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Biomedical subjects

N Shimojo

Publications and source records attributed to N Shimojo.

At least 73 records · Page 4Linked to original sources
PubMed1995

[Gamma Glutamyltransferase].

Gamma-Glutamyltransferase (GGT), formerly called gamma-glutamyltranspeptidase, is predominantly a membrane-bound enzyme. The estimation of enzyme activity in serum is useful in monitoring hepatobiliary complaints. The electrophoresis with surfactant (Triton X-100) developed by the authors demonstrates five distinct bands of enzyme activity in the serum from patients with hepatitis. These bands are called isoenzyme GGT1 to 5 from anode to cathode, respectively. Four isoenzymes GGT2 to 5, except GGT1 are demonstrated in normal adult serum. The affinity electrophoresis is more variable to identify the hepatoma associated isoenzyme, namely HA-GGT. Concanavalin A used in the method has no affinity with HA-GGT and this isoenzyme is separated from GGT2. The diagnostic sensitivity and specificity for the measurement of HA-GGT were 58% and 83%, respectively.

Animals↗
PubMed1995

[Nasal smear cytology in bronchial asthma: correlation of appearance and numbers of nasal smear mast cells, eosinophils or basophils and serum IgE antibodies to house dust mite in patients with bronchial asthma].

Nasal smear cytology was studied in pediatric patients with bronchial asthma with special reference with IgE RAST to house dust mite, Dermatophagoides pteronyssinus (Dp). Results obtained were as follows: (1) Numbers of eosinophils on the nasal smear correlated well with Dp RAST score, (2) mast cells were detected before Dp RAST becoming positive and appearance of eosinophils, (3) basophils appeared after detection of eosinophils and only in patients with nasal smear eosinophils. These results suggest that mast cells are the early marker for allergic inflammation and basophils and eosinophils appear in association with overt sensitization with house dust mite in house dust mite-sensitized asthmatic patients.

Adolescent↗
PubMed1994

An efficient method for purification of cuprozinc superoxide dismutase from bovine erythrocytes.

Cuprozinc superoxide dismutase (Cu,Zn-SOD) was isolated from bovine erythrocytes by pH-controlled ammonium sulfate-methanol extraction (ASME extraction). Adjustment of the pH of a suspension of the lysed red cells in the presence of ammonium sulfate (90% saturation) to pH 5.0, followed by partition with an equal amount of methanol, resulted in isolation of the enzyme with specific activity of greater than 2000 units/mg of protein. Further purification using DEAE-cellulose column chromatography gave a highly purified Cu,Zn-SOD showing a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using this procedure about 14 mg of pure Cu,Zn-SOD with a specific activity of 4728 units/mg of protein can be recovered from one liter of bovine blood. The enzyme was characterized and the results obtained were in agreement with earlier reports. This procedure appears, therefore, to be a convenient method for isolating the enzyme.

Ammonium Sulfate↗
PubMed1994

Measurements of urinary adipic acid and suberic acid using high-performance liquid chromatography.

A sensitive and specific method was developed for measuring medium-chain dicarboxylic acids (adipic and suberic acid) in urine. These acids were extracted from urine with diethyl ether and converted into fluorescent derivatives with 9-anthryldiazomethane, which can be separated by high-performance liquid chromatography. The reproducibility was high and the recovery from urine was above 90%. Urinary concentrations of adipic acid in streptozotocin-induced diabetic rats were significantly higher than those in control rats. In diabetic patients, both adipic acid and suberic acid tended to be high, but not significantly. This method should be useful for measuring dicarboxylic acids in urine.

Adipates↗
PubMed1994

Quantitative analysis of Lewis antigens on erythrocytes by flow cytometry.

We have developed a method for the quantitative analysis of Lewis antigens on human red blood cells (RBC) using immunofluorescence labeling and flow cytometry. Initially, Lewis a and Lewis b (Le(a) and Le(b)) antigens were labeled with monoclonal anti-Le(a) or anti-Le(b) antibodies followed by labeling with the fluorescein isothiocyanate (FITC)-conjugated second antibody. This method was not sensitive enough to identify the Lewis antigens on RBC, although the FITC method is very commonly used for antigens on white blood cells. Next, we selected the enhanced labeling technique using the avidin-biotin procedure. Biotinylated anti-mouse IgM was used for the second label and the reaction with R-phycoerythrin (RPE)-conjugated streptavidin followed to produce the fluorescence. The method was found to be effective for our objectives. From the results analyzed by the enhanced labeling technique, differences were not found in either the levels of the antigen-positive percentage and the peak mean channel of Le(a) antigens on RBC in the groups of blood type O and A (in ABO system). On the other hand, both the levels of Le(b) antigens on RBC were higher in the groups of blood type O than in those of blood type A. We found both Le(a) and Le(b) antigens on RBC from a few blood type O subjects. We conclude that enhanced labeling and flow cytometry constitute a useful technique for the determination of Lewis antigens on RBC and that this method enables the precise quantification of such antigens.

Bacterial Proteins↗
PubMed1994

Specificities of IgE, IgG and IgA antibodies to ovalbumin. Comparison of binding activities to denatured ovalbumin or ovalbumin fragments of IgE antibodies with those of IgG or IgA antibodies.

We studied the binding activities of IgE, IgG and IgA antibodies in patients with allergy to hen's egg white against two different ovalbumin (OVA) preparations, which were physically or chemically denatured OVA and enzyme-digested OVA fragments. The binding activities of IgE antibodies to these OVA preparations with those of IgG or IgA antibodies were compared. It was found that the binding activities of IgE antibodies to denatured OVA by treatment with dithiothreitol, urea or hydrochloric acid were similar to those of IgG or IgA antibodies. In contrast, the binding activities of IgE antibodies to heat-denatured OVA or by treatment with sodium hydroxide at pH 11.0 were different from those of IgG or IgA antibodies to these denatured OVA. Furthermore, we found that the binding activities of anti-OVA antibodies in sera from patients with allergy to hen's egg white against fragmented OVA were different between IgE antibodies and IgG or IgA antibodies. Thus, it can be concluded that IgE antibodies to OVA in sera from patients with allergy to egg white differ from IgG or IgA antibodies in respect to binding activities against different preparations of denatured or fragmented OVA, probably due to differences in fine specificities of these antibodies against OVA.

Allergens↗
PubMed1994

Identification of the disease-related T cell epitope of ovalbumin and epitope-targeted T cell inactivation in egg allergy.

An ovalbumin (OVA)-specific T cell line (TCL) was established from a patient with hen egg allergy. The TCL was CD4+, expressed alpha beta T cell receptor, and recognized OVA presented by HLA-DR10. Based on the response of the TCL to synthetic OVA peptides, it was found that the TCL recognized OVA 323-339, which is a major T cell epitope presented by murine I-Ad. The TCL secreted high levels of IL-5, but undetectable amounts of IL-2, interferon-gamma, and IL-4 when stimulated with OVA or the OVA 323-339 peptide. Since IL-5 is an important growth and chemotactic factor for eosinophils, it is possible that these OVA 323-339-specific T cells can contribute to human egg allergy. To our knowledge, this is the first demonstration of food allergen-specific TCL establishment and identification of a T cell epitope possibly related to the allergic reaction to food antigens. An analog peptide of the OVA 323-339 which is known to strongly bind to I-Ad partially inhibited the response of the TCL to OVA 323-339 presented by HLA-DR10, raising the possibility of peptide-based immunotherapy of food allergy.

Amino Acid Sequence↗
PubMed1994

Effects of exercise training on the distribution of metallic mercury in mice.

1. The purpose of this study was to correlate exercise induced changes of antioxidant enzymes with the distribution of mercury after mercury vapour exposure in mice. 2. Exercise training consisted of swimming (1 h/day for 5 days/week) for 9 weeks. After 9 weeks of training, swim-trained mice showed significantly elevated levels of catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GSHpx) in their red blood cells, CAT and GSHpx in their kidneys and SOD in the liver. 3. Exercised mice (Ex) and non-exercised mice (N.Ex) were exposed to mercury vapour (3.5 mg m-3) for 1 h. Mercury concentrations were assayed in the blood, brain, heart, lungs, liver and kidneys along with the mercury content of the entire body. The whole body mercury content showed no significant difference in any measurement (immediately, 24 h and 48 h after mercury exposure) between the Ex and N.Ex groups. Mercury concentrations in the Ex group were significantly higher than the N.Ex group in the heart, whole blood, red blood cells and the brain at 24 and 48 h; and in the plasma and kidneys at 24 h. 4. It was concluded that exercise training is a factor in distribution changes of mercury after exposure to mercury vapour, though it is not a factor in the total absorption and excretion of mercury.

Absorption↗
PubMed1994

Lactate in fetal scalp blood and umbilical artery blood measured during normal labor with a test strip method.

A new test strip method was used to determine the lactate concentration in fetal scalp blood during normal labor. Sixty-six fetal scalp blood samples were collected at cervical dilatations between 4 cm and 10 cm. The mean lactate value was 1.7 +/- 0.8 mmol/l simultaneously (IS.D.) and the mean pH sampled simultaneously was 7.36 +/- 0.04 (IS.D.). The corresponding values for base deficit was 2.1 (+/- 1.9) and for pCO2 5.8 (+/- 0.8). No difference was seen in lactate concentrations or pH values in early compared to late first stage of labor. The mean lactate concentration in the umbilical artery immediately after delivery was 3.7 mmol/l +/- 1.2 (IS.D.). The method was easy to handle and gave the result within 60 seconds.

Female↗
PubMed1994

Thyroglobulin-specific T cell line from a healthy individual does not produce proinflammatory cytokines on antigenic stimulation: an implication for possible fail-safe mechanism to avoid autoimmunity.

In order to investigate the regulation of autoimmune response to thyroglobulin (Tg), one of the thyroid autoantigens, we established a Tg-specific T cell line by stimulation of peripheral blood mononuclear cells from a healthy volunteer with Tg and characterized its cytokine production pattern. The Tg-specific T cell line, designated DH5D1, obtained from a limiting dilution culture bore alpha beta T cell receptor and was CD4 and CD45RO positive. Upon stimulation with Tg, DH5D1 secreted little or no titers of IL-2, TNF-alpha, and IFN-gamma, whereas activation with combination of phorbol myristate acetate and calcium ionophore produced measurable levels of these cytokines. These results indicate that the Tg-specific T cell line is not defective in its capacity to produce proinflammatory cytokines and suggest that the inability of cytokine production by autoreactive T cells of healthy individuals is one fail-safe mechanism for preventing aggression of harmful autoimmune response.

Antigens↗
PubMed1994

[Chemical iodination of hormonogenic tyrosine residues of human thyroglobulin is critical for the production of anti-thyroglobulin autoantibody and for the induction of experimental autoimmune thyroiditis in mice].

There is evidence from animal models that the iodine content of thyroglobulin (Tg) may influence its antigenicity in thyroid autoimmunity. To elucidate the effect of iodination of hormonogenic sites of human Tg (hTg) on its autoantigenicity, a synthetic peptide (TB: hTg 2546-2571), containing two hormonogenic tyrosine residues of hTg, and a chemically-iodinated peptide (TB-I) were prepared. We immunized C3H/He (H-2k) mice, a high responder strain to Tg, and BALB/c (H-2d), a low responder strain, with TB or TB-I plus lipopolysaccharide. Lymph node cells from the two strains immunized with TB or TB-I proliferated in response to both TB and TB-I. Anti-Tg autoantibodies were detected in both strains when immunized with TB-I, while immunization with TB failed to produce anti-Tg antibodies. Furthermore, one of the C3H/He mice immunized with TB-I developed diffuse thyroiditis, but BALB/c mice did not. These findings indicate that the iodination of the hormonogenic tyrosine residues of hTg, in other words, the synthesis of mono- and di-iodotyrosine (MIT and DIT) residues, is necessary for the production of anti-Tg autoantibodies in high and low responder mice and for the induction of autoimmune thyroiditis in high responder mice.

Amino Acid Sequence↗
PubMed1994

[The clinical manifestations of Sjögren's syndrome in children].

Sjögren's syndrome (SS) is thought to be uncommon in children. We studied the clinical manifestations and laboratory findings of 12 pediatric patients with SS, all of children did not have sicca symptoms but have lymphocytic infiltration of salivary glands, abnormal sialograms or abnormal results of scintigraphy compatible with typical SS. Seven cases had primary SS and five were secondary SS and had other autoimmune disorders (three cases with systemic lupus erythematosus, one case with dermatomyositis, and the other with mixed connective tissue disease). All patients were female. The mean age at onset of symptoms, including other autoimmune manifestations, was 12.2 years (range 9-15 years). The initial symptoms were some systemic manifestations (fever, exanthema, arthralgia, etc.) and various autoimmune phenomena (butterfly rash, Raynaud's phenomenon, proteinuria, weakness of muscles, etc.). On the other hand, no patients complained sicca symptoms. Laboratory studies in our patients revealed elevated levels of IgG (92%), antinuclear antibody (92%), rheumatoid factor (58%), anti-SS-A antibody (75%). These findings were similar to those found in adult patients with sicca symptoms previously reported in literature. From these studies, we suggest that lip biopsy, sialography and/or salivary gland's scintigraphy should be carried out in patients who had abnormal laboratory findings as mentioned above, irrespective of absence of sicca symptoms, in order to diagnose SS at early period.

Adolescent↗
PubMed1994

Preferential recognition of primary protein structures of alpha-casein by IgG and IgE antibodies of patients with milk allergy.

We studied the binding activities of IgE and IgG antibodies in patients with allergy to cow milk proteins, against different alpha-casein preparations: alpha-casein treated with urea, hydrochloric acid, sodium hydroxide, or sodium dodecyl sulfate (SDS); or heat-denatured alpha-casein. The binding activities of IgE and IgG antibodies to these denatured alpha-casein preparations were compared with those to native alpha-casein. The binding activities of IgE and IgG antibodies to these denatured alpha-casein preparations were similar to those to native alpha-casein although the binding activities of IgG antibodies to these denatured alpha-casein preparations were relatively heterogeneous compared with those of IgE antibodies. Since modifications of alpha-casein did not alter the ability of alpha-casein to react with these antibodies, IgE and IgG antibodies to alpha-casein in sera from patients with allergy preferentially bind to the antigenic determinants associated with primary protein structures.

Allergens↗