Serum antibodies against native, processed and digested cow's milk proteins in children with cow's milk protein intolerance

Fällström, S. P.; Ahlstedt, S.; Carlsson, B.; Lönnerdal, Bo; La, Hank

doi:10.1111/j.1365-2222.1986.tb01976.x

Cited by 29 publications

(12 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The antigenicity (Fallstrom et al 1986;Gortler and Urbanek 1990;Leary, Jr. 1992;Wahn et al 1992) and immunogenicity (Stephan et al 1990;Cordle et al 1991) of protein hydrolysates and milk proteins (Wahn et al 1981) have recently been studied in animal and human models. These studies demonstrated a decreasing antigenicity with the increasing degree of hydrolysis due to the reduction of epitopes.…”

Section: Discussionmentioning

confidence: 99%

Antigenicity for Humans of Cow Milk Caseins, Casein Hydrolysate and Casein Hydrolysate Fractions

Nentwich¹,

Szépfalusi²,

Kunz³

et al. 2004

Acta Vet. Brno

View full text Add to dashboard Cite

Nentwich I., Szépfalusi Zs., Kunz C., Spuergin P., Urbanek R.: Antigenicity for Humans of Cow Milk Caseins, Casein Hydrolysate and Casein Hydrolysate Fractions. Acta Vet. Brno 2004, 73: 291-298. Cow milk casein consists of several fractions each of which have different structure and differing antigenicity. The aim of the study was to investigate the capacity of cow milk casein, casein fractions, casein hydrolysate and its fractions to bind human IgG antibodies (antigenicity).Whole cow milk, bovine casein, α-casein native and dephosphorylated, β-and κ-casein, further a casein hydrolysate and its fractions were incubated in a IgG-ELISA assay with sera from five patients with cow milk intolerance and a pooled control serum from milk drinking healthy individuals.In healthy controls, predominantly β-caseins, both commercial and chromatographically separated, contained the strongest antigenic epitopes. In milk intolerant infants, however, κ -casein along with β-caseins was the strongest antigen. The antigenicity of the casein hydrolysate compared to nonhydrolysed casein was reduced down to 18.5 and 41.8% measured with patient and control sera, respectively. There were traces of intact protein in the hydrolysate. Antigenicity of the casein hydrolysate fractions reached only 24 to 44% of the antigenicity of the whole hydrolysate. Although their antigenicity roughly correlated with their molecular weight, only negligible differences among particular fractions were found.Cow milk beta-casein is the strongest antigen in healthy controls while kappa-casein possesses the high antigenicity in the milk intolerant individuals. For milk intolerant individuals, the tested casein hydrolysate was approximately 5 times less antigenic compared to whole casein. Antigenicity of the hydrolysate fractions were lower than that of the whole hydrolysate. Identification of cow milk caseins and its fractions with the highest bindnig capacity for human IgG antibodies is important for manufacturing of antigen-reduced formulas based on casein hydrolysates.

show abstract

Section: Discussionmentioning

confidence: 99%

Antigenicity for Humans of Cow Milk Caseins, Casein Hydrolysate and Casein Hydrolysate Fractions

Nentwich¹,

Szépfalusi²,

Kunz³

et al. 2004

Acta Vet. Brno

View full text Add to dashboard Cite

show abstract

“…IgE antibodies, which were evident in sera from most patients with allergy to hen's egg white but not from healthy subjects, play a major role in food hypersensitivity reactions, especially immediate type (type I) of allergic re action within the intestinal tract [24], In contrast, IgG and IgA antibodies to foods have been found in both foodallergic subjects [13,14] and healthy children [25]. Evi dence for involvement of IgG and IgA classes of immu noglobulin in food sensitivity reactions is much less con vincing.…”

Section: Discussionmentioning

confidence: 99%

“…The IgE, IgG and IgA class antibodies for OVA have been shown to exist in sera from patients with allergy [13,14]. RAST inhibition test demonstrated that allergenic epitopes are mainly determined by primary structure and OVA peptides 1-10 and 323-339 encompass allergenic epi topes, which are recognized by IgE antibodies from pa tients with allergy to hen's egg white [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Specificities of IgE, IgG and IgA Antibodies to Ovalbumin

Honma

Kohno²,

Saito³

et al. 1994

Int Arch Allergy Immunol

View full text Add to dashboard Cite

We studied the binding activities of IgE, IgG and IgA antibodies in patients with allergy to hen’s egg white against two different ovalbumin (OVA) preparations, which were physically or chemically denatured OVA and enzyme-digested OVA fragments. The binding activities of IgE antibodies to these OVA preparations with those of IgG or IgA antibodies were compared. It was found that the binding activities of IgE antibodies to denatured OVA by treatment with dithiothreitol, urea or hydrochloric acid were similar to those of IgG or IgA antibodies. In contrast, the binding activities of IgE antibodies to heat-denatured OVA or by treatment with sodium hydroxide at pH 11.0 were different from those of IgG or IgA antibodies to these denatured OVA. Furthermore, we found that the binding activities of anti-OVA antibodies in sera from patients with allergy to hen’s egg white against fragmented OVA were different between IgE antibodies and IgG or IgA antibodies. Thus, it can be concluded that IgE antibodies to OVA in sera from patients with allergy to egg white differ from IgG or IgA antibodies in respect to binding activities against different preparations of denatured or fragmented OVA, probably due to differences in fine specificities of these antibodies against OVA.

show abstract

“…This is probably a physiological phenomenon, as most exposed individuals have low levels of antibodies in serum against cow's milk proteins, including b -lactoglobulin, as well as cereal proteins such as gliadin [2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Avidity progression of dietary antibodies in healthy and coeliac children

Saalman

Dahlgren

Fällström

et al. 2003

Clinical and Experimental Immunology

View full text Add to dashboard Cite

SUMMARYIn most individuals minute amounts of food proteins pass undegraded across the intestinal mucosa and trigger antibody formation. Children with coeliac disease have enhanced antibody production against gliadin as well as other dietary antigens, e.g. b -lactoglobulin, in cow's milk. Antibody avidity, i.e. the binding strength between antibody and antigen, often increases during antibody responses and may be related to the biological effectiveness of antibodies. The aim of the present study was to determine the avidity of serum IgG antibodies against b -lactoglobulin and gliadin in healthy children during early childhood and compare these avidities to those found in children with coeliac disease. The average antibody avidity was analysed using a thiocyanate elution assay, whereas the antibody activity of the corresponding sera was assayed by ELISA. The avidity of serum IgG antibodies against b -lactoglobulin as well as gliadin increased with age in healthy children, even in the face of falling antibody titres to the same antigens. Children with untreated coeliac disease had IgG anti-b -lactoglobulin antibodies of significantly higher avidity than healthy children of the same age, and the same trend was observed for IgG antigliadin antibodies. The present data suggest that the avidities of antibodies against dietary antigens increase progressively during early childhood, and that this process seems to be accelerated during active coeliac disease.

show abstract

Serum antibodies against native, processed and digested cow's milk proteins in children with cow's milk protein intolerance

Cited by 29 publications

References 13 publications

Antigenicity for Humans of Cow Milk Caseins, Casein Hydrolysate and Casein Hydrolysate Fractions

Antigenicity for Humans of Cow Milk Caseins, Casein Hydrolysate and Casein Hydrolysate Fractions

Specificities of IgE, IgG and IgA Antibodies to Ovalbumin

Avidity progression of dietary antibodies in healthy and coeliac children

Contact Info

Product

Resources

About