Biomedical subjects
A Urisu
Publications and source records attributed to A Urisu.
[Allergen analysis of buckwheat by the immunoblotting method].
Inhalation or ingestion of very small amounts of buckwheat allergen can initiate severe symptoms including wheezing, rhinorrhea, urticaria, vomiting and anaphylactic shock in patients with hypersensitivity against buckwheat. However, few studies of the immunological properties of buckwheat allergen have been made. The aim of the present investigation was to analyze the allergen in buckwheat antigen using the immunoblotting method, radioallergosorbent test (RAST) and RAST inhibition assay. Buckwheat 24 kilodalton protein (BW24KD) was shown by immunoblotting analysis to be the most frequently recognized allergenic component, binding to IgE antibodies from 100% of the patients' sera. There was a significant positive correlation (p < 0.001) between % bindings for BW24KD and buckwheat. In the RAST inhibition assay using patients' sera which showed positive IgE antibodies to buckwheat and BW24KD, there was effective inhibition in a dose-dependent manner between inhibition in a dose-dependent manner between BW24KD and buckwheat. These data indicated that BW24KD was a major allergen in buckwheat antigens. The experiments of SDS-PAGE using digestion buffer with or without 2-mercaptoethanol suggested that BW24KD was a component of heterodimer and the paired components had different molecular weights.
Nucleotide sequence of a cDNA clone encoding a major allergenic protein in rice seeds. Homology of the deduced amino acid sequence with members of alpha-amylase/trypsin inhibitor family.
A cDNA clone of rice major allergenic protein (RAP) was isolated from a cDNA library of maturing rice seeds. The cDNA had an open reading frame (486 nucleotides) which coded a 162 amino acid residue polypeptide comprising a 27-residue signal peptide and a 135-residue mature protein of M(r) 14,764. The deduced amino acid sequence of RAP showed a considerable similarity to barley trypsin inhibitor [1983, J. Biol. Chem. 258, 7998-8003] and wheat alpha-amylase inhibitor [1981, Phytochemistry 20, 1781-1784].
16-kilodalton rice protein is one of the major allergens in rice grain extract and responsible for cross-allergenicity between cereal grains in the Poaceae family.
Cross-allergenicity between five cereal grains including rice, wheat, corn, Japanese millet (Panicum crus-galli L. var. frumentaceum Trin.) and Italian millet (Setaria italica Beauv. var. germanica schrad.) was examined by radioallergosorbent test (RAST) and RAST inhibition assay. There were significant close correlations between every combinations of RAST values for the five cereal grain extracts. RAST inhibition assay of each extract against RAST discs coupled with other cereal grain extracts indicated marked cross-reactivity of IgE binding between these cereal grain extracts. Rice protein 16KD (RP16KD) was shown to be one of major allergens in rice grain extracts by immunoblotting analysis, histamine release assay from human leukocytes and RAST inhibition. Next, the involvement of RP16KD in the cross-allergenicity between these cereals was investigated. RAST values for RP16KD significantly correlated with that for Italian millet as well as rice but not with those for corn and wheat. There was a trend of positive correlation between RAST values for RP16KD and Japanese millet. In the RAST inhibition assay using sera with positive RAST for these five cereal grain extracts and RP16KD, RP16KD inhibited IgE binding to these all cereal discs in a dose-dependent manner. Similarly, all of the five cereal grain extracts showed an effective decrease in IgE binding to the RP16KD disc. These results indicated possible participation of IgE binding structure on RP16KD in cross-allergenicity between these cereal grain extracts in the Poaceae family.
Rice protein 16KD--a major allergen in rice grain extract.
The allergenic activity of Rice protein 16 KD (RP16KD) isolated from water soluble rice proteins was examined by radioallergosorbent test (RAST), RAST inhibition and histamine release assay. All of the 31 sera which showed positive RAST values for rice grain extract were positive for RP16KD RAST. Furthermore, there was a significant correlation (r = 0.56, p less than 0.01) between these RAST values. PR16KD effectively inhibited IgE binding to the rice grain extract disc in RAST inhibition assays using 4 sera with positive RAST values for both antigens. In 17 subjects with positive RAST values for rice grain extract, a significant positive correlation (r = 0.53, p less than 0.05) was found between the maximum percent histamine releases from their leukocytes by rice grain extract and RP16KD. These data strongly suggest that RP16KD is one of the major allergens of rice grain.
[The involvement of rice protein 16KD in cross-allergenicity between antigens in rice, wheat, corn, Japanese millet, Italian millet].
Cross-reactivity between rice, wheat, corn, Japanese millet and Italian millet in Poaceae family were studied by absorption test, radioallergosorbent test (RAST), and RAST inhibition assay. In absorption test using Phadebas RAST discs, more than 50% absorption of IgE antibodies was observed between rice, wheat and corn. There were significant correlations of RAST values for cereal grains including rice, wheat, corn, Japanese millet and Italian millet. RAST inhibition assay between every combinations of these cereals showed dose-dependent decrease in IgE-binding. These data indicated cross-reactivity with IgE antibodies between the five cereals in Poaceae family. RAST values for RP16KD significantly correlated with those for Italian millet as well as rice but not with those for corn and wheat. There was a trend of positive correlation between RAST values for RP16KD and Japanese millet. In RAST inhibition assay using sera with positive RAST for these five cereal grains and RP16KD, RP16KD inhibited IgE-binding to these all cereal discs in dose-dependent manner. Similarly, all of five cereal grain extracts showed an effective diminution in IgE-binding to RP16KD disc. These results indicated possible participation of IgE-binding structure on RP16KD in cross-reactivity between these cereal grains in Poaceae family.
[Relationship between immediate hypersensitive reactions by buckwheat ingestion and specific IgE for rice in subject with positive IgE-RAST for buckwheat].
IgE-mediated mechanisms are important in immediate hypersensitive reactions (IHR) to buckwheat. However, a part of subjects with high IgE for buckwheat show no IHR to buckwheat ingestion. Inspite of cross-allergenicity between buckwheat and rice, rice ingestion rarely induces IHR even in subjects with high IgE for rice unlike buckwheat-induced IHR. We speculated that there were some relationships between the presence of IHR to buckwheat and recognition of cross-allergenic determinants on buckwheat components with rice components. We examined IgE-RAST for rice in 58 subjects with positive IgE-RAST for buckwheat. IgE-RAST for Dermatophagoides pteronyssinus (Dp), egg white and cow's milk as unrelated antigens with rice were also assessed for a comparison. Subjects (n = 33) without IHR to buckwheat showed higher IgE-RAST values for rice than those (n = 25) with IHR, whereas there were no differences in IgE-RAST values for Dp, egg white and cow's milk between two groups with and without IHR. IgE-RAST values for buckwheat showed significant close correlations to those for rice in subjects without IHR to buckwheat but not in those with IHR. There were no significant correlations between IgE-RAST values for buckwheat and for Dp, egg white or cow's milk in both groups with and without IHR. These results suggested that the IgE from subjects without IHR to buckwheat recognized cross-allergenic determinants with rice on the buckwheat components.
[Histamine release from human leukocytes by human recombinant interleukin-3].
Human recombinant interleukin-3 (hrIL-3) released histamine from human leukocytes in vitro. The histamine release by hrIL-3 significantly correlated with those by anti-IgE, thrombin, and f-met. peptide, but not by A23187. Histamine release by hrIL-3 was a Ca2(+)-dependent reaction, as was that by anti-IgE, although the time course of histamine release by hrIL-3 was slower than that by anti-IgE. Pre-treatment of leukocytes with hrIL-3 decreased the histamine release by hrIL-3 itself, but enhanced the histamine releases by anti-IgE, f-met. peptide, thrombin and A23187. These results suggested that the mechanism of hrIL-3-induced histamine release was different from those of anti-IgE, f-met. peptide, thrombin, and A23187. There was no significant difference between hrIL-3-induced histamine release of leukocytes from asthmatics and healthy controls.
[Inhibitory action amlexanox on interleukin-3-induced enhancement of histamine releasability of human leukocytes].
Amlexanox, an anti-allergic drug, showed a concentration-dependent inhibition against hrIL-3-induced enhancement of in vitro histamine release from human leukocytes by anti-IgE. The significant inhibitory action of amlexanox was observed in one out of nine and six out of nine allergic subjects at concentrations of 10(-5) M and 10(-4) M, respectively. This means that the inhibitory effect of amlexanox varied from patient to patient. Post-treatment as well as simultaneous treatment with amlexanox produced an inhibitory action on the enhancing effect of hrIL-3, suggesting that hrIL-3-induced enhancement of releasability is a reversible reaction. AA-861, OKY-046, superoxide dismutase and prostaglandin E2 showed no effects on the hrIL-3-induced enhancement of histamine releasability. The inhibitory action of amlexamox to the hrIL-3-induced enhancement of histamine releasability may be a new anti-allergic mechanism, details of which remains unclear.
[Allergic individuals to Japanese cedar or orchard grass consist of two subgroups based on the sensitization to Dermatophagoides pteronyssinus].
One hundred and twenty-six allergic subjects were divided into three groups based on the RAST results for Dermatophagoides pteronyssinus (D.p) and Japanese cedar (J.C.). We compared sex, age of examination for RAST, serum IgE, family history of allergic diseases, prevalence rate of bronchial asthma (BA) and allergic rhinitis (AR), and onset of AR among three groups. No significant difference in the other variables except serum IgE and prevalence rate of BA was found between the group with D.p-positive and J.C.-positive RAST and the group with D.p-positive and J.C.-negative RAST. The group with positive RAST for D.p and J.C. showed lower age of the examination, higher serum IgE, higher incidence of allergic family history, higher prevalence rate of BA, and lower onset age of AR than the group with negative RAST for D.p and positive RAST for J.C. We suggested that in J.C. RAST-positive group there might be two different subgroups distinguished by RAST result for D.p Similar results were obtained from the assessment of RAST for Orchard grass instead of J.C.
Human herpesvirus type 6 infection (exanthem subitum) without fever.
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Studies on the osmophilic fungus Wallemia sebi as an allergen evaluated by skin prick test and radioallergosorbent test.
Recently, Wallemia sebi, a species of osmophilic fungi, has been abundantly detected in house dust using low water activity media. In this study, allergenic activity of W. sebi was assessed by skin prick test and radioallergosorbent test (RAST) in 74 asthmatic patients ranging from 6 to 32 years of age. Aspergillus fumigatus and house dust were used for comparison. In skin prick test, W. sebi extract, A. fumigatus extract and house dust extract elicited positive reactions in 4 (5.4%), 4 (5.4%) and 51 (68.9%) patients, respectively. RAST showed positive results in 14 subjects (18.9%) for W. sebi extract, in 8 (10.8%) for A. fumigatus extract and in 59 (79.7%) for house dust extract. These results indicated that some asthmatic individuals showed immediate-type hypersensitivity to W. sebi, and which means this fungal species may be of importance to atopic diseases as a causative agent.
[Allergenic and antigenic activities of the osmophilic fungus Wallemia sebi asthmatic patients].
Recently large amounts of Wallemia sebi, a species of osmophilic fungi, have been detected in house dust by low water activity media. The allergenic activity of W. sebi was examined by skin prick tests and radioallergosorbent tests (RAST) in 74 asthmatic patients (mean age 11.7, range 6-32). Aspergillus fumigatus and house dust were used for comparison. In the skin prick tests, W. sebi extract, A. fumigatus extract and house dust extract elicited positive reactions in 4 (5.4%), 4 (5.4%) and 51 (68.9%) patients, respectively. RAST showed positive results in 14 subjects (18.9%) for W. sebi extract, in 8 (10.8%) for A. fumigatus extract and in 59 (79.7%) for house dust extract. These results indicated that some asthmatic individuals showed immediate type hypersensitivity to W. sebi, which means this fungal species may be important as a causative agent in atopic diseases. Additionally, the authors measured W. sebi-specific IgG by enzyme-linked immunosorbent assay in asthmatic (n = 28) and non-atopic patients (n = 28). W. sebi-specific IgG was found in sera from all subjects in each group. W. sebi-specific IgG in asthmatics (mean +/- SD = 0.686 +/- 0.160) was significantly higher than that in non-atopics (mean +/- SD = 0.572 +/- 0.188) (p less than 0.01).
[A clinical study of two cases with immediate hypersensitivity to apple-pulp and an investigation of cross-allergenicity between apple-pulp allergen and some other pollen allergens].
In Japan there are no case reports of immediate hypersensitivity to apple-pulp. Here, we report on two patients: a 23-year-old woman and a 14-year-old girl with 3-year and 7-year histories, respectively, of anaphylactic reactions to apple-pulp. In the first patient, eating raw apples immediately elicited itching and tingling of the lips and mouth with severe edema of the lips and tongue, irritation of the throat and slight colic in the upper abdomen. In the second, nausea and vomiting occurred after ingestion of apples. In skin prick tests, they showed positive reactions to apple-pulp extract prepared by the method of Björkstén et al. and to fresh apple juice. In addition, IgE antibody to the apple-pulp extract was detected in the sera of both patients. They also possessed IgE antibodies to some other species of both pollens and fruits/vegetables in their sera. In the present study, cross-allergenicity between apple-pulp and five pollen species, which consisted of birch, Japanese cedar, orchard grass, mugwort and ragweed pollen, was investigated by RAST inhibition. The apple-pulp extract effectively inhibited RASTs to all the pollens except Japanese cedar pollen. These results suggested that the four pollens might have shared allergen with the apple-pulp extract.
[Identification of orchard grass (Dactylis glomerata) pollen allergens by immunoblotting].
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Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae.
Fimbriae were removed from Bordetella pertussis (serotype 1.3.6) by mechanical shearing and purified by precipitation with ammonium sulfate, pH-dependent precipitation at pH 7.4, followed by two successive extractions of the precipitated fimbriae with 4 M urea. By electron microscopy, the precipitated fimbriae appeared as aggregated bundles of long, relatively straight filaments which were disaggregated to individual flexuous filaments at pH 10.5. These purified fimbriae were identified as serotype 6 agglutinogens, since antibody to the purified fimbriae agglutinated B. pertussis strains serotyped as 1.3.6, 1.2.3.6, or 1.2.3.4.6 but did not agglutinate strains of serotype 1.2.3.4, 1.2.3, or 1.3. In contrast, antibody to serotype 2 fimbriae only agglutinated B. pertussis strains containing serotype 2 agglutinogen. Purified type 6 and 2 fimbriae were found to be weakly cross-reactive by enzyme-linked immunosorbent assay, using polyclonal antibody to each type of fimbria. In an immunoblot assay, polyclonal antibodies to a 22,000-dalton subunit of fimbriae from B. bronchiseptica reacted strongly with the type 2 fimbrial subunit of B. pertussis, but only weakly with the type 6 subunit. When subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the protein subunit of the type 6 fimbriae migrated with a molecular weight of 21,500, whereas the type 2 fimbrial subunit had a molecular weight of 22,000. The two types of subunits had similar amino acid compositions and showed amino-terminal sequence homology in 15 of 21 amino acids. The amino-terminal amino acid sequences of the B. pertussis fimbriae were distinct from those reported for fimbriae from other gram-negative bacteria. Neither the type 6 nor the type 2 fimbriae caused hemagglutination when assayed with several types of erythrocytes.
Filamentous hemagglutinin has a major role in mediating adherence of Bordetella pertussis to human WiDr cells.
[35S]methionine-labeled Bordetella pertussis adhered to monolayers of WiDr cells, an epitheliumlike cell line from a human intestinal carcinoma. Adherence was proportional to the density of the WiDr cells and to the concentration of B. pertussis in the assay. Adherence of virulent phase I strains Tohama phase I, 114, and BP338 was much greater than adherence of avirulent strains Tohama phase III and 423 phase IV. Mutants deficient in the production of the filamentous hemagglutinin (FHA) were hemagglutination negative and adhered to WiDr cells much less efficiently than the parent strains. Preincubation of B. pertussis cells with FHA increased their hemagglutination activity and adherence to WiDr cells. Goat antibody to FHA inhibited, in a dose-dependent manner, the adherence of strain Tohama I but not the adherence of FHA-deficient mutant Tohama 325. At similar protein concentrations, normal goat antibody, goat antibody to pertussis toxin, or the Fab fragments of goat antibody to serotype 2 fimbriae had no effect on adherence. Also, an FHA-positive strain without fimbriae showed high adherence, while a fimbriated FHA-deficient mutant adhered poorly. Our data indicate that FHA plays a major role in adherence of B. pertussis to human WiDr cells. Fimbriae do not appear to mediate attachment of B. pertussis to WiDr cells.
Involvement of filamentous hemagglutinin in the adherence of Bordetella pertussis to human WiDr cell cultures.
Attachment of 35S-methionine-labelled Bordetella pertussis to monolayers of WiDr cells, an epithelium-like cell line from a human intestinal carcinoma, was examined. The amount of adherence was proportional to the density of the WiDr cells and to the concentration of B. pertussis in the assay. The amount of attachment of virulent strains Tohama phase I, 114 and 338 was much greater than the attachment of avirulent strains, Tohama phase III and 423 phase IV. Attachment of strain Tohama 325, a spontaneous mutant of Tohama I, and strains 353 and 354, Tn5 insertion mutants of 338 was also examined. These mutants have phenotypic properties similar to the parent strain, except the mutants are deficient in the production of the filamentous hemagglutinin (FHA). The FHA deficient mutants adhered to WiDr cells much less efficiently than the parent strains. Goat antibody to FHA inhibited, in a dose dependent manner, the attachment of Tohama I, but not of strain 325. At the same protein concentrations, normal goat antibody or goat antibody to the lymphocytosis-promoting factor had no effect on attachment. Preincubation of bacteria with FHA enhanced the attachment of Tohama I, Tohama 325, and Tohama III. These data support the involvement of FHA in the adherence of B. pertussis to human WiDr cell cultures.