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BM180, a novel 180-kDa basement membrane protein enriched in guanidine-HCl extracts of lacrimal and parotid exocrine secretory glands, was immunopurified using the secretion inhibitory monoclonal antibody 3E12. The N-terminal amino acid sequence was found to be VRVPVPQLQPQNP. An identical sequence comprises the N-terminus of the wheat storage protein alpha-gliadin. The presence of a gliadin-like protein in basement membranes was confirmed using a monoclonal and several polyclonal anti-gliadin antibodies, the former of which detected a 180-kDa protein in basement membrane blots. A full-length alpha-gliadin cDNA was found to hybridize at high stringency with mouse and human genomic DNA; and in lacrimal gland Northern blots with a 2.3-kb message. Since BM180 appears to be required for stimulus-secretion coupling by lacrimal acinar cells, circulating anti-alpha-gliadin antibodies associated with Sjögren's syndrome ('Dry Eye') and more commonly in Coeliac disease, may be secretion inhibitory.

Microsporum canis NCPF 179 and M. canis NCPF 177 dermatophyte cytoplasmic extracts (DCEs) were used as antigens to generate monoclonal antibodies (mAbs). Hybridomas with supernatants of optical density (OD) > 1 for homologous dermatophyte cytoplasmic extracts (CE) and OD

SUMMARY A case of fatal systemic Weber-Christian disease is described. In vitro immunological function and lipoprotein measurements are presented with a subsequent discussion on the possible aetiology of the condition.

Peripheral-blood lymphocytes from patients with cœliac disease showed a marked increase in D.N.A. synthesis after incubation in vitro with a subfraction of gluten. Lymphocytes from control patients showed no increased D.N.A. synthesis under the same conditions. The possible use of this specific lymphocyte-stimulation assay as a screening test for cœliac disease is discussed.

Previous studies have suggested that, apart from IgE-mediated reactions, some of the symptoms of food allergy may be caused by IgG antibodies to food proteins. This study was carried out to see if there were any distinctive features of the IgG sub-class antibody response to dietary antigens which occurs in food allergic patients. IgG sub-class antibodies were measured using a quantitative enzyme-linked immuno-sorbent assay (ELISA) to wheat gliadin, ovalbumin and bovine casein in twenty patients who had coeliac disease and in twenty-eight egg allergic patients. These were compared with twenty-one atopic dermatitis patients who did not have food allergy and twenty-six healthy control subjects. Coeliac disease patients tended to have raised IgG antibody levels (especially IgG1) to all three antigens but these overlapped considerably with that seen in egg allergic and atopic dermatitis patients. Coeliacs who avoided gluten had anti-gliadin antibody levels which did not differ from those seen in healthy subjects but nevertheless had raised anti-ovalbumin and casein-specific antibodies. The IgG antibody was largely restricted to IgG1 and IgG4 sub-class although the relative amount of each varied with the antigen. Although gliadin-specific antibodies were mainly IgG1, ovalbumin-specific antibodies were mainly IgG4. The increased antibody levels to all three antigens in coeliacs were caused by a raised IgG1 response, IgG4 antibodies were usually normal. Egg allergic patients also had raised IgG1 but not IgG4 antibodies to ovalbumin. These data show that the response to different dietary antigens can vary with the antigen. The fact that IgG1 and not IgG4 antibodies were raised to all three antigens in patients with coeliac disease suggests that they are a secondary consequence of the disease, perhaps reflecting increased transport of antigens across a damaged gut mucosa rather than a specific immunopathological reaction. However, the observation that antibodies to gliadin, and not ovalbumin or casein, fell following gluten avoidance shows that the response to gliadin, at least, is dependent upon continued exposure to antigen.

Gliadin antibodies of different immunoglobulin classes may be measured very satisfactorily by M RS PAH (mixed reverse (solid phase) passive antiglobulin haemadsorption) using an alcoholic solution of gliadin proteins in a microtitre plate test. We report the antibody levels in 20 healthy control persons, 12 recently diagnosed coeliac cases, 21 patients on a prescribed gluten-free diet and 22 patients with inflammatory bowel disease.

Summary Dermatitis herpetiformis (DH) and coeliac disease (CD) are linked but their association with linear IgA dermatosis (LAD) is unclear. Thirty-seven patients with DH and 27 with linear IgA dermatosis were investigated, of which 23/37 DH patients and 1/10 LAD patients had small intestinal enteropathy. Elevated IgG and IgA gliadin antibodies were found in the DH patients with enteropathy (CD). IgG gliadin antibodies in DH patients were directed against alpha, beta, gamma and omega gliadin subfractions. Elevated IgA gliadin antibodies in the adult LAD patients (n= 14) suggests that this condition may be associated with enteropathy or an IgA diathesis.

We have measured IgG1, 2, 3 and 4 subclass antibodies to gliadin and casein in normal controls, treated and untreated coeliac patients. The amount of antibody in each subclass was determined separately as a titre and as a concentration, by reference to a standard curve. Both methods of quantitation, carried out in separate assays, yielded comparable results (IgG antibody r = 0.86, IgG1 antibody r = 0.89). In all the coeliac patients, the majority of antibody was IgG1, and little IgG2, 3, 4 antibody was detected. Untreated coeliac patients had higher titres of IgG and IgG1 antibodies to gliadin and casein compared with normal controls. In the treated coeliac patients compared with the normal controls, there was no significant difference between the titres of IgG and IgG1 antibodies to gliadin but there were higher titres to casein.

Dermatitis herpetiformis (DH) and coeliac disease are associated and the rash of DH is gluten-dependent. The gliadin fraction responsible for the rash is unknown. In linear IgA dermatoses the role of gluten in the skin eruption remains controversial. Anti-gliadin antibodies (AGA) were measured by an enzyme-linked immunosorbent assay in 10 normal controls; 35 patients with dermatitis herpetiformis (DH); 14 adults with linear IgA disease; and 13 patients with chronic bullous dermatosis of childhood. The presence of enteropathy was assessed by jejunal biopsy and intra-epithelial lymphocyte (IEL) counts. DH with normal IEL counts on normal diet: IgG and IgA-AGA identical to controls. DH with raised IEL counts on gluten-free diet: slightly elevated IgG and IgA-AGA. DH with raised IEL counts on a normal diet: IgG and IgA were higher, with median IgG 1:2048 (control 1:512) median IgA 1:512 (control 1:128). DH patients with high IgG AGA had elevated titres to α, β, γ, and ω subfractions. The highest levels were for α and the lowest for ω. For linear IgA disease IgG is normal but adults had raised IgA-AGA compared to controls (P= 0.005). In dermatitis herpetiformis the presence of anti-gliadin antibody was dependent on the degree of enteropathy, and, if present, was directed against all gliadin subfractions. The significance of the elevated IgA—AGA in the linear IgA disease is unknown.