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Saudi Medical Journal Oct 2020Food containing gluten and casein could play a role in autism spectrum disorders (ASD) symptoms. The present review aimed to update the evidence about the role of the...
Food containing gluten and casein could play a role in autism spectrum disorders (ASD) symptoms. The present review aimed to update the evidence about the role of the gluten- and casein-free diet (GCFD) on the management of ASD. Web of Science, Science Direct, Google Scholar, and PubMed databases were used to search for randomized controlled trials (RCT) conducted between January 2000 and February 2020. In total, 9 RCT were included (521 participants) with age range between 2 to 18 years. Four of these studies did not show a significant improvement regarding the symptoms of ASD. The rest of these studies (n=5) showed improvement in communication, stereotyped movements, aggressiveness, language, hyperactivity, tantrums, and signs of attention deficit hyperactivity disorder compared to control group. Hence, the data remains insu cient to support the use of GCFD to improve the symptoms of ASD in children.
Topics: Adolescent; Autism Spectrum Disorder; Caseins; Child; Child, Preschool; Clinical Decision-Making; Diet, Gluten-Free; Diet, Protein-Restricted; Dietary Proteins; Female; Humans; Male
PubMed: 33026043
DOI: 10.15537/smj.2020.10.25308 -
The Journal of Nutrition May 2021Diet has been shown to play an important role in maintaining normal homeostasis in the human body. Milk and milk products are a major component of the Western diet, but...
Diet has been shown to play an important role in maintaining normal homeostasis in the human body. Milk and milk products are a major component of the Western diet, but their consumption may predispose sensitive individuals to adverse health outcomes. Current literature about milk products recognizes various bioactive components including lactate, whey protein, and β-casein protein. Specifically, cow milk has 2 major subvariants of its β-casein protein, A1 and A2, due to a single nucleotide difference that changes the codon at position 67. Whereas the A2 polymorphism is unlikely to undergo enzymatic cleavage during digestion, the A1 polymorphism is more likely to undergo enzymatic cleavage resulting in the product peptide β-casomorphin-7, a known μ-opioid receptor agonist. The objective of this article is to review the current understanding of the 2 major β-casein subvariants and their effects on various organ systems that may have an impact on the health of an individual. Synthesis of the current existing literature on this topic is relevant given the increased association of milk consumption with adverse effects in susceptible individuals resulting in a rising interest in consuming milk alternatives. We discuss the influence of the β-casein protein on the gastrointestinal system, endocrine system, nervous system, and cardiovascular system as well as its role in antioxidants and methylation. A1 milk consumption has been associated with enhanced inflammatory markers. It has also been reported to have an opioid-like response that can lead to manifestations of clinical symptoms of neurological disorders such as autism spectrum disorder. On the other hand, A2 milk consumption has been associated with beneficial effects and is easier to digest in sensitive individuals. Further research is warranted to investigate the short- and long-term effects of consumption of A1 β-casein in comparison with milk with A2 β-casein proteins.
Topics: Animals; Caseins; Cattle; Humans; Milk; Polymorphism, Genetic
PubMed: 33693747
DOI: 10.1093/jn/nxaa454 -
The Cochrane Database of Systematic... Apr 2008It has been suggested that peptides from gluten and casein may have a role in the origins of autism and that the physiology and psychology of autism might be explained... (Review)
Review
BACKGROUND
It has been suggested that peptides from gluten and casein may have a role in the origins of autism and that the physiology and psychology of autism might be explained by excessive opioid activity linked to these peptides. Research has reported abnormal levels of peptides in the urine and cerebrospinal fluid of people with autism.
OBJECTIVES
To determine the efficacy of gluten and/or casein free diets as an intervention to improve behaviour, cognitive and social functioning in individuals with autism.
SEARCH STRATEGY
The following electronic databases were searched: CENTRAL(The Cochrane Library Issue 2, 2007), MEDLINE (1966 to April 2007), PsycINFO (1971 to April 2007), EMBASE (1974 to April 2007), CINAHL (1982 to April 2007), ERIC (1965 to 2007), LILACS (1982 to April 2007), and the National Research register 2007 (Issue1). Review bibliographies were also examined to identify potential trials.
SELECTION CRITERIA
All randomised controlled trials (RCT) involving programmes which eliminated gluten, casein or both gluten and casein from the diets of individuals diagnosed with an autistic spectrum disorder.
DATA COLLECTION AND ANALYSIS
Abstracts of studies identified in searches of electronic databases were assessed to determine inclusion by two independent authors The included trials did not share common outcome measures and therefore no meta-analysis was possible. Data are presented in narrative form.
MAIN RESULTS
Two small RCTs were identified (n = 35). No meta-analysis was possible. There were only three significant treatment effects in favour of the diet intervention: overall autistic traits, mean difference (MD) = -5.60 (95% CI -9.02 to -2.18), z = 3.21, p=0.001 (Knivsberg 2002) ; social isolation, MD = -3.20 (95% CI -5.20 to 1.20), z = 3.14, p = 0.002) and overall ability to communicate and interact, MD = 1.70 (95% CI 0.50 to 2.90), z = 2.77, p = 0.006) (Knivsberg 2003). In addition three outcomes showed no significant difference between the treatment and control group and we were unable to calculate mean differences for ten outcomes because the data were skewed. No outcomes were reported for disbenefits including harms.
AUTHORS' CONCLUSIONS
Research has shown of high rates of use of complementary and alternative therapies (CAM) for children with autism including gluten and/or casein exclusion diets. Current evidence for efficacy of these diets is poor. Large scale, good quality randomised controlled trials are needed.
Topics: Autistic Disorder; Caseins; Child; Glutens; Humans; Randomized Controlled Trials as Topic
PubMed: 18425890
DOI: 10.1002/14651858.CD003498.pub3 -
Food Chemistry Jun 2020Casein-based hydrogels are biocompatible, biodegradable, renewable, easy to obtain, inexpensive, and non-toxic. They exist in different physicochemical states, e.g.... (Review)
Review
Casein-based hydrogels are biocompatible, biodegradable, renewable, easy to obtain, inexpensive, and non-toxic. They exist in different physicochemical states, e.g. particle hydrogels, which can be dived in suspensions or emulsions and macro hydrogels that are gel colloid type. These biomaterials have drawn increasing attention in recent years due to their abilities to form networks of different tensile strengths and to encapsulate, protect and release biomolecules. This mini-review outlines the recent advances in casein-based hydrogel research and the uses of casein-based hydrogels as drug delivery system for both hydrophobic and hydrophilic molecules. The food and biomedical potential along with possible future uses of the casein-based hydrogels are discussed throughout the document.
Topics: Animals; Biocompatible Materials; Caseins; Drug Delivery Systems; Food; Humans; Hydrogels
PubMed: 31951886
DOI: 10.1016/j.foodchem.2019.126063 -
Nutrients Feb 2022The use of casein glycomacropeptide (CGMP) as a protein substitute in phenylketonuria (PKU) has grown in popularity. CGMP is derived from κ casein and is a sialic-rich... (Review)
Review
The use of casein glycomacropeptide (CGMP) as a protein substitute in phenylketonuria (PKU) has grown in popularity. CGMP is derived from κ casein and is a sialic-rich glycophosphopeptide, formed by the action of chymosin during the production of cheese. It comprises 20-25% of total protein in whey products and has key biomodulatory properties. In PKU, the amino acid sequence of CGMP has been adapted by adding the amino acids histidine, leucine, methionine, tyrosine and tryptophan naturally low in CGMP. The use of CGMP compared to mono amino acids (L-AAs) as a protein substitute in the treatment of PKU promises several potential clinical benefits, although any advantage is supported only by evidence from non-PKU conditions or PKU animal models. This review examines if there is sufficient evidence to support the bioactive properties of CGMP leading to physiological benefits when compared to L-AAs in PKU, with a focus on blood phenylalanine control and stability, body composition, growth, bone density, breath odour and palatability.
Topics: Animals; Caseins; Peptide Fragments; Phenylalanine; Phenylketonurias
PubMed: 35215457
DOI: 10.3390/nu14040807 -
Topics in Current Chemistry (Cham) Aug 2017Casein is the collective name for a family of milk proteins. In bovine milk, casein comprises four peptides: α, α, β, and κ, differing in their amino acid,... (Review)
Review
Casein is the collective name for a family of milk proteins. In bovine milk, casein comprises four peptides: α, α, β, and κ, differing in their amino acid, phosphorus and carbohydrate content but similar in their amphiphilic character. Hydrophilic and hydrophobic regions of casein show block distribution in the protein chain. Casein peptides carry negative charge on their surface as a result of phosphorylation and tend to bind nanoclusters of amorphous calcium phosphate. Due to these properties, in suitable conditions, casein molecules agglomerate into spherical micelles. The high content of casein in milk (2.75 %) has made it one of the most popular proteins. Novel research techniques have improved understanding of its properties, opening up new applications. However, casein is not just a dietary protein. Its properties promise new and unexpected applications in science and the pharmaceutical and functional food industries. One example is an encapsulation of health-related substances in casein matrices. This review discusses gelation, coacervation, self-assembly and reassembly of casein peptides as means of encapsulation. We highlight information on encapsulation of health-related substances such as drugs and dietary supplements inside casein micro- and nanoparticles.
Topics: Animals; Caseins; Drug Carriers; Nanoparticles; Pharmaceutical Preparations
PubMed: 28712055
DOI: 10.1007/s41061-017-0158-z -
Journal of Dairy Science Aug 2022Milk is a primary protein source that has always played a role in mammalian health. Despite the intensification of research projects on dromedary and the knowledge of...
Milk is a primary protein source that has always played a role in mammalian health. Despite the intensification of research projects on dromedary and the knowledge of the genetic diversity at the casein loci, the genetic structure of the Tunisian camel population still needs exploration. This study sought to determine the genetic diversity of 3 casein gene variants in 5 Tunisian camel ecotypes: c.150G>T at CSN1S1 (α-casein), g.2126A>G at CSN2 (β-casein), and g.1029T>C at CSN3 (κ-casein). The obtained results were compared with data published on Sudanese and Nigerian camels to establish the level of differentiation within and between populations. A total of 159 blood samples were collected from 5 Tunisian camel ecotypes and the extracted DNA was genotyped by PCR-RFLP. A streamlined genotyping protocol was also developed for CSN3. Results indicated that allele T was quite rare (0.06) at CSN1S1 for all ecotypes. Minor allele frequency was found for G (0.462) in CSN2 except for Ardhaoui Medenine ecotype who deviated from the average CSN2 allele frequency of the total population. Allele C showed minor allele frequency of 0.384 in CSN3. Among the Tunisian population, GAT (0.343) was the most represented haplotype in all ecotypes except for Ardhaoui Medenine, where GGC (0.322) was the most frequent one. Significant differences in heterozygosity and local inbreeding were observed across the Tunisian, Sudanese, and Nigerian populations, although the global fixation index indicated that only 2.2% of the genetic variance is related to ecotype differences. Instead, phylogenetic analysis revealed a closer link between the Tunisian and Sudanese populations through a clade subdivision with 3 main branches among the ecotypes. This study represents the first attempt to understand casein gene variability in Tunisian camels; with further study, milk traits and genetic differentiation among populations can be associated with the history of camel domestication.
Topics: Animals; Camelus; Caseins; Milk; Nigeria; Phylogeny
PubMed: 35840403
DOI: 10.3168/jds.2022-22081 -
Molecules (Basel, Switzerland) Jan 2021Casein and whey being food supplements have been considered to be used in oral health care products. However, the response of oral cells to micellar casein and whey...
Casein and whey being food supplements have been considered to be used in oral health care products. However, the response of oral cells to micellar casein and whey powder remains unclear. Considering that milk contains the growth factor TGF-β, and lactoperoxidase was recently reported to decrease the expression of inhibitor of DNA-binding (ID) proteins, there is a rationale to assume that casein and whey can also provoke these responses in oral cells. To examine the TGF-β activity, gingival fibroblasts were exposed to reconstituted casein and whey powder from food supplement before the expression of TGF-β target genes were analyzed by reverse transcription-quantitative polymerase chain reaction. Immunoassays were performed for interleukin11 (IL11) in the cell culture supernatant and for TGF-β in the reconstituted casein and whey. We blocked TGF-β by neutralizing the antibody and the TGF-β receptor type I kinase with the inhibitor SB431542. We also showed smad3 phosphorylation and smad2/3 nuclear translocation by Western blot and immunostaining, respectively. Moreover, with reconstituted casein and whey powder, ID1 and ID3 expression analysis was evaluated in HSC2 human oral squamous carcinoma cells. We report here that casein and whey powder caused a robust increase of TGF-β target genes interleukin11 (IL11), NADPH oxidase 4 (NOX4) and proteoglycan4 (PRG4) in gingival fibroblasts that was blocked by SB431542 and the neutralizing antibody. Moreover, casein and whey powder increased the phosphorylation of smad3 and nuclear translocation of smad2/3. No changes of proliferation markers Ki67 and cyclinD1 were observed. Furthermore, reconstituted casein and whey powder decreased ID1 and ID3 expression in the HSC2 oral squamous carcinoma cells. These findings suggest that the processing of milk into casein and whey powder maintains the TGF-β activity and its capacity to regulate ID1 and ID3 genes in oral fibroblasts and oral squamous carcinoma cells, respectively. These data increase the scientific knowledge on the biological activity of casein and whey with a special emphasis on oral health.
Topics: Animals; Caseins; Cell Line; Fibroblasts; Gene Expression Regulation; Gingiva; Inhibitor of Differentiation Proteins; Micelles; Powders; Transforming Growth Factor beta; Whey
PubMed: 33477984
DOI: 10.3390/molecules26020507 -
Food Research International (Ottawa,... Apr 2022The kinetics of binding of calcium ions in molar excess to individual caseins and casein ingredients was studied in pH 6.4 aqueous solutions using stopped-flow...
The kinetics of binding of calcium ions in molar excess to individual caseins and casein ingredients was studied in pH 6.4 aqueous solutions using stopped-flow absorption spectroscopy. An initial second-order reaction, faster for β-casein than for α-casein due to lower energy of activation (ΔE = 8.2 kJ∙mol; ΔE = 18.1 kJ∙mol, respectively), is followed by a slower first-order reaction with similar energies of activation (ΔE = 25.3 kJ∙mol and ΔE = 20.7 kJ∙mol) as determined from temperature dependence of rate between 25 °C and 50 °C. Sodium caseinate reacts faster with calcium than both α-casein and β-casein in the first reaction of the two consecutive reactions, while the rate of the second falls between α-casein and β-casein. Global spectral analysis showed the UV-visible spectra of the reaction intermediates of the caseins to be more similar to the final products than to the initial casein reactants. Dynamic and static light scattering indicated decreasing particle sizes and increasing particle surface upon calcium-binding most significantly at low temperatures. The calcium binding to casein was found endothermic by isothermal titration calorimetry. Calcium binding seems to be controlled by enthalpy/entropy compensation corresponding to an isoequilibrium temperature of 38 °C in agreement with binding of calcium to o-phosphoserine rather than to aspartate or glutamate side chains of the caseins. Binding capacity and affinity for calcium to α-casein and sodium caseinate both increased with increasing temperature in agreement with the endothermic nature of the binding. Decreasing enthalpy of binding for each calcium indicating a decrease in heat capacity of the caseins upon calcium-binding. The small difference between binding enthalpy and energy of activation for association of calcium to α-casein lead to the conclusion that calcium dissociation goes through an early transition state. The rate of calcium dissociation hardly depends on temperature also explaining why calcium binding to caseins is important for calcium bioaccessibility.
Topics: Calcium; Caseins; Micelles; Temperature; Thermodynamics
PubMed: 35337555
DOI: 10.1016/j.foodres.2022.110981 -
Molecules (Basel, Switzerland) Aug 2021Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular...
Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10 L/mol (298 K), 6.17 × 10 L/mol (305 K) and 5.73 × 10 L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 10 L/mol at 298 K, 3.90 × 10 L/mol at 305 K and 3.41 × 10 L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (-7.53 kcal/mol) was lower than that at pH 7.4 (-7.01 kcal/mol). The molecular dynamics simulation study showed that the binding energy (-131.07 kJ/mol) of β-casein-curcumin complex was relatively low at pH 2.0 and 298 K. α-Helix content in β-casein was decreased and random coil content was increased in the presence of curcumin. These results can promote a deep understanding of interaction between curcumin and β-casein and provide a reference for improving the bioavailability of curcumin.
Topics: Caseins; Curcumin; Hydrogen Bonding; Hydrogen-Ion Concentration; Imaging, Three-Dimensional; Molecular Docking Simulation; Molecular Dynamics Simulation; Protein Binding; Protein Structure, Secondary; Spectrum Analysis; Structural Homology, Protein; Thermodynamics
PubMed: 34443680
DOI: 10.3390/molecules26165092