Serum antibodies (measured by MRSPAH) to alcohol-soluble gliadins in adult coeliac patients

Kieffer, M; Frazier, P. J.; Daniels, N. W. R.; Ciclitira, Paul J.; Coombs, R.R.A.

doi:10.1016/0022-1759(81)90142-3

Cited by 39 publications

(15 citation statements)

References 4 publications

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“…RGP has 12.5% ground oats, 38% barley and 15% wheat middlings while CRM (for rats) has approxi mately 32% whole wheat flour and 20% barley. The tests were performed as described by Kieffer et al [1981Kieffer et al [ , 1982, In the latter paper the ELIZA procedure was used in which the antiglobulin reagent was conjugated with peroxidase. In the present investigation the antiglobulin reagents (anti-rabbit IgG, an ti-rat IgG and anti-guinea-pig IgG) were coupled to trypsin-treated sheep erythrocytes as used by Kieffer et al [ 1981 ].…”

Section: Animals and Dielsmentioning

confidence: 99%

Naturally Developing Antibodies to Wheat Gliadin Fractions and to Other Cereal Antigens in Rabbits, Rats and Guinea Pigs on Normal Laboratory Diets

Coombs

Kieffer

Fraser

et al. 1983

Int Arch Allergy Immunol

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Rabbits, rats and guinea pigs on normal laboratory diets were examined for gliadin and other cereal antibodies comparable to those found in the sera of human coeliac patients. Many of the rabbits had very high levels of gliadin antibodies. Rats showed much lower titres more comparable to the findings in normal human sera. In both these species the reactivity was directed principally against the α-gliadins. The spectrum of reactivity against the prolamines of other cereals was again comparable to that of human coeliac sera. A difference, however, was the high reactivity with maize prolamine; this was decidedly lower in sera of coeliac patients. Guinea pigs were distinctive in having relatively no serum antibodies to wheat gliadin and also minimal reactivity to the albumins, globulins and glutenins of wheat. Normal guinea pigs did, however, have antibodies to oat and maize prolamines. Following parenteral injection with total ethanol-soluble wheat gliadin, guinea pigs developed high-titred antibodies, not only to wheat gliadin fractions 1–8 (α-, β-, γ- and ω- gliadins), but also to all the cereal prolamines except those of rice. These investigations are steps in the evaluation of the role of circulating gliadin antibodies in gluten-sensitive enteropathy.

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Section: Animals and Dielsmentioning

confidence: 99%

Naturally Developing Antibodies to Wheat Gliadin Fractions and to Other Cereal Antigens in Rabbits, Rats and Guinea Pigs on Normal Laboratory Diets

Coombs

Kieffer

Fraser

et al. 1983

Int Arch Allergy Immunol

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“…This method was first introduced in 1981 when we were challenged by the difficulty of measuring gliadin antibodies in patients with coeliac disease – gliadin being considered to be the offending allergen. As the gliadins are soluble only in 70% ethanol, a feasible test procedure was not obvious, but solved by evaporating the alcoholic solution of gliadin on to the walls of the wells of plastic polystyrene microtitre plates [36] and performing a mixed reverse (solid-phase) passive antiglobulin haemagglutination (M RS PAH) reaction (fig. 3).…”

Section: The Antiglobulin Reaction Is 50 Years Oldmentioning

confidence: 99%

Historical Note: Past, Present and Future of the Antiglobulin Test

Coombs

1998

Vox Sanguinis

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This is a review of two invited talks on the antiglobulin reaction on the occasion of the 50th Anniversaries of the International Blood Group Reference Laboratory, now at Bristol, and the National Blood Service, London, and coincidentally the 51st anniversary of the antiglobulin test! The first talk (as specially requested) is a very personal reminiscence of the discovery, with Rob Race and Arthur Mourant, of the antiglobulin test in blood group serology. The second talk traces developments in antiglobulin testing in general immunology using, of course, isotype-specific antiglobulin reagents as and when they became available. Special emphasis was given to: (1) testing for poorly agglutinating bacterial antibodies; (2) special procedures for measuring reaginic (IgE) antibodies to various allergens; (3) the incorporation of an antiglobulin step or stage in many of the routine automated immunoassay procedures; (4) the special experimental procedures in the form of mixed antiglobulin reactions to reveal antibodies to the surface antigens on tissue cells, and, finally, (5) by chemically coupling antiglobulin to red blood cells, a distinctive integrated immunoassay system was developed, enabling reverse passive haemagglutination as an assay for immunoglobulins, rosetting reactions to reveal native IgG receptors on lymphocytes or antibody immunoglobulin reacting with CD marker antigens; this same reagent, namely red-cell-labelled antiglobulin, can be used to detect antibodies reacting with either bacteria or antigens adsorbed on the walls of wells of microtitre plates. The need for improved stabilization and preservation of the antiglobulin-linked red cells to prolong their ‘shelf-life’ is stressed.

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“…These measurements of specific antibody to /Mac toglobulin in the intestinal contents were amply con firmed by MrsPAH reactions using red cells labelled with Ig anti-guinea pig IgG to reveal guinea pig Ig binding to /Mactoglobulin adsorbed on multiwell microtitre plates [Kieffer et al, 1981].…”

Section: Measurement Of Antibodies To [I-lactoglobulin In the Intestimentioning

confidence: 99%

Antigenic Stimulation with Proteins of Cow’s Milk via the Oral Route in Guinea Pigs and Rats 2.

Suzuki¹,

Koritz²,

Coombs³

1987

Int Arch Allergy Immunol

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The intestinal contents of guinea pigs and rats on a milk-drinking diet were examined for mucosal-secreted antibody to β-lactoglobulin. Assay of the immunoglobulin content of duodenum, jejunum and ileum of the guinea pig gave geometric means of 70, 90 and 95 µg/ml. In the rat, where isotype-specific antiglobulin reagents were available, similar figures were obtained but it could be shown that the vast majority was IgA. Passive haemagglutination titres up to 1,000 of secreted anti-β-lactoglobulin antibody (resistant to the endogenous proteases in the intestinal contents) were measured in guinea pigs. Fifteen days after cessation of milk-drinking, the antibody had dropped to undetectable levels. No such antibody could be shown in rats. Rats also failed to develop detectable serum antibody whereas, the guinea pigs had passive haemagglutination titres in the order of 16,000.

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Serum antibodies (measured by MRSPAH) to alcohol-soluble gliadins in adult coeliac patients

Cited by 39 publications

References 4 publications

Naturally Developing Antibodies to Wheat Gliadin Fractions and to Other Cereal Antigens in Rabbits, Rats and Guinea Pigs on Normal Laboratory Diets

Naturally Developing Antibodies to Wheat Gliadin Fractions and to Other Cereal Antigens in Rabbits, Rats and Guinea Pigs on Normal Laboratory Diets

Historical Note: Past, Present and Future of the Antiglobulin Test

Antigenic Stimulation with Proteins of Cow’s Milk via the Oral Route in Guinea Pigs and Rats 2.

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