Recombinant Proteins ; biosynthesis ; genetics ; isolation & purification ; Sodium Hydroxide ; chemistry

PURPOSE: Despite most epidemiologic studies reporting that an increase in milk intake affects the growth of prostate cancer, the results of experimental studies are not consistent. In this study, we investigated the proliferation of prostate cancer cells treated with casein, the main protein in milk. MATERIALS AND METHODS: Prostate cancer cells (LNCaP and PC3), lung cancer cells (A459), stomach cancer cells (SNU484), breast cancer cells (MCF7), immortalized human embryonic kidney cells (HEK293), and immortalized normal prostate cells (RWPE1) were treated with either 0.1 or 1 mg/mL of alpha-casein and total casein extracted from bovine milk. Treatments were carried out in serum-free media for 72 hours. The proliferation of each cell line was evaluated by an 3-(4,5-Dimethyl-thiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) assay. RESULTS: alpha-Casein and total casein did not affect the proliferations of RWPE1, HEK293, A459, SNU484, MCF7, HEK293, or RWPE1 cells. However, PC3 cells treated with 1 mg/mL of alpha-casein and casein showed increased proliferation (228% and 166%, respectively), and the proliferation of LNCaP cells was also enhanced by 134% and 142%, respectively. The proliferation mechanism of alpha-casein in PC3 and LNCaP cells did not appear to be related to the induction of Insulin-like growth factor-1 (IGF-1), since the level of IGF-1 did not change upon the supplementation of casein. CONCLUSIONS: The milk protein, casein, promotes the proliferation of prostate cancer cells such as PC3 and LNCaP.
Breast Neoplasms ; Caseins* ; Cell Line ; Cell Proliferation ; Culture Media, Serum-Free ; Humans ; Insulin-Like Growth Factor I ; Kidney ; Lung Neoplasms ; Milk ; Milk Proteins* ; Prostate ; Prostatic Neoplasms* ; Stomach Neoplasms