Biomedical subjects
Publications and source records attributed to H Lowenstein.
This is a revision of the allergen nomenclature system which was proposed in 1986. The nomenclature is for allergens which induce IgE-mediated allergy in humans. A table of allergens with known partial or complete sequences as of December 1993 is given.
The effect of a 3-year course of cat or dog immunotherapy (IT) was evaluated in 32 patients with a history of asthma on exposure to cat or dog. Twenty-one subjects (14 children and seven adults) received cat IT and 11 subjects (six children and five adults) received dog IT. Bronchial challenges with allergen and histamine were performed once a year. Specific IgE, IgG1, and IgG4 were measured, and skin prick tests were done in connection with the challenges. Allergen sensitivity decreased significantly in both treated groups (p less than 0.001 and p less than 0.05 in the cat-allergen and dog-allergen treated groups, respectively). Bronchial hyperreactivity measured by the provocative concentration of histamine causing a 20% decrease in peak expiratory flow in the cat-allergen treated patients (p less than 0.001) but not in the dog-allergen treated patients. Skin sensitivity decreased in both groups (p less than 0.01 and p less than 0.05), whereas specific IgE increased initially but dropped to the pretreatment level during the second year. Specific IgG1 and IgG4 increased during the first and second year in the cat-allergen treated group (p less than 0.01 and p less than 0.001), whereas only IgG4 increased in the dog-allergen treated group (p less than 0.01). Five cat-allergen treated children and one of the adults who completed 3 years of therapy had mild systemic reactions. We conclude that cat IT ameliorated bronchial allergen sensitivity and bronchial hyperreactivity and resulted in an adequate antibody response. Dog IT was less efficacious but led to attenuation of bronchial allergen sensitivity.
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Six candidate extracts of Lolium perenne (rye-grass) pollen have been studied in 6 laboratories using a variety of immunochemical and physicochemical techniques. Radioallergosorbent test inhibition, crossed immunoelectrophoresis, crossed radio-immunoelectrophoresis, sodium dodecyl sulphate-polyacrylamide gel electrophoresis combined with immunoblot, thin-layer isoelectric focusing and enzyme-linked immunosorbent assay inhibition were used to evaluate each of the coded extracts. The source materials were also studied for identity and possible contamination by light microscopy. On the basis of these data, the Rye-Grass Working Party recommended to the Steering Committee of the Allergen Standardization Subcommittee of the International Union of Immunological Societies that the extract coded C be chosen as the candidate international reference preparation.
A lyophilized candidate extract of Bermuda-grass (Cynodon dactylon) pollen, intended for use as an International Reference Standard, was prepared by pooling four individual candidate extracts. In preliminary investigations, the four candidate extracts encompassed a variety of extraction methods. The collaborative testing program simultaneously analyzed the proposed reference and the individual extracts and included 11 laboratories performing RAST inhibition, histamine release, crossed immunoelectrophoresis, crossed radioimmunoelectrophoresis, isoelectric focusing, sodium dodecyl sulfate gel electrophoresis, and protein determinations with a variety of reagents and methods. The four candidate extracts and the pooled reference were found to be equivalent. The stability of this extract has also been studied. This International Reference Preparation of Bermuda grass-pollen extract should be useful for research and industry.
This article presents a nomenclature system for allergens which has been officially recommended by the International Union of Immunological Societies (IUIS). The nomenclature is based on proposals of the IUIS Sub-Committee for Allergen Nomenclature and is applicable to highly purified, well-characterized allergens and to non-purified or partially purified allergenic extracts.
By means of crossed radio-immunoelectrophoresis specific IgE antibodies to Trichophyton rubrum were demonstrated in serum from seven of eight patients with chronic T. rubrum infection. Total IgE values were within normal limits in all. In contrast, no specific IgE antibodies were found in sera from 10 patients with inflammatory ringworm lesions due to Microsporum canis, T. mentagrophytes or T. verrucosum or from six non infected controls. A long-lasting exposure to a constant antigen load is considered of importance for the development of humoral immunity including IgE production.
An extract of mixed dog hair and dandruff from six different dog breeds (alsatian, boxer, collie, poodle, and long-haired and short-haired dachshund) was obtained by mild extraction, centrifugation, dialysis and freeze-drying. Extract of hair and dandruff from the individual dog breeds was obtained in the same way, but the material was not freeze-dried. Examination and characterization of the mixed extract by means of crossed immunoelectrophoresis revealed a precipitation pattern composed of 25 antigens, some of which were mutually partially identical, and a high content of dog serum proteins was found. Quantitative and qualitative differences between the individual dog breeds were demonstrated. Partial identity of the antigens of the mixed extract with antigens of serum, antigens of extracts of hair and dandruff from cat, cow, horse and guinea pig, and antigens from extract of house dust was also observed. By means of crossed radioimmunoelectrophoresis, using sera from 21 patients who were RAST-positive to dog hair and dandruff extract, the specific IgE-binding to antigens of the mixed extract was examined. On the basis of these results major and minor allergens were identified. Dog albumin was found to be a very important major allergen, but alpha1-antitrypsin and gamma-globulin were also identified. Furthermore, four non-serum proteins were shown to be allergens. No breed-specific allergens could be identified in the extracts from the individual dog breeds.
Freeze-dried extract of Cladosporium herbarum Link ex Fr. was obtained by growing, harvesting, extracting, centrifuging, dialysing and freeze-drying. Quantitative immunoelectrophoresis using rabbit antibodies revealed the extraction procedure to be reproducible and the extract to be composed of 57 antigens, none of which originated from the substrate used in the growth. The molecular weight distribution and the approximate molecular weight of some antigens of C. herbarum were obtained using gel filtration. The pI distribution and the approximate pIs of a few distinct antigens of C. herbarum were obtained by isoelectric focusing. Preliminary identification of 4 allergens from C. herbarum was performed by means of CRIE (crossed radioimmunoelectrophoresis).
Children with cow's milk intolerance, clinically non-confirmed cow's milk intolerance, coeliac disease, non-confirmed malabsorption, other gastrointestinal disorders and normal children were investigated for the presence of precipitins against 40 individual bovine whey proteins by means of the crossed immunoelectrophoresis with intermediate gel technique. In the various groups of children the amount and specificity of bovine whey precipitins were neither connected with the various gastrointestinal disorders nor with alternating diet and challenge with milk. Bovine whey-specific IgE could not be detected in any of the patients clinically suspected for cow's milk intolerance by cutaneous test, RAST or CRIE. The immunoglobulin level of the patients investigated did not differ significantly from the normal ranges. It is concluded that investigations of serum precipitins against bovine whey proteins do not give any significant information concerning cow's milk intolerance.
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Extract of wheat flour obtained by extraction, centrifugation and dialysis was immunochemically characterized by quantitative immunoelectrophoresis using rabbit antibodies. The analysis revealed wheat flour to be composed of 40 antigens, some of which were immunologically partially identical with antigens of rye flour and of common grass pollen. Furthermore, antigens of the gliadin fraction of wheat flour were identified. 25 bakers with allergic complaints working in and around Copenhagen were clinically tested with wheat flour and related extracts. Among 13 bakers with respiratory complaints (asthma and/or rhinitis), 11 showed positive reactions to wheat flour extract when tested in histamine release from basophil leukocytes radioallergosorbent test and skin test, whereas further 2 were positive in the basophil test only. The ability of the IgE of individual sera to adsorb to the individual antigens of wheat flour was examined by means of crossed radioimmunoelectrophoresis. On the basis of these results, individual allergenic components of wheat flour were identified, three of these with comparatively high affinity and frequency.
Human ceruloplasmin from fresh serum has been purified by chromatography on hydroxyapatite and Con A-Sepharose. Quantitative immunoelectrophoretic analysis of fresh serum, stored serum and fractions from the different purification steps for human ceruloplasmin has been carried out. A combination of the latter, advanced technique with amino acid analysis, molecular weight determination by size chromatography, urea treatment, staining for oxidase activity and enzymatic proteolysis, has revealed that: 1) human cerulplasmin is a heterogeneous mixture of two glycoproteins (x) differing only in their carbohydrate content and 2) the protein part contains at least one very labile peptide bond which upon enzymatic hydrolysis gives rise to peptides with molecular weights of 93,000 (y) and 24,000 (z) dalton, respectively. The two glycoproteins are immunochemically identical. The y peptide is immunochemically partially identical, and the z peptide immunochemically non-identical, with the parent molecule. The y and z peptides are non-identical. On the basis of these observations a simplified two-dimensional model of human ceruloplasmin is proposed.
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