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Biomedical subjects

H Yasueda

Publications and source records attributed to H Yasueda.

At least 91 records · Page 5Linked to original sources
PubMed1989

Comparative analysis of physicochemical and immunochemical properties of the two major allergens from Dermatophagoides pteronyssinus and the corresponding allergens from Dermatophagoides farinae.

Two major allergens, DP1 (Der p I) and DP2 (Der p II), were isolated from the whole culture extract of Dermatophagoides pteronyssinus, and the physicochemical and immunochemical properties of these allergens were compared with those of the corresponding allergens from Dermatophagoides farinae, DF1 (Der fI) and DF2 (Der fII). On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, polyacrylamide gel isoelectric focusing and amino acid analysis, both DP1 and DP2 were demonstrated to have close physicochemical similarity with DF1 and DF2, respectively. On immunodiffusion with the use of rabbit antisera, the two Der I allergens showed the reaction of typical partial identity, while the two Der II allergens showed the reaction of almost complete identity. Radioallergosorbent test (RAST) and RAST absorption experiments with the use of sera from mite-allergic patients showed that human IgE antibody response to the Der I allergens was directed against both cross-reactive and species-specific determinants. In contrast, IgE antibodies to the Der II allergens were demonstrated to react almost completely to cross-reactive determinants.

Allergens↗
PubMed1989

Measurement of allergens associated with dust mite allergy. I. Development of sensitive radioimmunoassays for the two groups of Dermatophagoides mite allergens, Der I and Der II.

Sensitive radioimmunoassays were developed to measure the two groups of major allergens (Der I and Der II) of Dermatophagoides pteronyssinus and Dermatophagoides farinae, in which radiolabeled protein A served as a general tracer. Glass rods covalently coupled with F(ab')2 fragments of rabbit antiserum IgG were incubated first with mite or house dust extracts, and then with affinity-purified rabbit antibodies. The bound allergen-antibody complex was detected with a 125I-labeled protein A. The two Der I allergens, Der p I and Der f I, were measured separately with the use of immunoabsorbed rabbit antibodies directed against species-specific determinants, while the two Der II allergens, Der p II and Der f II, were measured as 'Der II' with the use of antibodies directed against common determinants on both allergens. Each assay demonstrated consistently parallel dilution curves with mite and house dust extracts. The mean intraassay and interassay coefficient of variation for each assay ranged from 4.3 to 7.7% and from 3.6 to 9.0%, respectively. The Der p I and Der f I assays were shown to be highly species-specific so that the ratio of Der p I: Der f I would provide a good index of the distribution of the two mite species in a dust sample. The concentrations of the Der I and Der II allergens in different types of mite extract and dust samples from houses were compared using these assays.(ABSTRACT TRUNCATED AT 250 WORDS)

Allergens↗
PubMed1989

Measurement of allergens associated with dust mite allergy. II. Concentrations of airborne mite allergens (Der I and Der II) in the house.

Assays of mite allergens (Der p I, Der f I and Der II) in the air of houses became feasible with the use of a low-noise air sampler and a sensitive radioimmunoassay described previously. The levels of the airborne allergens Der I (Der p I + Der f I) and Der II in the living room of 10 houses during usual domestic life were very low, 29.5 and 6.3 pg/m3, respectively, with a Der I: Der II ratio of 4.7:1. At the time of bedmaking, they greatly increased, about 1,000-fold, to 30,900 and 12,600 pg/m3, respectively, with a Der I: Der II ratio of 2.5:1. The amounts of Der I and Der II in the floor dust of the living room were 2,040 and 2,690 ng/g of fine dust, respectively, with a Der I: Der II ratio of 0.8:1. Der I seemed more prone to become airborne than Der II.

Air↗
PubMed1989

[Measurement of IgE, IgG1 and IgG4 antibodies against mite Sephadex fractions and purified allergens by means of enzyme-linked immunosorbent assay].

Mite antigens (Dermatophagoides farinae) were fractionated by a Sephadex G-200 column and their reactivities with IgE, IgG1 and IgG4 antibodies were investigated with enzyme-linked immunosorbent assay (ELISA). High IgE antibody values were observed in fractions with low molecular weight (allergenic part), while high IgG1 and IgG4 antibody values were observed in fractions with high molecular weight. High IgG4 antibody values to crude mite extract and fractions with high molecular weight were detected in individuals who had received immunotherapy. However, IgG4 antibodies directed to allergenic part were found in only one out of 12 sera tested. IgG4-ELISA using DF1 (major allergen of Dermatophagoides farinae) as antigen was also performed. In the group treated with mite, significant IgG4 antibody levels were detected in only one out of 13 sera tested. In the group treated with house dust, significant IgG4 antibodies were detected in only one out of 12 sera tested. Patients who showed high IgG4 antibody responses to crude mite extract and to high molecular weight did not show responses to allergenic part and DF1. The only case who showed positive IgG4 responses to allergenic part also reacted with DF1. Those results suggest that IgG1 and IgG4 antibody values in ELISA using crude mite extract as antigen do not reflect major allergen-specific antibody values. The importance of the use of partially purified antigens in measuring major allergen-specific IgG4 antibodies was also suggested.

Allergens↗
PubMed1988

Isocratic determination of arachidonic acid 5-lipoxygenase products in human neutrophils by high-performance liquid chromatography.

A high-performance liquid chromatographic method was developed to determine arachidonic 5-lipoxygenase products in calcium ionophore-stimulated neutrophils. This procedure allows the simultaneous measurement of leukotriene B4 (LTB4) and its omega-oxidation products without using a gradient elution system. 20-Carboxy-LTB4, 20-hydroxy-LTB4, 6-trans-LTB4, 12-epi-6-trans-LTB4, LTB4 and 5s,12s-dihydroxyeicosatetraenoic acid can be separated and quantitated by reversed-phase chromatography using isocratic elution. The generation and degradation of 5-lipoxygenase products by human neutrophils following stimulation with calcium ionophore have been examined by this method.

12-Hydroxy-5,8,10,14-eicosatetraenoic Acid↗
PubMed1988

Effect of deuterium oxide on leukotriene C4 generation in immunologically stimulated human leukocytes.

Addition of deuterium oxide (D2O), 6-36%, resulted in a dose-dependent increase in allergen- or anti-IgE-induced leukotriene C4 (LTC4) generation from human basophils. In the presence of 36% D2O, the enhancement was 260 +/- 135% for allergen stimulation and 480 +/- 152% for anti-IgE stimulation as compared with the control incubated in normal buffer. The increasing effect of D2O on LTC4 generation from basophils was completely reversed by washing the cells before incubation with allergen. Vinblastine as well as colchicine, at a concentration of 100 microM, counteracted the effect of D2O. The enhanced release of histamine and LTC4 from basophils challenged with allergen was suppressed by Dimaprit, a histamine H2 receptor agonist, at a concentration required to inhibit the release by 50% of 5 X 10(-5) M for histamine and 10(-5) M for LTC4. These observations suggest that microtubules may be involved in LTC4 generation from immunologically stimulated basophils.

Basophils↗
PubMed1986

Allergen induced histamine release and immunoreactive-leukotriene C4 generation from leukocytes in mite sensitive asthmatic patients.

Leukocytes from mite sensitive asthmatic patient were challenged with the allergen and the supernatant was assayed for histamine and immunoreactive-leukotriene C4 (i-LTC4). The release of histamine was quantitated by an automated fluorometric technique and i-LTC4 was determined using a commercial radioimmunoassay kit. The results of analysis of the supernatant by high speed liquid chromatography, together with observations of modulation of the formation by agents, indicated that i-LTC4 consisted of LTC4 with a little amount of LTD4. i-LTC4 was generated as a result of basophil activation but not derived from the other cells such as monocytes and eosinophils. Allergen induced a concentration-dependent release of histamine and i-LTC4 and the maximal release of histamine and i-LTC4 occurred at the same dose of the allergen. At optimal concentration of the allergen, basophils produced 20.4 +/- 17.9 ng of i-LTC4/10(6)-cells (mean +/- S.D., n = 39) and histamine release was 55.6 +/- 20.1% of total histamine. There was a significant correlation in the capacity of leukocytes to release histamine and i-LTC4 (r = 0.47, p less than 0.01). We found a correlation between maximal histamine release or cell sensitivity, allergen concentration for 50% histamine release, and a ratio of specific IgE to mite to total IgE in the serum, but the amount of i-LTC4 failed to correlate significantly with the ratio. The releasability and the cell sensitivity of asthmatic patients' cells to the allergen for histamine release paralleled the severity to symptoms, but this correlation was not significant in i-LTC4 generation.

Adult↗
PubMed1986

Isolation and characterization of two allergens from Dermatophagoides farinae.

Two purified allergens, designated as DF1 and DF2, were isolated from the extract of the whole culture of Dermatophagoides farinae by a combination of ammonium sulfate precipitation and ion exchange, hydrophobic, chelate and gel chromatography. DF1 was isolated as a heat-sensitive acidic protein with an apparent molecular weight of 25,000 and an isoelectric point of 4.6-7.2. DF2 was isolated as a heat-stable basic protein with an apparent molecular weight of 15,000 and an isoelectric point of 7.8-8.3. No allergenic cross-reactivity was seen between DF1 and DF2. Both DF1 and DF2 were shown to be the major allergens of D. farinae by the results of radioallergosorbent test and histamine release assay.

Allergens↗
PubMed1986

Cross-reactivity between the pollens of Cupressus sempervirens (common cypress) and of Cryptomeria japonica (Japanese cedar).

A clinical and immunologic study was performed comparing a group of French patients allergic to the pollens of cypress (Cupressus sempervirens, which belongs to the Cupressaceae family) and a group of Japanese patients allergic to the pollens of Sugi (Cryptomeria japonica, which belongs to the Taxodiaceae family). By skin testing, RAST, and RAST inhibition, clear cross-reactivity was detected between the two pollens. No cross-reactivity was detected between the pollens of Cupressus sempervirens and Sugi and the Pinaceae family. In addition, one can speculate that an antigen in Cupressus sempervirens is cross-reactive with SBP, the major allergen of Sugi, suggesting that there is a closer relationship between the Taxodiaceae family and the Cupressaceae family than between these two families and the other families of the gymnosperms. This finding throws new light on the taxonomy of the gymnosperms.

Cross Reactions↗
PubMed1985

Increased activity of 5-lipoxygenase in polymorphonuclear leukocytes from asthmatic patients.

The formation of 5-lipoxygenase products of arachidonic acid, 5-HETE and 5,12-diHETE, was determined in 100,000 X g supernatant of polymorphonuclear leukocytes from 17 healthy subjects, 17 patients with extrinsic asthma and 15 patients with intrinsic asthma. After the supernatant was incubated with 14C-arachidonic acid in the presence of calcium and indomethacin, the lipoxygenase products of arachidonic acid were separated by thin layer chromatography. The results were expressed as the percentage conversion of 14C-arachidonic acid into the product per 10(7) cells. The formation of 5,12-diHETE, but not of 5-HETE, was significantly increased in the cells from the group of patients with extrinsic asthma (4.38 +/- 0.78%, mean +/- S.E.; p less than 0.01) and intrinsic asthma (6.09 +/- 1.11%; p less than 0.01), when compared to normal subjects (1.74 +/- 0.30%). Both extrinsic and intrinsic asthmatics had significantly enhanced 5-lipoxygenase activity, which was expressed as the sum of percentage conversion of 14C-arachidonic acid into 5-HETE and 5,12-diHETE. The percentage conversion in normal subjects was 4.19 +/- 0.39%, 6.24 +/- 0.84% for 17 patients with extrinsic asthma (p less than 0.05), and 8.59 +/- 1.29% for 15 patients with intrinsic asthma (p less than 0.01). There was no significant difference between these asthmatic groups. These results indicate that 5-lipoxygenase activity is increased in patients with bronchial asthma.

Adult↗
PubMed1984

An attempt to produce an antibody of histamine and histamine derivatives.

Three conjugates of different histamine derivatives to bovine serum albumin were prepared, and an attempt was made to determine whether antibody against histamine and histamine derivatives could be produced in rabbits by immunization with these conjugates. Antibody produced by immunization with bovine serum albumin-succinylhistamine conjugate could not recognize the hapten moiety of the immunogen. Immunization of rabbits with conjugate of bovine serum albumin and p-[2-(N alpha-trifluoroacetylhistamine)azo]benzoic acid resulted in the production of antibody to N alpha-trifluoroacetylhistamine. The antibody had a specificity for histamine metabolites and their derivatives. However, the antibody also showed a small but not negligible affinity for trifluoroacetylated serotonin, norepinephrine and aniline, indicating that the antibody specificity was directed mainly to the trifluoroacetamide group. After immunization of rabbits with bovine serum albumin and p-[2-(N alpha-propionylhistamine)azo]benzoic acid conjugate, antibody against N alpha-propionylhistamine could be produced. However, the antibody had a very low affinity even for N alpha-propionylhistamine. Specific antibody to histamine and histamine derivatives could thus not be produced by immunization with the present hapten-carrier conjugates.

Animals↗
PubMed1983

Isolation and partial characterization of the major allergen from Japanese cedar (Cryptomeria japonica) pollen.

A purified allergen, antigen SBP, was obtained from the pollen of the Japanese cedar (Cryptomeria japonica, Sugi in Japanese) by ammonium sulfate precipitation, ion-exchange chromatography on diethylaminoethyl and carboxymethyl cellulose, and gel chromatography on Sephadex G-150. Antigen SBP was a heat-sensitive basic glycoprotein of approximately 40,000 molecular weight. By preparative isoelectric focusing and gel chromatography on Sephadex G-100, antigen SBP could be further separated into four subfractions, differing in both isoelectric point and molecular weight. By immunodiffusion analysis, direct skin testing, and radioallergosorbent test inhibition, it was shown that antigen SBP was the major allergen of Japanese cedar pollen, and the four subfractions were seen to be antigenically and allergenically identical.

Allergens↗